메뉴 건너뛰기




Volumn 80, Issue 2, 2016, Pages 429-450

Assembly of lipoic acid on its cognate enzymes: An extraordinary and essential biosynthetic pathway

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOACID DEHYDROGENASE; 2 OXOISOVALERATE DEHYDROGENASE (LIPOAMIDE); ACETOIN DEHYDROGENASE; ACETYL COENZYME A; GLYCINE CLEAVAGE SYSTEM; LIPB PROTEIN; LIPM PROTEIN; MITOCHONDRIAL RNA; OXOGLUTARATE DEHYDROGENASE; PROTEIN; PYRUVATE DEHYDROGENASE; SMALL INTERFERING RNA; THIOCTIC ACID; TRANSFER RNA; TRICARBOXYLIC ACID; UNCLASSIFIED DRUG; CARRIER PROTEIN; MULTIENZYME COMPLEX; OXIDOREDUCTASE; TRANSFERASE;

EID: 84973443037     PISSN: 10922172     EISSN: 10985557     Source Type: Journal    
DOI: 10.1128/MMBR.00073-15     Document Type: Article
Times cited : (114)

References (164)
  • 1
    • 0031605517 scopus 로고    scopus 로고
    • From lipoic acid to multi-enzyme complexes
    • Reed LJ. 1998. From lipoic acid to multi-enzyme complexes. Protein Sci 7:220-224. http://dx.doi.org/10.1002/pro.5560070125.
    • (1998) Protein Sci , vol.7 , pp. 220-224
    • Reed, L.J.1
  • 2
    • 0035914303 scopus 로고    scopus 로고
    • A trail of research from lipoic acid to alpha-keto acid dehydrogenase complexes
    • Reed LJ. 2001. A trail of research from lipoic acid to alpha-keto acid dehydrogenase complexes. J Biol Chem 276:38329-38336. http://dx.doi.org/10.1074/jbc. R100026200.
    • (2001) J Biol Chem , vol.276 , pp. 38329-38336
    • Reed, L.J.1
  • 3
    • 0027034878 scopus 로고
    • Microorganisms in vitamin and biofactor research
    • Snell EE. 1992. Microorganisms in vitamin and biofactor research. J Nutr Sci Vitaminol (Tokyo) 38:34-39. http://dx.doi.org/10.3177/jnsv. 38. Special-34.
    • (1992) J Nutr Sci Vitaminol (Tokyo) , vol.38 , pp. 34-39
    • Snell, E.E.1
  • 4
    • 0027183415 scopus 로고
    • From bacterial nutrition to enzyme structure: A personal odyssey
    • Snell EE. 1993. From bacterial nutrition to enzyme structure: a personal odyssey. Annu Rev Biochem 62:1-27. http://dx.doi.org/10.1146/annurev. bi.62.070193.000245.
    • (1993) Annu Rev Biochem , vol.62 , pp. 1-27
    • Snell, E.E.1
  • 5
    • 0002654844 scopus 로고
    • Chemistry and function of lipoic acid, p 99-126
    • Florkin M, Stotz EH ed, Elsevier, New York, NY
    • Reed LJ. 1966. Chemistry and function of lipoic acid, p 99-126. In Florkin M, Stotz EH (ed), Comprehensive biochemistry, vol 14. Elsevier, New York, NY.
    • (1966) Comprehensive Biochemistry , vol.14
    • Reed, L.J.1
  • 6
    • 0004791238 scopus 로고
    • The chemistry and function of the pyruvate oxidation factor (lipoic acid)
    • Gunsalus IC. 1953. The chemistry and function of the pyruvate oxidation factor (lipoic acid). J Cell Physiol Suppl 41(Suppl 1):113-136.
    • (1953) J Cell Physiol Suppl , vol.41 , pp. 113-136
    • Gunsalus, I.C.1
  • 7
    • 0037684214 scopus 로고
    • Pyruvic acid metabolism. IV. Occurrence, properties, and partial purification of pyruvate oxidation factor
    • Gunsalus IC, Struglia L, O'Kane DJ. 1952. Pyruvic acid metabolism. IV. Occurrence, properties, and partial purification of pyruvate oxidation factor. J Biol Chem 194:859-869.
    • (1952) J Biol Chem , vol.194 , pp. 859-869
    • Gunsalus, I.C.1    Struglia, L.2    O'Kane, D.J.3
  • 8
    • 0002908647 scopus 로고
    • Crystalline alpha-lipoic acid; a catalytic agent associated with pyruvate dehydrogenase
    • Reed LJ, De BB, Gunsalus IC, Hornberger CS, Jr. 1951. Crystalline alpha-lipoic acid; a catalytic agent associated with pyruvate dehydrogenase. Science 114:93-94. http://dx.doi.org/10.1126/science.114.2952.93.
    • (1951) Science , vol.114 , pp. 93-94
    • Reed, L.J.1    De, B.B.2    Gunsalus, I.C.3    Hornberger, C.S.4
  • 9
    • 26844556483 scopus 로고
    • Croonian Lecture: Lethal synthesis
    • Peters RA. 1952. Croonian Lecture: lethal synthesis. Proc R Soc Lond B Biol Sci 139:143-170. http://dx.doi.org/10.1098/rspb.1952.0001.
    • (1952) Proc R Soc Lond B Biol Sci , vol.139 , pp. 143-170
    • Peters, R.A.1
  • 10
    • 77049164127 scopus 로고
    • Discussion: Biological activity of analogues and derivatives of thioctic acid
    • Stokstad ELR. 1954. Discussion: biological activity of analogues and derivatives of thioctic acid. Fed Proc 13:712-714.
    • (1954) Fed Proc , vol.13 , pp. 712-714
    • Stokstad, E.L.R.1
  • 11
    • 0007623841 scopus 로고
    • α-Keto acid dehydrogenation complexes. II. The role of protein-bound lipoic acid and flavin adenine dinucleotide
    • Koike M, Reed LJ. 1960. α-Keto acid dehydrogenation complexes. II. The role of protein-bound lipoic acid and flavin adenine dinucleotide. J Biol Chem 235:1931-1938.
    • (1960) J Biol Chem , vol.235 , pp. 1931-1938
    • Koike, M.1    Reed, L.J.2
  • 12
    • 84961044156 scopus 로고
    • Studies on a lipoic acid-activating system
    • Reed LJ, Leach FR, Koike M. 1958. Studies on a lipoic acid-activating system. J Biol Chem 232:123-142.
    • (1958) J Biol Chem , vol.232 , pp. 123-142
    • Reed, L.J.1    Leach, F.R.2    Koike, M.3
  • 13
    • 0001752523 scopus 로고
    • Studies on the nature and reactions of protein-bound lipoic acid
    • Reed LJ, Koike M, Levitch ME, Leach FR. 1958. Studies on the nature and reactions of protein-bound lipoic acid. J Biol Chem 232:143-158.
    • (1958) J Biol Chem , vol.232 , pp. 143-158
    • Reed, L.J.1    Koike, M.2    Levitch, M.E.3    Leach, F.R.4
  • 14
    • 0026079562 scopus 로고
    • Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: A paradigm in the design of a multifunctional protein
    • Perham RN. 1991. Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein. Biochemistry 30:8501-8512. http://dx.doi.org/10.1021/bi00099a001.
    • (1991) Biochemistry , vol.30 , pp. 8501-8512
    • Perham, R.N.1
  • 15
    • 0029027567 scopus 로고
    • Structure and posttranslational modification of lipoyl domain of 2-oxo-acid dehydrogenase multienzyme complexes
    • Perham RN. 1995. Structure and posttranslational modification of lipoyl domain of 2-oxo-acid dehydrogenase multienzyme complexes. Methods Enzymol 251:436-448. http://dx.doi.org/10.1016/0076-6879 (95) 51147-4.
    • (1995) Methods Enzymol , vol.251 , pp. 436-448
    • Perham, R.N.1
  • 16
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: Catalytic machines for multistep reactions
    • Perham RN. 2000. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu Rev Biochem 69:961-1004. http://dx.doi.org/10.1146/annurev. biochem.69.1.961.
    • (2000) Annu Rev Biochem , vol.69 , pp. 961-1004
    • Perham, R.N.1
  • 17
    • 0023726352 scopus 로고
    • Characterization and conservation of the inner E2 core domain structure of branched-chain alpha-keto acid dehydrogenase complex from bovine liver. Construction of a cDNA encoding the entire transacylase (E2b) precursor
    • Griffin TA, Lau KS, Chuang DT. 1988. Characterization and conservation of the inner E2 core domain structure of branched-chain alpha-keto acid dehydrogenase complex from bovine liver. Construction of a cDNA encoding the entire transacylase (E2b) precursor. J Biol Chem 263:14008-14014.
    • (1988) J Biol Chem , vol.263 , pp. 14008-14014
    • Griffin, T.A.1    Lau, K.S.2    Chuang, D.T.3
  • 18
    • 0024459807 scopus 로고
    • Branched-chain alpha-keto acid dehydrogenase complex from bovine kidney: Radial distribution of mass determined from darkfield electron micrographs
    • Hackert ML, Xu WX, Oliver RM, Wall JS, Hainfeld JF, Mullinax TR, Reed LJ. 1989. Branched-chain alpha-keto acid dehydrogenase complex from bovine kidney: radial distribution of mass determined from darkfield electron micrographs. Biochemistry 28:6816-6821. http://dx.doi.org/10.1021/bi00443a006.
    • (1989) Biochemistry , vol.28 , pp. 6816-6821
    • Hackert, M.L.1    Xu, W.X.2    Oliver, R.M.3    Wall, J.S.4    Hainfeld, J.F.5    Mullinax, T.R.6    Reed, L.J.7
  • 19
    • 0035212268 scopus 로고    scopus 로고
    • The glycine decarboxylase system: A fascinating complex
    • Douce R, Bourguignon J, Neuburger M, Rebeille F. 2001. The glycine decarboxylase system: a fascinating complex. Trends Plant Sci 6:167-176. http://dx.doi.org/10.1016/S1360-1385 (01) 01892-1.
    • (2001) Trends Plant Sci , vol.6 , pp. 167-176
    • Douce, R.1    Bourguignon, J.2    Neuburger, M.3    Rebeille, F.4
  • 20
    • 48649091869 scopus 로고    scopus 로고
    • Glycine cleavage system: Reaction mechanism, physiological significance, and hyperglycinemia
    • Kikuchi G, Motokawa Y, Yoshida T, Hiraga K. 2008. Glycine cleavage system: reaction mechanism, physiological significance, and hyperglycinemia. Proc Jpn Acad Ser B Phys Biol Sci 84:246-263. http://dx.doi.org/10.2183/pjab.84.246.
    • (2008) Proc Jpn Acad Ser B Phys Biol Sci , vol.84 , pp. 246-263
    • Kikuchi, G.1    Motokawa, Y.2    Yoshida, T.3    Hiraga, K.4
  • 21
    • 0030022535 scopus 로고    scopus 로고
    • Glycine decarboxylase and pyruvate dehydrogenase complexes share the same dihydrolipoamide dehydrogenase in pea leaf mitochondria: Evidence from mass spectrometry and primary-structure analysis
    • Bourguignon J, Merand V, Rawsthorne S, Forest E, Douce R. 1996. Glycine decarboxylase and pyruvate dehydrogenase complexes share the same dihydrolipoamide dehydrogenase in pea leaf mitochondria: evidence from mass spectrometry and primary-structure analysis. Biochem J 313:229-234. http://dx.doi.org/10.1042/bj3130229.
    • (1996) Biochem J , vol.313 , pp. 229-234
    • Bourguignon, J.1    Merand, V.2    Rawsthorne, S.3    Forest, E.4    Douce, R.5
  • 22
    • 0025180164 scopus 로고
    • The lpd gene product functions as the L protein in the Escherichia coli glycine cleavage enzyme system
    • Steiert PS, Stauffer LT, Stauffer GV. 1990. The lpd gene product functions as the L protein in the Escherichia coli glycine cleavage enzyme system. J Bacteriol 172:6142-6144.
    • (1990) J Bacteriol , vol.172 , pp. 6142-6144
    • Steiert, P.S.1    Stauffer, L.T.2    Stauffer, G.V.3
  • 23
    • 0031431663 scopus 로고    scopus 로고
    • Lipoylation of acyltransferase components of 2-oxo acid dehydrogenase complexes
    • Quinn J. 1997. Lipoylation of acyltransferase components of 2-oxo acid dehydrogenase complexes. Methods Enzymol 279:193-202. http://dx.doi.org/10.1016/S0076-6879 (97) 79023-2.
    • (1997) Methods Enzymol , vol.279 , pp. 193-202
    • Quinn, J.1
  • 24
    • 0029915259 scopus 로고    scopus 로고
    • Expression, lipoylation and structure determination of recombinant pea H-protein in Escherichia coli
    • Macherel D, Bourguignon J, Forest E, Faure M, Cohen-Addad C, Douce R. 1996. Expression, lipoylation and structure determination of recombinant pea H-protein in Escherichia coli. Eur J Biochem 236:27-33. http://dx.doi.org/10.1111/j.1432-1033.1996.00027.x.
    • (1996) Eur J Biochem , vol.236 , pp. 27-33
    • Macherel, D.1    Bourguignon, J.2    Forest, E.3    Faure, M.4    Cohen-Addad, C.5    Douce, R.6
  • 25
    • 0024560461 scopus 로고
    • Kinetics and specificity of reductive acylation of lipoyl domains from 2-oxo acid dehydrogenase multienzyme complexes
    • Graham LD, Packman LC, Perham RN. 1989. Kinetics and specificity of reductive acylation of lipoyl domains from 2-oxo acid dehydrogenase multienzyme complexes. Biochemistry 28:1574-1581. http://dx.doi.org/10.1021/bi00430a023.
    • (1989) Biochemistry , vol.28 , pp. 1574-1581
    • Graham, L.D.1    Packman, L.C.2    Perham, R.N.3
  • 26
    • 0023813683 scopus 로고
    • Investigation of the mechanism of active site coupling in the pyruvate dehydrogenase multienzyme complex of Escherichia coli by protein engineering
    • Miles JS, Guest JR, Radford SE, Perham RN. 1988. Investigation of the mechanism of active site coupling in the pyruvate dehydrogenase multienzyme complex of Escherichia coli by protein engineering. J Mol Biol 202:97-106. http://dx.doi.org/10.1016/0022-2836 (88) 90522-0.
    • (1988) J Mol Biol , vol.202 , pp. 97-106
    • Miles, J.S.1    Guest, J.R.2    Radford, S.E.3    Perham, R.N.4
  • 27
    • 0031053675 scopus 로고    scopus 로고
    • Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii
    • Berg A, Vervoort J, De Kok A. 1997. Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Eur J Biochem 244:352-360. http://dx.doi.org/10.1111/j.1432-1033.1997.00352.x.
    • (1997) Eur J Biochem , vol.244 , pp. 352-360
    • Berg, A.1    Vervoort, J.2    De Kok, A.3
  • 28
    • 0032519817 scopus 로고    scopus 로고
    • Kinetics and specificity of reductive acylation of wild-type and mutated lipoyl domains of 2-oxo-acid dehydrogenase complexes from Azotobacter vinelandii
    • Berg A, Westphal AH, Bosma HJ, De Kok A. 1998. Kinetics and specificity of reductive acylation of wild-type and mutated lipoyl domains of 2-oxo-acid dehydrogenase complexes from Azotobacter vinelandii. Eur J Biochem 252:45-50. http://dx.doi.org/10.1046/j.1432-1327.1998.2520045.x.
    • (1998) Eur J Biochem , vol.252 , pp. 45-50
    • Berg, A.1    Westphal, A.H.2    Bosma, H.J.3    De Kok, A.4
  • 29
    • 0034713840 scopus 로고    scopus 로고
    • Restricted motion of the lipoyl-lysine swinging arm in the pyruvate dehydrogenase complex of Escherichia coli
    • Jones DD, Stott KM, Howard MJ, Perham RN. 2000. Restricted motion of the lipoyl-lysine swinging arm in the pyruvate dehydrogenase complex of Escherichia coli. Biochemistry 39:8448-8459. http://dx.doi.org/10.1021/bi992978i.
    • (2000) Biochemistry , vol.39 , pp. 8448-8459
    • Jones, D.D.1    Stott, K.M.2    Howard, M.J.3    Perham, R.N.4
  • 30
    • 0032813519 scopus 로고    scopus 로고
    • Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes
    • Aevarsson A, Seger K, Turley S, Sokatch JR, Hol WG. 1999. Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat Struct Biol 6:785-792. http://dx.doi.org/10.1038/11563.
    • (1999) Nat Struct Biol , vol.6 , pp. 785-792
    • Aevarsson, A.1    Seger, K.2    Turley, S.3    Sokatch, J.R.4    Hol, W.G.5
  • 31
    • 0030298405 scopus 로고    scopus 로고
    • Recognition of a surface loop of the lipoyl domain underlies substrate channelling in the pyruvate dehydrogenase multienzyme complex
    • Wallis NG, Allen MD, Broadhurst RW, Lessard IA, Perham RN. 1996. Recognition of a surface loop of the lipoyl domain underlies substrate channelling in the pyruvate dehydrogenase multienzyme complex. J Mol Biol 263:463-474. http://dx.doi.org/10.1006/jmbi.1996.0589.
    • (1996) J Mol Biol , vol.263 , pp. 463-474
    • Wallis, N.G.1    Allen, M.D.2    Broadhurst, R.W.3    Lessard, I.A.4    Perham, R.N.5
  • 32
    • 0028221946 scopus 로고
    • Structural dependence of posttranslational modification and reductive acetylation of the lipoyl domain of the pyruvate dehydrogenase multienzyme complex
    • Wallis NG, Perham RN. 1994. Structural dependence of posttranslational modification and reductive acetylation of the lipoyl domain of the pyruvate dehydrogenase multienzyme complex. J Mol Biol 236:209-216. http://dx.doi.org/10.1006/jmbi.1994.1130.
    • (1994) J Mol Biol , vol.236 , pp. 209-216
    • Wallis, N.G.1    Perham, R.N.2
  • 33
    • 0028940085 scopus 로고
    • The lipoamide arm in the glycine decarboxylase complex is not freely swinging
    • Cohen-Addad C, Pares S, Sieker L, Neuburger M, Douce R. 1995. The lipoamide arm in the glycine decarboxylase complex is not freely swinging. Nat Struct Biol 2:63-68. http://dx.doi.org/10.1038/nsb0195-63.
    • (1995) Nat Struct Biol , vol.2 , pp. 63-68
    • Cohen-Addad, C.1    Pares, S.2    Sieker, L.3    Neuburger, M.4    Douce, R.5
  • 34
    • 0027340272 scopus 로고
    • Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex
    • Dardel F, Davis AL, Laue ED, Perham RN. 1993. Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex. J Mol Biol 229:1037-1048. http://dx.doi.org/10.1006/jmbi.1993.1103.
    • (1993) J Mol Biol , vol.229 , pp. 1037-1048
    • Dardel, F.1    Davis, A.L.2    Laue, E.D.3    Perham, R.N.4
  • 35
    • 0027466730 scopus 로고
    • Prediction of the three-dimensional structures of the biotinylated domain from yeast pyruvate carboxylase and of the lipoylated H-protein from the pea leaf glycine cleavage system: A new automated method for the prediction of protein tertiary structure
    • Brocklehurst SM, Perham RN. 1993. Prediction of the three-dimensional structures of the biotinylated domain from yeast pyruvate carboxylase and of the lipoylated H-protein from the pea leaf glycine cleavage system: a new automated method for the prediction of protein tertiary structure. Protein Sci 2:626-639.
    • (1993) Protein Sci , vol.2 , pp. 626-639
    • Brocklehurst, S.M.1    Perham, R.N.2
  • 36
    • 0027975343 scopus 로고
    • X-ray structure determination at 2.6-A resolution of a lipoate-containing protein: The H-protein of the glycine decarboxylase complex from pea leaves
    • Pares S, Cohen-Addad C, Sieker L, Neuburger M, Douce R. 1994. X-ray structure determination at 2.6-A resolution of a lipoate-containing protein: the H-protein of the glycine decarboxylase complex from pea leaves. Proc Natl Acad Sci U S A 91:4850-4853. http://dx.doi.org/10.1073/pnas.91.11.4850.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 4850-4853
    • Pares, S.1    Cohen-Addad, C.2    Sieker, L.3    Neuburger, M.4    Douce, R.5
  • 37
    • 0035813096 scopus 로고    scopus 로고
    • The biotinyl domain of Escherichia coli acetyl-CoA carboxylase. Evidence that the "thumb" structure is essential and that the domain functions as a dimer
    • Cronan JE, Jr. 2001. The biotinyl domain of Escherichia coli acetyl-CoA carboxylase. Evidence that the "thumb" structure is essential and that the domain functions as a dimer. J Biol Chem 276:37355-37364.
    • (2001) J Biol Chem , vol.276 , pp. 37355-37364
    • Cronan, J.E.1
  • 38
    • 0029646091 scopus 로고
    • Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing
    • Athappilly FK, Hendrickson WA. 1995. Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure 3:1407-1419. http://dx.doi.org/10.1016/S0969-2126 (01) 00277-5.
    • (1995) Structure , vol.3 , pp. 1407-1419
    • Athappilly, F.K.1    Hendrickson, W.A.2
  • 39
    • 0033586767 scopus 로고    scopus 로고
    • Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy
    • Roberts EL, Shu N, Howard MJ, Broadhurst RW, Chapman-Smith A, Wallace JC, Morris T, Cronan JE, Jr, Perham RN. 1999. Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy. Biochemistry 38:5045-5053. http://dx.doi.org/10.1021/bi982466o.
    • (1999) Biochemistry , vol.38 , pp. 5045-5053
    • Roberts, E.L.1    Shu, N.2    Howard, M.J.3    Broadhurst, R.W.4    Chapman-Smith, A.5    Wallace, J.C.6    Morris, T.7    Cronan, J.E.8    Perham, R.N.9
  • 40
    • 0030668421 scopus 로고    scopus 로고
    • Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase
    • Yao X, Wei D, Soden C, Jr, Summers MF, Beckett D. 1997. Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase. Biochemistry 36:15089-15100. http://dx.doi.org/10.1021/bi971485f.
    • (1997) Biochemistry , vol.36 , pp. 15089-15100
    • Yao, X.1    Wei, D.2    Soden, C.3    Summers, M.F.4    Beckett, D.5
  • 41
    • 0000041171 scopus 로고    scopus 로고
    • High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii
    • Reddy DV, Shenoy BC, Carey PR, Sonnichsen FD. 2000. High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii. Biochemistry 39:2509-2516. http://dx.doi.org/10.1021/bi9925367.
    • (2000) Biochemistry , vol.39 , pp. 2509-2516
    • Reddy, D.V.1    Shenoy, B.C.2    Carey, P.R.3    Sonnichsen, F.D.4
  • 42
    • 0037151041 scopus 로고    scopus 로고
    • Interchangeable enzyme modules. Functional replacement of the essential linker of the biotinylated subunit of acetyl-CoA carboxylase with a linker from the lipoylated subunit of pyruvate dehydrogenase
    • Cronan JE, Jr. 2002. Interchangeable enzyme modules. Functional replacement of the essential linker of the biotinylated subunit of acetyl-CoA carboxylase with a linker from the lipoylated subunit of pyruvate dehydrogenase. J Biol Chem 277:22520-22527.
    • (2002) J Biol Chem , vol.277 , pp. 22520-22527
    • Cronan, J.E.1
  • 43
    • 0029148130 scopus 로고
    • Purification and properties of the lipoate protein ligase of Escherichia coli
    • Green DE, Morris TW, Green J, Cronan JE, Jr, Guest JR. 1995. Purification and properties of the lipoate protein ligase of Escherichia coli. Biochem J 309:853-862. http://dx.doi.org/10.1042/bj3090853.
    • (1995) Biochem J , vol.309 , pp. 853-862
    • Green, D.E.1    Morris, T.W.2    Green, J.3    Cronan, J.E.4    Guest, J.R.5
  • 44
    • 0028247161 scopus 로고
    • Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product
    • Morris TW, Reed KE, Cronan JE, Jr. 1994. Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product. J Biol Chem 269:16091-16100.
    • (1994) J Biol Chem , vol.269 , pp. 16091-16100
    • Morris, T.W.1    Reed, K.E.2    Cronan, J.E.3
  • 45
    • 0028331916 scopus 로고
    • Mutants of Escherichia coli K-12 that are resistant to a selenium analog of lipoic acid identify unknown genes in lipoate metabolism
    • Reed KE, Morris TW, Cronan JE, Jr. 1994. Mutants of Escherichia coli K-12 that are resistant to a selenium analog of lipoic acid identify unknown genes in lipoate metabolism. Proc Natl Acad Sci U S A 91:3720-3724. http://dx.doi.org/10.1073/pnas.91.9.3720.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3720-3724
    • Reed, K.E.1    Morris, T.W.2    Cronan, J.E.3
  • 46
    • 0343119106 scopus 로고
    • Turbidimetric and polarographic assays for lipoic acid using mutants of Escherichia coli
    • Herbert AA, Guest JR. 1970. Turbidimetric and polarographic assays for lipoic acid using mutants of Escherichia coli. Methods Enzymol 18(Pt A):269-272. http://dx.doi.org/10.1016/0076-6879 (71) 18314-0.
    • (1970) Methods Enzymol , vol.18 , pp. 269-272
    • Herbert, A.A.1    Guest, J.R.2
  • 47
    • 0026873622 scopus 로고
    • Incorporation of the enantiomers of lipoic acid into the pyruvate dehydrogenase complex from Escherichia coli in vivo
    • Oehring R, Bisswanger H. 1992. Incorporation of the enantiomers of lipoic acid into the pyruvate dehydrogenase complex from Escherichia coli in vivo. Biol Chem Hoppe Seyler 373:333-335. http://dx.doi.org/10.1515/bchm3.1992.373.1.333.
    • (1992) Biol Chem Hoppe Seyler , vol.373 , pp. 333-335
    • Oehring, R.1    Bisswanger, H.2
  • 48
    • 54749129835 scopus 로고    scopus 로고
    • An engineered aryl azide ligase for site-specific mapping of protein-protein interactions through photo-cross-linking
    • Baruah H, Puthenveetil S, Choi YA, Shah S, Ting AY. 2008. An engineered aryl azide ligase for site-specific mapping of protein-protein interactions through photo-cross-linking. Angew Chem Int Ed Engl 47:7018-7021. http://dx.doi.org/10.1002/anie.200802088.
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 7018-7021
    • Baruah, H.1    Puthenveetil, S.2    Choi, Y.A.3    Shah, S.4    Ting, A.Y.5
  • 49
    • 84859626359 scopus 로고    scopus 로고
    • Site-specific protein modification using lipoic acid ligase and bis-aryl hydrazone formation
    • Cohen JD, Zou P, Ting AY. 2012. Site-specific protein modification using lipoic acid ligase and bis-aryl hydrazone formation. Chembiochem 13:888-894. http://dx.doi.org/10.1002/cbic.201100764.
    • (2012) Chembiochem , vol.13 , pp. 888-894
    • Cohen, J.D.1    Zou, P.2    Ting, A.Y.3
  • 51
    • 76649096993 scopus 로고    scopus 로고
    • Characterization of corrosive bacterial consortia isolated from petroleumproduct-transporting pipelines
    • Rajasekar A, Anandkumar B, Maruthamuthu S, Ting YP, Rahman PK. 2010. Characterization of corrosive bacterial consortia isolated from petroleumproduct-transporting pipelines. Appl Microbiol Biotechnol 85:1175-1188. http://dx.doi.org/10.1007/s00253-009-2289-9.
    • (2010) Appl Microbiol Biotechnol , vol.85 , pp. 1175-1188
    • Rajasekar, A.1    Anandkumar, B.2    Maruthamuthu, S.3    Ting, Y.P.4    Rahman, P.K.5
  • 53
    • 25844453475 scopus 로고    scopus 로고
    • Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site
    • Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, Taniguchi H. 2005. Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site. J Biol Chem 280:33645-33651.
    • (2005) J Biol Chem , vol.280 , pp. 33645-33651
    • Fujiwara, K.1    Toma, S.2    Okamura-Ikeda, K.3    Motokawa, Y.4    Nakagawa, A.5    Taniguchi, H.6
  • 54
    • 0033769643 scopus 로고    scopus 로고
    • Lipoylating and biotinylating enzymes contain a homologous catalytic module
    • Reche PA. 2000. Lipoylating and biotinylating enzymes contain a homologous catalytic module. Protein Sci 9:1922-1929. http://dx.doi.org/10.1110/ps.9.10.1922.
    • (2000) Protein Sci , vol.9 , pp. 1922-1929
    • Reche, P.A.1
  • 55
    • 31344446409 scopus 로고    scopus 로고
    • Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification
    • McManus E, Luisi BF, Perham RN. 2006. Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification. J Mol Biol 356:625-637. http://dx.doi.org/10.1016/j.jmb.2005.11.057.
    • (2006) J Mol Biol , vol.356 , pp. 625-637
    • McManus, E.1    Luisi, B.F.2    Perham, R.N.3
  • 56
    • 27844503528 scopus 로고    scopus 로고
    • Crystal structure of lipoate-protein ligase A bound with the activated intermediate: Insights into interaction with lipoyl domains
    • Kim DJ, Kim KH, Lee HH, Lee SJ, Ha JY, Yoon HJ, Suh SW. 2005. Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains. J Biol Chem 280:38081-38089. http://dx.doi.org/10.1074/jbc. M507284200.
    • (2005) J Biol Chem , vol.280 , pp. 38081-38089
    • Kim, D.J.1    Kim, K.H.2    Lee, H.H.3    Lee, S.J.4    Ha, J.Y.5    Yoon, H.J.6    Suh, S.W.7
  • 57
    • 69249127867 scopus 로고    scopus 로고
    • The Thermoplasma acidophilum LplA-LplB complex defines a new class of bipartite lipoate-protein ligases
    • Christensen QH, Cronan JE. 2009. The Thermoplasma acidophilum LplA-LplB complex defines a new class of bipartite lipoate-protein ligases. J Biol Chem 284:21317-21326. http://dx.doi.org/10.1074/jbc. M109.015016.
    • (2009) J Biol Chem , vol.284 , pp. 21317-21326
    • Christensen, Q.H.1    Cronan, J.E.2
  • 58
    • 68149164450 scopus 로고    scopus 로고
    • A unique lipoylation system in the Archaea. Lipoylation in Thermoplasma acidophilum requires two proteins
    • Posner MG, Upadhyay A, Bagby S, Hough DW, Danson MJ. 2009. A unique lipoylation system in the Archaea. Lipoylation in Thermoplasma acidophilum requires two proteins. FEBS J 276:4012-4022. http://dx.doi.org/10.1111/j.1742-4658.2009.07110.x.
    • (2009) FEBS J , vol.276 , pp. 4012-4022
    • Posner, M.G.1    Upadhyay, A.2    Bagby, S.3    Hough, D.W.4    Danson, M.J.5
  • 59
    • 84871436925 scopus 로고    scopus 로고
    • Post-translational modification in the archaea: Structural characterization of multi-enzyme complex lipoylation
    • Posner MG, Upadhyay A, Crennell SJ, Watson AJ, Dorus S, Danson MJ, Bagby S. 2013. Post-translational modification in the archaea: structural characterization of multi-enzyme complex lipoylation. Biochem J 449:415-425. http://dx.doi.org/10.1042/BJ20121150.
    • (2013) Biochem J , vol.449 , pp. 415-425
    • Posner, M.G.1    Upadhyay, A.2    Crennell, S.J.3    Watson, A.J.4    Dorus, S.5    Danson, M.J.6    Bagby, S.7
  • 60
    • 84924898047 scopus 로고    scopus 로고
    • The Streptomyces coelicolor lipoate-protein ligase is a circularly permuted version of the Escherichia coli enzyme composed of discrete interacting domains
    • Cao X, Cronan JE. 2015. The Streptomyces coelicolor lipoate-protein ligase is a circularly permuted version of the Escherichia coli enzyme composed of discrete interacting domains. J Biol Chem 290:7280-7290. http://dx.doi.org/10.1074/jbc. M114.626879.
    • (2015) J Biol Chem , vol.290 , pp. 7280-7290
    • Cao, X.1    Cronan, J.E.2
  • 61
    • 33344466006 scopus 로고    scopus 로고
    • Co-repressor induced order and biotin repressor dimerization: A case for divergent followed by convergent evolution
    • Wood ZA, Weaver LH, Brown PH, Beckett D, Matthews BW. 2006. Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution. J Mol Biol 357:509-523. http://dx.doi.org/10.1016/j.jmb.2005.12.066.
    • (2006) J Mol Biol , vol.357 , pp. 509-523
    • Wood, Z.A.1    Weaver, L.H.2    Brown, P.H.3    Beckett, D.4    Matthews, B.W.5
  • 62
    • 0028244665 scopus 로고
    • Purification and characterization of lipoyl-AMP:N epsilon-lysine lipoyltransferase from bovine liver mitochondria
    • Fujiwara K, Okamura-Ikeda K, Motokawa Y. 1994. Purification and characterization of lipoyl-AMP:N epsilon-lysine lipoyltransferase from bovine liver mitochondria. J Biol Chem 269:16605-16609.
    • (1994) J Biol Chem , vol.269 , pp. 16605-16609
    • Fujiwara, K.1    Okamura-Ikeda, K.2    Motokawa, Y.3
  • 63
    • 77951221077 scopus 로고    scopus 로고
    • Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A
    • Fujiwara K, Maita N, Hosaka H, Okamura-Ikeda K, Nakagawa A, Taniguchi H. 2010. Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A. J Biol Chem 285:9971-9980. http://dx.doi.org/10.1074/jbc. M109.078717.
    • (2010) J Biol Chem , vol.285 , pp. 9971-9980
    • Fujiwara, K.1    Maita, N.2    Hosaka, H.3    Okamura-Ikeda, K.4    Nakagawa, A.5    Taniguchi, H.6
  • 65
    • 0035800735 scopus 로고    scopus 로고
    • Purification, characterization, and cDNA cloning of lipoate-activating enzyme from bovine liver
    • Fujiwara K, Takeuchi S, Okamura-Ikeda K, Motokawa Y. 2001. Purification, characterization, and cDNA cloning of lipoate-activating enzyme from bovine liver. J Biol Chem 276:28819-28823. http://dx.doi.org/10.1074/jbc. M101748200.
    • (2001) J Biol Chem , vol.276 , pp. 28819-28823
    • Fujiwara, K.1    Takeuchi, S.2    Okamura-Ikeda, K.3    Motokawa, Y.4
  • 66
    • 0035929654 scopus 로고    scopus 로고
    • Molecular identification and characterization of two medium-chain acyl-CoA synthetases, MACS1 and the Sa gene product
    • Fujino T, Takei YA, Sone H, Ioka RX, Kamataki A, Magoori K, Takahashi S, Sakai J, Yamamoto TT. 2001. Molecular identification and characterization of two medium-chain acyl-CoA synthetases, MACS1 and the Sa gene product. J Biol Chem 276:35961-35966. http://dx.doi.org/10.1074/jbc. M106651200.
    • (2001) J Biol Chem , vol.276 , pp. 35961-35966
    • Fujino, T.1    Takei, Y.A.2    Sone, H.3    Ioka, R.X.4    Kamataki, A.5    Magoori, K.6    Takahashi, S.7    Sakai, J.8    Yamamoto, T.T.9
  • 67
    • 0037247845 scopus 로고    scopus 로고
    • Isolation, sequencing, and expression of a cDNA for the HXM-A form of xenobiotic/mediumchain fatty acid:CoA ligase from human liver mitochondria
    • Vessey DA, Lau E, Kelley M, Warren RS. 2003. Isolation, sequencing, and expression of a cDNA for the HXM-A form of xenobiotic/mediumchain fatty acid:CoA ligase from human liver mitochondria. J Biochem Mol Toxicol 17:1-6. http://dx.doi.org/10.1002/jbt.10056.
    • (2003) J Biochem Mol Toxicol , vol.17 , pp. 1-6
    • Vessey, D.A.1    Lau, E.2    Kelley, M.3    Warren, R.S.4
  • 70
    • 0028821293 scopus 로고
    • Lipoic acid metabolism in Escherichia coli: The lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein
    • Morris TW, Reed KE, Cronan JE, Jr. 1995. Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein. J Bacteriol 177:1-10.
    • (1995) J Bacteriol , vol.177 , pp. 1-10
    • Morris, T.W.1    Reed, K.E.2    Cronan, J.E.3
  • 71
    • 0026018074 scopus 로고
    • Lipoic acid metabolism in Escherichia coli: Isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. Coli lip locus, and identification of the lipoylated protein of the glycine cleavage system
    • Vanden Boom TJ, Reed KE, Cronan JE, Jr. 1991. Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system. J Bacteriol 173:6411-6420.
    • (1991) J Bacteriol , vol.173 , pp. 6411-6420
    • Vanden Boom, T.J.1    Reed, K.E.2    Cronan, J.E.3
  • 72
    • 0030747906 scopus 로고    scopus 로고
    • A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria
    • Jordan SW, Cronan JE, Jr. 1997. A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. J Biol Chem 272:17903-17906.
    • (1997) J Biol Chem , vol.272 , pp. 17903-17906
    • Jordan, S.W.1    Cronan, J.E.2
  • 73
    • 0037371576 scopus 로고    scopus 로고
    • The Escherichia coli lipB gene encodes lipoyl (octanoyl)-acyl carrier protein: Protein transferase
    • Jordan SW, Cronan JE, Jr. 2003. The Escherichia coli lipB gene encodes lipoyl (octanoyl)-acyl carrier protein: protein transferase. J Bacteriol 185:1582-1589. http://dx.doi.org/10.1128/JB.185.5.1582-1589.2003.
    • (2003) J Bacteriol , vol.185 , pp. 1582-1589
    • Jordan, S.W.1    Cronan, J.E.2
  • 74
    • 0031418198 scopus 로고    scopus 로고
    • Biosynthesis of lipoic acid and posttranslational modification with lipoic acid in Escherichia coli
    • Jordan SW, Cronan JE, Jr. 1997. Biosynthesis of lipoic acid and posttranslational modification with lipoic acid in Escherichia coli. Methods Enzymol 279:176-183. http://dx.doi.org/10.1016/S0076-6879 (97) 79021-9.
    • (1997) Methods Enzymol , vol.279 , pp. 176-183
    • Jordan, S.W.1    Cronan, J.E.2
  • 75
    • 79953157667 scopus 로고    scopus 로고
    • Protein-protein interactions in assembly of lipoic acid on the 2-oxoacid dehydrogenases of aerobic metabolism
    • Hassan BH, Cronan JE. 2011. Protein-protein interactions in assembly of lipoic acid on the 2-oxoacid dehydrogenases of aerobic metabolism. J Biol Chem 286:8263-8276. http://dx.doi.org/10.1074/jbc. M110.194191.
    • (2011) J Biol Chem , vol.286 , pp. 8263-8276
    • Hassan, B.H.1    Cronan, J.E.2
  • 77
    • 0348229020 scopus 로고    scopus 로고
    • Assembly of the covalent linkage between lipoic acid and its cognate enzymes
    • Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE. 2003. Assembly of the covalent linkage between lipoic acid and its cognate enzymes. Chem Biol 10:1293-1302. http://dx.doi.org/10.1016/j.chembiol.2003.11.016.
    • (2003) Chem Biol , vol.10 , pp. 1293-1302
    • Zhao, X.1    Miller, J.R.2    Jiang, Y.3    Marletta, M.A.4    Cronan, J.E.5
  • 78
    • 0027401765 scopus 로고
    • Lipoic acid metabolism in Escherichia coli: Sequencing and functional characterization of the lipA and lipB genes
    • Reed KE, Cronan JE, Jr. 1993. Lipoic acid metabolism in Escherichia coli: sequencing and functional characterization of the lipA and lipB genes. J Bacteriol 175:1325-1336.
    • (1993) J Bacteriol , vol.175 , pp. 1325-1336
    • Reed, K.E.1    Cronan, J.E.2
  • 79
    • 0016800742 scopus 로고
    • Lipoic acid content of Escherichia coli and other microorganisms
    • Herbert AA, Guest JR. 1975. Lipoic acid content of Escherichia coli and other microorganisms. Arch Microbiol 106:259-266. http://dx.doi.org/10.1007/BF00446532.
    • (1975) Arch Microbiol , vol.106 , pp. 259-266
    • Herbert, A.A.1    Guest, J.R.2
  • 80
    • 0014344705 scopus 로고
    • Biochemical and genetic studies with lysine+methionine mutants of Escherichia coli: Lipoic acid and alphaketoglutarate dehydrogenase-less mutants
    • Herbert AA, Guest JR. 1968. Biochemical and genetic studies with lysine+methionine mutants of Escherichia coli: lipoic acid and alphaketoglutarate dehydrogenase-less mutants. J Gen Microbiol 53:363-381. http://dx.doi.org/10.1099/00221287-53-3-363.
    • (1968) J Gen Microbiol , vol.53 , pp. 363-381
    • Herbert, A.A.1    Guest, J.R.2
  • 81
    • 70350436283 scopus 로고    scopus 로고
    • Scavenging of cytosolic octanoic acid by mutant LplA lipoate ligases allows growth of Escherichia coli strains lacking the LipB octanoyltransferase of lipoic acid synthesis
    • Hermes FA, Cronan JE. 2009. Scavenging of cytosolic octanoic acid by mutant LplA lipoate ligases allows growth of Escherichia coli strains lacking the LipB octanoyltransferase of lipoic acid synthesis. J Bacteriol 191:6796-6803. http://dx.doi.org/10.1128/JB.00798-09.
    • (2009) J Bacteriol , vol.191 , pp. 6796-6803
    • Hermes, F.A.1    Cronan, J.E.2
  • 82
    • 0025095918 scopus 로고
    • Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli
    • Ali ST, Guest JR. 1990. Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli. Biochem J 271:139-145. http://dx.doi.org/10.1042/bj2710139.
    • (1990) Biochem J , vol.271 , pp. 139-145
    • Ali, S.T.1    Guest, J.R.2
  • 83
    • 0025323632 scopus 로고
    • Octanoylation of the lipoyl domains of the pyruvate dehydrogenase complex in a lipoyldeficient strain of Escherichia coli
    • Ali ST, Moir AJ, Ashton PR, Engel PC, Guest JR. 1990. Octanoylation of the lipoyl domains of the pyruvate dehydrogenase complex in a lipoyldeficient strain of Escherichia coli. Mol Microbiol 4:943-950. http://dx.doi.org/10.1111/j.1365-2958.1990.tb00667.x.
    • (1990) Mol Microbiol , vol.4 , pp. 943-950
    • Ali, S.T.1    Moir, A.J.2    Ashton, P.R.3    Engel, P.C.4    Guest, J.R.5
  • 84
    • 29244461444 scopus 로고    scopus 로고
    • The reaction of LipB, the octanoyl-[acyl carrier protein]: Protein N-octanoyltransferase of lipoic acid synthesis, proceeds through an acyl-enzyme intermediate
    • Zhao X, Miller JR, Cronan JE. 2005. The reaction of LipB, the octanoyl-[acyl carrier protein]:protein N-octanoyltransferase of lipoic acid synthesis, proceeds through an acyl-enzyme intermediate. Biochemistry 44:16737-16746. http://dx.doi.org/10.1021/bi051865y.
    • (2005) Biochemistry , vol.44 , pp. 16737-16746
    • Zhao, X.1    Miller, J.R.2    Cronan, J.E.3
  • 86
    • 39749136116 scopus 로고    scopus 로고
    • Structural basis of octanoic acid recognition by lipoate-protein ligase B
    • Kim Do J, Lee SJ, Kim HS, Kim KH, Lee HH, Yoon HJ, Suh SW. 2008. Structural basis of octanoic acid recognition by lipoate-protein ligase B. Proteins 70:1620-1625. http://dx.doi.org/10.1002/prot.21843.
    • (2008) Proteins , vol.70 , pp. 1620-1625
    • Kim Do, J.1    Lee, S.J.2    Kim, H.S.3    Kim, K.H.4    Lee, H.H.5    Yoon, H.J.6    Suh, S.W.7
  • 87
    • 78649299811 scopus 로고    scopus 로고
    • Lipoic acid synthesis: A new family of octanoyltransferases generally annotated as lipoate protein ligases
    • Christensen QH, Cronan JE. 2010. Lipoic acid synthesis: a new family of octanoyltransferases generally annotated as lipoate protein ligases. Biochemistry 49:10024-10036. http://dx.doi.org/10.1021/bi101215f.
    • (2010) Biochemistry , vol.49 , pp. 10024-10036
    • Christensen, Q.H.1    Cronan, J.E.2
  • 88
    • 0027983037 scopus 로고
    • Convergent evolution: The need to be explicit
    • Doolittle RF. 1994. Convergent evolution: the need to be explicit. Trends Biochem Sci 19:15-18. http://dx.doi.org/10.1016/0968-0004 (94) 90167-8.
    • (1994) Trends Biochem Sci , vol.19 , pp. 15-18
    • Doolittle, R.F.1
  • 89
    • 77951557120 scopus 로고    scopus 로고
    • Nonhomologous isofunctional enzymes: A systematic analysis of alternative solutions in enzyme evolution
    • Omelchenko M, Galperin M, Wolf Y, Koonin E. 2010. Nonhomologous isofunctional enzymes: a systematic analysis of alternative solutions in enzyme evolution. Biol Direct 5:31. http://dx.doi.org/10.1186/1745-6150-5-31.
    • (2010) Biol Direct , vol.5 , pp. 31
    • Omelchenko, M.1    Galperin, M.2    Wolf, Y.3    Koonin, E.4
  • 90
    • 79954422712 scopus 로고    scopus 로고
    • A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis
    • Christensen QH, Martin N, Mansilla MC, De Mendoza D, Cronan JE. 2011. A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis. Mol Microbiol 80:350-363. http://dx.doi.org/10.1111/j.1365-2958.2011.07598.x.
    • (2011) Mol Microbiol , vol.80 , pp. 350-363
    • Christensen, Q.H.1    Martin, N.2    Mansilla, M.C.3    De Mendoza, D.4    Cronan, J.E.5
  • 91
    • 80052424778 scopus 로고    scopus 로고
    • A complex lipoate utilization pathway in Listeria monocytogenes
    • Christensen QH, Hagar JA, O'Riordan MX, Cronan JE. 2011. A complex lipoate utilization pathway in Listeria monocytogenes. J Biol Chem 286:31447-31456. http://dx.doi.org/10.1074/jbc. M111.273607.
    • (2011) J Biol Chem , vol.286 , pp. 31447-31456
    • Christensen, Q.H.1    Hagar, J.A.2    O'Riordan, M.X.3    Cronan, J.E.4
  • 92
    • 0000300645 scopus 로고
    • Biosynthesis of lipoic acid. 1. Incorporation of specifically tritiated octanoic acid into lipoic acid
    • Parry RJ. 1977. Biosynthesis of lipoic acid. 1. Incorporation of specifically tritiated octanoic acid into lipoic acid. J Am Chem Soc 99:6464-6466. http://dx.doi.org/10.1021/ja00461a061.
    • (1977) J Am Chem Soc , vol.99 , pp. 6464-6466
    • Parry, R.J.1
  • 93
    • 0001179909 scopus 로고
    • Biosynthesis of lipoic acid. 2. Stereochemistry of sulfur introduction as C-6 of octanoic acid
    • Parry RJ. 1978. Biosynthesis of lipoic acid. 2. Stereochemistry of sulfur introduction as C-6 of octanoic acid. J Am Chem Soc 100:5243-5244. http://dx.doi.org/10.1021/ja00484a073.
    • (1978) J Am Chem Soc , vol.100 , pp. 5243-5244
    • Parry, R.J.1
  • 94
    • 0018841201 scopus 로고
    • Stoichiometry and stereochemistry of deuterium incorporated into fatty acids by cells of Escherichia coli grown on [methyl-2H3]acetate
    • White RH. 1980. Stoichiometry and stereochemistry of deuterium incorporated into fatty acids by cells of Escherichia coli grown on [methyl-2H3]acetate. Biochemistry 19:9-15. http://dx.doi.org/10.1021/bi00542a002.
    • (1980) Biochemistry , vol.19 , pp. 9-15
    • White, R.H.1
  • 95
    • 0018875796 scopus 로고
    • Stable isotope studies on the biosynthesis of lipoic acid in Escherichia coli
    • White RH. 1980. Stable isotope studies on the biosynthesis of lipoic acid in Escherichia coli. Biochemistry 19:15-19. http://dx.doi.org/10.1021/bi00542a003.
    • (1980) Biochemistry , vol.19 , pp. 15-19
    • White, R.H.1
  • 96
    • 33847086495 scopus 로고
    • Biosynthesis of lipoic acid: Extent of incorporation of deuterated hydroxy- and thiooctanoic acids into lipoic acid
    • White RH. 1980. Biosynthesis of lipoic acid: extent of incorporation of deuterated hydroxy- and thiooctanoic acids into lipoic acid. J Am Chem Soc 102:6605-6607. http://dx.doi.org/10.1021/ja00541a059.
    • (1980) J Am Chem Soc , vol.102 , pp. 6605-6607
    • White, R.H.1
  • 97
    • 84919361067 scopus 로고    scopus 로고
    • Fatty acid biosynthesis revisited: Structure elucidation and metabolic engineering
    • Beld J, Lee DJ, Burkart MD. 2015. Fatty acid biosynthesis revisited: structure elucidation and metabolic engineering. Mol Biosyst 11:38-59. http://dx.doi.org/10.1039/C4MB00443D.
    • (2015) Mol Biosyst , vol.11 , pp. 38-59
    • Beld, J.1    Lee, D.J.2    Burkart, M.D.3
  • 98
    • 0034642248 scopus 로고    scopus 로고
    • Escherichia coli LipA is a lipoyl synthase: In vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein
    • Miller JR, Busby RW, Jordan SW, Cheek J, Henshaw TF, Ashley GW, Broderick JB, Cronan JE, Jr, Marletta MA. 2000. Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein. Biochemistry 39:15166-15178. http://dx.doi.org/10.1021/bi002060n.
    • (2000) Biochemistry , vol.39 , pp. 15166-15178
    • Miller, J.R.1    Busby, R.W.2    Jordan, S.W.3    Cheek, J.4    Henshaw, T.F.5    Ashley, G.W.6    Broderick, J.B.7    Cronan, J.E.8    Marletta, M.A.9
  • 99
    • 0026668860 scopus 로고
    • The biosynthesis of lipoic acid. Cloning of lip, a lipoate biosynthetic locus of Escherichia coli
    • Hayden MA, Huang I, Bussiere DE, Ashley GW. 1992. The biosynthesis of lipoic acid. Cloning of lip, a lipoate biosynthetic locus of Escherichia coli. J Biol Chem 267:9512-9515.
    • (1992) J Biol Chem , vol.267 , pp. 9512-9515
    • Hayden, M.A.1    Huang, I.2    Bussiere, D.E.3    Ashley, G.W.4
  • 100
    • 0027157794 scopus 로고
    • Biosynthesis of lipoic acid: Characterization of the lipoic acid auxotrophs Escherichia coli W1485-lip2 and JRG33-lip9
    • Hayden MA, Huang IY, Iliopoulos G, Orozco M, Ashley GW. 1993. Biosynthesis of lipoic acid: characterization of the lipoic acid auxotrophs Escherichia coli W1485-lip2 and JRG33-lip9. Biochemistry 32:3778-3782. http://dx.doi.org/10.1021/bi00065a033.
    • (1993) Biochemistry , vol.32 , pp. 3778-3782
    • Hayden, M.A.1    Huang, I.Y.2    Iliopoulos, G.3    Orozco, M.4    Ashley, G.W.5
  • 101
    • 3242882336 scopus 로고    scopus 로고
    • AdoMet radical proteins-from structure to evolution-alignment of divergent protein sequences reveals strong secondary structure element conservation
    • Nicolet Y, Drennan CL. 2004. AdoMet radical proteins-from structure to evolution-alignment of divergent protein sequences reveals strong secondary structure element conservation. Nucleic Acids Res 32:4015-4025. http://dx.doi.org/10.1093/nar/gkh728.
    • (2004) Nucleic Acids Res , vol.32 , pp. 4015-4025
    • Nicolet, Y.1    Drennan, C.L.2
  • 102
    • 84866018235 scopus 로고    scopus 로고
    • Radical SAM enzymes and radical enzymology
    • Booker SJ. 2012. Radical SAM enzymes and radical enzymology. Biochim Biophys Acta 1824:1151-1153. http://dx.doi.org/10.1016/j.bbapap. 2012.07.006.
    • (2012) Biochim Biophys Acta , vol.1824 , pp. 1151-1153
    • Booker, S.J.1
  • 103
    • 77955076779 scopus 로고    scopus 로고
    • Mechanistic and functional versatility of radical SAM enzymes
    • Booker SJ, Grove TL. 2010. Mechanistic and functional versatility of radical SAM enzymes. F1000 Biol Rep 2:52. http://dx.doi.org/10.3410/B2-52.
    • (2010) F1000 Biol Rep , vol.2 , pp. 52
    • Booker, S.J.1    Grove, T.L.2
  • 104
    • 0026949744 scopus 로고
    • Conversion of dethiobiotin to biotin in cell-free extracts of Escherichia coli
    • Ifuku O, Kishimoto J, Haze S, Yanagi M, Fukushima S. 1992. Conversion of dethiobiotin to biotin in cell-free extracts of Escherichia coli. Biosci Biotechnol Biochem 56:1780-1785. http://dx.doi.org/10.1271/bbb.56.1780.
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 1780-1785
    • Ifuku, O.1    Kishimoto, J.2    Haze, S.3    Yanagi, M.4    Fukushima, S.5
  • 105
    • 4644229658 scopus 로고    scopus 로고
    • Escherichia coli lipoyl synthase binds two distinct [4Fe-4S] clusters per polypeptide
    • Cicchillo RM, Lee KH, Baleanu-Gogonea C, Nesbitt NM, Krebs C, Booker SJ. 2004. Escherichia coli lipoyl synthase binds two distinct [4Fe-4S] clusters per polypeptide. Biochemistry 43:11770-11781. http://dx.doi.org/10.1021/bi0488505.
    • (2004) Biochemistry , vol.43 , pp. 11770-11781
    • Cicchillo, R.M.1    Lee, K.H.2    Baleanu-Gogonea, C.3    Nesbitt, N.M.4    Krebs, C.5    Booker, S.J.6
  • 107
    • 14844317304 scopus 로고    scopus 로고
    • Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: Both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide
    • Cicchillo RM, Booker SJ. 2005. Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide. J Am Chem Soc 127:2860-2861. http://dx.doi.org/10.1021/ja042428u.
    • (2005) J Am Chem Soc , vol.127 , pp. 2860-2861
    • Cicchillo, R.M.1    Booker, S.J.2
  • 108
  • 109
    • 33747285132 scopus 로고    scopus 로고
    • Lipoyl synthase inserts sulfur atoms into an octanoyl substrate in a stepwise manner
    • Douglas P, Kriek M, Bryant P, Roach PL. 2006. Lipoyl synthase inserts sulfur atoms into an octanoyl substrate in a stepwise manner. Angew Chem Int Ed Engl 45:5197-5199. http://dx.doi.org/10.1002/anie.200601910.
    • (2006) Angew Chem Int Ed Engl , vol.45 , pp. 5197-5199
    • Douglas, P.1    Kriek, M.2    Bryant, P.3    Roach, P.L.4
  • 110
    • 33644944475 scopus 로고    scopus 로고
    • The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate
    • Bryant P, Kriek M, Wood RJ, Roach PL. 2006. The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate. Anal Biochem 351:44-49. http://dx.doi.org/10.1016/j.ab.2006.01.023.
    • (2006) Anal Biochem , vol.351 , pp. 44-49
    • Bryant, P.1    Kriek, M.2    Wood, R.J.3    Roach, P.L.4
  • 111
    • 84904628766 scopus 로고    scopus 로고
    • Evidence for a catalytically and kinetically competent enzyme-substrate cross-linked intermediate in catalysis by lipoyl synthase
    • Lanz ND, Pandelia ME, Kakar ES, Lee KH, Krebs C, Booker SJ. 2014. Evidence for a catalytically and kinetically competent enzyme-substrate cross-linked intermediate in catalysis by lipoyl synthase. Biochemistry 53:4557-4572. http://dx.doi.org/10.1021/bi500432r.
    • (2014) Biochemistry , vol.53 , pp. 4557-4572
    • Lanz, N.D.1    Pandelia, M.E.2    Kakar, E.S.3    Lee, K.H.4    Krebs, C.5    Booker, S.J.6
  • 113
    • 35348854977 scopus 로고    scopus 로고
    • Self-sacrifice in radical Sadenosylmethionine proteins
    • Booker SJ, Cicchillo RM, Grove TL. 2007. Self-sacrifice in radical Sadenosylmethionine proteins. Curr Opin Chem Biol 11:543-552. http://dx.doi.org/10.1016/j.cbpa.2007.08.028.
    • (2007) Curr Opin Chem Biol , vol.11 , pp. 543-552
    • Booker, S.J.1    Cicchillo, R.M.2    Grove, T.L.3
  • 114
    • 17844383968 scopus 로고    scopus 로고
    • Biotin synthase is catalytic in vivo, but catalysis engenders destruction of the protein
    • Choi-Rhee E, Cronan JE. 2005. Biotin synthase is catalytic in vivo, but catalysis engenders destruction of the protein. Chem Biol 12:461-468. http://dx.doi.org/10.1016/j.chembiol.2005.02.006.
    • (2005) Chem Biol , vol.12 , pp. 461-468
    • Choi-Rhee, E.1    Cronan, J.E.2
  • 115
    • 78649312971 scopus 로고    scopus 로고
    • Biotin synthase exhibits burst kinetics and multiple turnovers in the absence of inhibition by products and product-related biomolecules
    • Farrar CE, Siu KK, Howell PL, Jarrett JT. 2010. Biotin synthase exhibits burst kinetics and multiple turnovers in the absence of inhibition by products and product-related biomolecules. Biochemistry 49:9985-9996. http://dx.doi.org/10.1021/bi101023c.
    • (2010) Biochemistry , vol.49 , pp. 9985-9996
    • Farrar, C.E.1    Siu, K.K.2    Howell, P.L.3    Jarrett, J.T.4
  • 116
    • 84899550455 scopus 로고    scopus 로고
    • Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources
    • Li GW, Burkhardt D, Gross C, Weissman JS. 2014. Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources. Cell 157:624-635. http://dx.doi.org/10.1016/j.cell.2014.02.033.
    • (2014) Cell , vol.157 , pp. 624-635
    • Li, G.W.1    Burkhardt, D.2    Gross, C.3    Weissman, J.S.4
  • 117
    • 72449134935 scopus 로고    scopus 로고
    • A lipA (yutB) mutant, encoding lipoic acid synthase, provides insight into the interplay between branched-chain and unsaturated fatty acid biosynthesis in Bacillus subtilis
    • Martin N, Lombardia E, Altabe SG, De Mendoza D, Mansilla MC. 2009. A lipA (yutB) mutant, encoding lipoic acid synthase, provides insight into the interplay between branched-chain and unsaturated fatty acid biosynthesis in Bacillus subtilis. J Bacteriol 191:7447-7455. http://dx.doi.org/10.1128/JB.01160-09.
    • (2009) J Bacteriol , vol.191 , pp. 7447-7455
    • Martin, N.1    Lombardia, E.2    Altabe, S.G.3    De Mendoza, D.4    Mansilla, M.C.5
  • 118
    • 79954414898 scopus 로고    scopus 로고
    • A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis
    • Martin N, Christensen QH, Mansilla MC, Cronan JE, De Mendoza D. 2011. A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis. Mol Microbiol 80:335-349. http://dx.doi.org/10.1111/j.1365-2958.2011.07597.x.
    • (2011) Mol Microbiol , vol.80 , pp. 335-349
    • Martin, N.1    Christensen, Q.H.2    Mansilla, M.C.3    Cronan, J.E.4    De Mendoza, D.5
  • 119
    • 77956286293 scopus 로고    scopus 로고
    • Sortase transpeptidases: Insights into mechanism, substrate specificity, and inhibition
    • Clancy KW, Melvin JA, McCafferty DG. 2010. Sortase transpeptidases: insights into mechanism, substrate specificity, and inhibition. Biopolymers 94:385-396. http://dx.doi.org/10.1002/bip. 21472.
    • (2010) Biopolymers , vol.94 , pp. 385-396
    • Clancy, K.W.1    Melvin, J.A.2    McCafferty, D.G.3
  • 120
    • 34248227584 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. GPI anchoring of protein in yeast and mammalian cells, or: How we learned to stop worrying and love glycophospholipids
    • Orlean P, Menon AK. 2007. Thematic review series: lipid posttranslational modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids. J Lipid Res 48:993-1011. http://dx.doi.org/10.1194/jlr. R700002-JLR200.
    • (2007) J Lipid Res , vol.48 , pp. 993-1011
    • Orlean, P.1    Menon, A.K.2
  • 121
    • 5044234799 scopus 로고    scopus 로고
    • A glycine-dependent riboswitch that uses cooperative binding to control gene expression
    • Mandal M, Lee M, Barrick JE, Weinberg Z, Emilsson GM, Ruzzo WL, Breaker RR. 2004. A glycine-dependent riboswitch that uses cooperative binding to control gene expression. Science 306:275-279. http://dx.doi.org/10.1126/science.1100829.
    • (2004) Science , vol.306 , pp. 275-279
    • Mandal, M.1    Lee, M.2    Barrick, J.E.3    Weinberg, Z.4    Emilsson, G.M.5    Ruzzo, W.L.6    Breaker, R.R.7
  • 122
    • 84895530472 scopus 로고    scopus 로고
    • Metabolic evolution of a deep-branching hyperthermophilic chemoautotrophic bacterium
    • Braakman R, Smith E. 2014. Metabolic evolution of a deep-branching hyperthermophilic chemoautotrophic bacterium. PLoS One 9:e87950. http://dx.doi.org/10.1371/journal.pone.0087950.
    • (2014) PLoS One , vol.9 , pp. e87950
    • Braakman, R.1    Smith, E.2
  • 123
    • 84885848221 scopus 로고    scopus 로고
    • The role of the Saccharomyces cerevisiae lipoate protein ligase homologue, Lip3, in lipoic acid synthesis
    • Hermes FA, Cronan JE. 2013. The role of the Saccharomyces cerevisiae lipoate protein ligase homologue, Lip3, in lipoic acid synthesis. Yeast 30:415-427. http://dx.doi.org/10.1002/yea.2979.
    • (2013) Yeast , vol.30 , pp. 415-427
    • Hermes, F.A.1    Cronan, J.E.2
  • 124
    • 0025145542 scopus 로고
    • PET genes of Saccharomyces cerevisiae
    • Tzagoloff A, Dieckmann CL. 1990. PET genes of Saccharomyces cerevisiae. Microbiol Rev 54:211-225.
    • (1990) Microbiol Rev , vol.54 , pp. 211-225
    • Tzagoloff, A.1    Dieckmann, C.L.2
  • 125
    • 0027292252 scopus 로고
    • Isolation and characterization of LIP5 A lipoate biosynthetic locus of Saccharomyces cerevisiae
    • Sulo P, Martin NC. 1993. Isolation and characterization of LIP5 A lipoate biosynthetic locus of Saccharomyces cerevisiae. J Biol Chem 268:17634-17639.
    • (1993) J Biol Chem , vol.268 , pp. 17634-17639
    • Sulo, P.1    Martin, N.C.2
  • 126
    • 0035872909 scopus 로고    scopus 로고
    • The isolation and characterisation of a Saccharomyces cerevisiae gene (LIP2) involved in the attachment of lipoic acid groups to mitochondrial enzymes
    • Marvin ME, Williams PH, Cashmore AM. 2001. The isolation and characterisation of a Saccharomyces cerevisiae gene (LIP2) involved in the attachment of lipoic acid groups to mitochondrial enzymes. FEMS Microbiol Lett 199:131-136. http://dx.doi.org/10.1111/j.1574-6968.2001.tb10663.x.
    • (2001) FEMS Microbiol Lett , vol.199 , pp. 131-136
    • Marvin, M.E.1    Williams, P.H.2    Cashmore, A.M.3
  • 127
    • 0030739786 scopus 로고    scopus 로고
    • Cloning and characterization of the lipoyl-protein ligase gene LIPB from the yeast Kluyveromyces lactis: Synergistic respiratory deficiency due to mutations in LIPB and mitochondrial F1-ATPase subunits
    • Chen XJ. 1997. Cloning and characterization of the lipoyl-protein ligase gene LIPB from the yeast Kluyveromyces lactis: synergistic respiratory deficiency due to mutations in LIPB and mitochondrial F1-ATPase subunits. Mol Gen Genet 255:341-349. http://dx.doi.org/10.1007/s004380050505.
    • (1997) Mol Gen Genet , vol.255 , pp. 341-349
    • Chen, X.J.1
  • 129
    • 55449098768 scopus 로고    scopus 로고
    • Intersection of RNA processing and the type II fatty acid synthesis pathway in yeast mitochondria
    • Schonauer MS, Kastaniotis AJ, Hiltunen JK, Dieckmann CL. 2008. Intersection of RNA processing and the type II fatty acid synthesis pathway in yeast mitochondria. Mol Cell Biol 28:6646-6657. http://dx.doi.org/10.1128/MCB.01162-08.
    • (2008) Mol Cell Biol , vol.28 , pp. 6646-6657
    • Schonauer, M.S.1    Kastaniotis, A.J.2    Hiltunen, J.K.3    Dieckmann, C.L.4
  • 130
    • 0031026270 scopus 로고    scopus 로고
    • Why do mitochondria synthesize fatty acids? Evidence for involvement in lipoic acid production
    • Wada H, Shintani D, Ohlrogge J. 1997. Why do mitochondria synthesize fatty acids? Evidence for involvement in lipoic acid production. Proc Natl Acad Sci U S A 94:1591-1596. http://dx.doi.org/10.1073/pnas.94.4.1591.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 1591-1596
    • Wada, H.1    Shintani, D.2    Ohlrogge, J.3
  • 131
    • 0034953587 scopus 로고    scopus 로고
    • Lipoic acid metabolism in Arabidopsis thaliana: Cloning and characterization of a cDNA encoding lipoyltransferase
    • Wada M, Yasuno R, Jordan SW, Cronan JE, Jr, Wada H. 2001. Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase. Plant Cell Physiol 42:650-656. http://dx.doi.org/10.1093/pcp/pce081.
    • (2001) Plant Cell Physiol , vol.42 , pp. 650-656
    • Wada, M.1    Yasuno, R.2    Jordan, S.W.3    Cronan, J.E.4    Wada, H.5
  • 132
    • 0035850835 scopus 로고    scopus 로고
    • Identification of an Arabidopsis cDNA encoding a lipoyltransferase located in plastids
    • Wada M, Yasuno R, Wada H. 2001. Identification of an Arabidopsis cDNA encoding a lipoyltransferase located in plastids. FEBS Lett 506:286-290. http://dx.doi.org/10.1016/S0014-5793 (01) 02932-5.
    • (2001) FEBS Lett , vol.506 , pp. 286-290
    • Wada, M.1    Yasuno, R.2    Wada, H.3
  • 133
    • 84890988080 scopus 로고    scopus 로고
    • Two redundant octanoyltransferases and one obligatory lipoyl synthase provide proteinlipoylation autonomy to plastids of Arabidopsis
    • Ewald R, Hoffmann C, Neuhaus E, Bauwe H. 2014. Two redundant octanoyltransferases and one obligatory lipoyl synthase provide proteinlipoylation autonomy to plastids of Arabidopsis. Plant Biol (Stuttg) 16:35-42. http://dx.doi.org/10.1111/plb.12028.
    • (2014) Plant Biol (Stuttg) , vol.16 , pp. 35-42
    • Ewald, R.1    Hoffmann, C.2    Neuhaus, E.3    Bauwe, H.4
  • 134
    • 0032197523 scopus 로고    scopus 로고
    • Biosynthesis of lipoic acid in Arabidopsis: Cloning and characterization of the cDNA for lipoic acid synthase
    • Yasuno R, Wada H. 1998. Biosynthesis of lipoic acid in Arabidopsis: cloning and characterization of the cDNA for lipoic acid synthase. Plant Physiol 118:935-943. http://dx.doi.org/10.1104/pp. 118.3.935.
    • (1998) Plant Physiol , vol.118 , pp. 935-943
    • Yasuno, R.1    Wada, H.2
  • 135
    • 0037165633 scopus 로고    scopus 로고
    • The biosynthetic pathway for lipoic acid is present in plastids and mitochondria in Arabidopsis thaliana
    • Yasuno R, Wada H. 2002. The biosynthetic pathway for lipoic acid is present in plastids and mitochondria in Arabidopsis thaliana. FEBS Lett 517:110-114. http://dx.doi.org/10.1016/S0014-5793 (02) 02589-9.
    • (2002) FEBS Lett , vol.517 , pp. 110-114
    • Yasuno, R.1    Wada, H.2
  • 136
    • 84903650266 scopus 로고    scopus 로고
    • Lipoate-protein ligase and octanoyltransferase are essential for protein lipoylation in mitochondria of Arabidopsis
    • Ewald R, Hoffmann C, Florian A, Neuhaus E, Fernie AR, Bauwe H. 2014. Lipoate-protein ligase and octanoyltransferase are essential for protein lipoylation in mitochondria of Arabidopsis. Plant Physiol 165:978-990. http://dx.doi.org/10.1104/pp. 114.238311.
    • (2014) Plant Physiol , vol.165 , pp. 978-990
    • Ewald, R.1    Hoffmann, C.2    Florian, A.3    Neuhaus, E.4    Fernie, A.R.5    Bauwe, H.6
  • 137
    • 34047258486 scopus 로고    scopus 로고
    • Characterization of a lipoate-protein ligase A gene of rice (Oryza sativa L.)
    • Kang SG, Jeong HK, Lee E, Natarajan S. 2007. Characterization of a lipoate-protein ligase A gene of rice (Oryza sativa L.). Gene 393:53-61. http://dx.doi.org/10.1016/j.gene.2007.01.011.
    • (2007) Gene , vol.393 , pp. 53-61
    • Kang, S.G.1    Jeong, H.K.2    Lee, E.3    Natarajan, S.4
  • 138
    • 66449128208 scopus 로고    scopus 로고
    • Down-regulation of mitochondrial acyl carrier protein in mammalian cells compromises protein lipoylation and respiratory complex I and results in cell death
    • Feng D, Witkowski A, Smith S. 2009. Down-regulation of mitochondrial acyl carrier protein in mammalian cells compromises protein lipoylation and respiratory complex I and results in cell death. J Biol Chem 284:11436-11445. http://dx.doi.org/10.1074/jbc. M806991200.
    • (2009) J Biol Chem , vol.284 , pp. 11436-11445
    • Feng, D.1    Witkowski, A.2    Smith, S.3
  • 140
    • 34347237265 scopus 로고    scopus 로고
    • Coupling of the de novo fatty acid biosynthesis and lipoylation pathways in mammalian mitochondria
    • Witkowski A, Joshi AK, Smith S. 2007. Coupling of the de novo fatty acid biosynthesis and lipoylation pathways in mammalian mitochondria. J Biol Chem 282:14178-14185. http://dx.doi.org/10.1074/jbc. M701486200.
    • (2007) J Biol Chem , vol.282 , pp. 14178-14185
    • Witkowski, A.1    Joshi, A.K.2    Smith, S.3
  • 141
    • 24044496587 scopus 로고    scopus 로고
    • Mammalian mitochondria contain a soluble acyl carrier protein
    • Cronan JE, Fearnley IM, Walker JE. 2005. Mammalian mitochondria contain a soluble acyl carrier protein. FEBS Lett 579:4892-4896. http://dx.doi.org/10.1016/j.febslet.2005.07.077.
    • (2005) FEBS Lett , vol.579 , pp. 4892-4896
    • Cronan, J.E.1    Fearnley, I.M.2    Walker, J.E.3
  • 142
    • 84915761829 scopus 로고    scopus 로고
    • Architecture of mammalian respiratory complex I
    • Vinothkumar KR, Zhu J, Hirst J. 2014. Architecture of mammalian respiratory complex I. Nature 515:80-84. http://dx.doi.org/10.1038/nature13686.
    • (2014) Nature , vol.515 , pp. 80-84
    • Vinothkumar, K.R.1    Zhu, J.2    Hirst, J.3
  • 143
    • 24344504437 scopus 로고    scopus 로고
    • Endogenous production of lipoic acid is essential for mouse development
    • Yi X, Maeda N. 2005. Endogenous production of lipoic acid is essential for mouse development. Mol Cell Biol 25:8387-8392. http://dx.doi.org/10.1128/MCB.25.18.8387-8392.2005.
    • (2005) Mol Cell Biol , vol.25 , pp. 8387-8392
    • Yi, X.1    Maeda, N.2
  • 144
    • 83455253737 scopus 로고    scopus 로고
    • Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation
    • Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W. 2011. Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation. Am J Hum Genet 89:792-797. http://dx.doi.org/10.1016/j.ajhg.2011.11.011.
    • (2011) Am J Hum Genet , vol.89 , pp. 792-797
    • Mayr, J.A.1    Zimmermann, F.A.2    Fauth, C.3    Bergheim, C.4    Meierhofer, D.5    Radmayr, D.6    Zschocke, J.7    Koch, J.8    Sperl, W.9
  • 145
    • 69949104384 scopus 로고    scopus 로고
    • Alphalipoic acid as a dietary supplement: Molecular mechanisms and therapeutic potential
    • Shay KP, Moreau RF, Smith EJ, Smith AR, Hagen TM. 2009. Alphalipoic acid as a dietary supplement: molecular mechanisms and therapeutic potential. Biochim Biophys Acta 1790:1149-1160. http://dx.doi.org/10.1016/j.bbagen. 2009.07.026.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1149-1160
    • Shay, K.P.1    Moreau, R.F.2    Smith, E.J.3    Smith, A.R.4    Hagen, T.M.5
  • 146
    • 0030768236 scopus 로고    scopus 로고
    • The pharmacology of the antioxidant lipoic acid
    • Biewenga GP, Haenen GR, Bast A. 1997. The pharmacology of the antioxidant lipoic acid. Gen Pharmacol 29:315-331. http://dx.doi.org/10.1016/S0306-3623 (96) 00474-0.
    • (1997) Gen Pharmacol , vol.29 , pp. 315-331
    • Biewenga, G.P.1    Haenen, G.R.2    Bast, A.3
  • 148
    • 0031946421 scopus 로고    scopus 로고
    • Redox regulation of cell functions by alphalipoate: Biochemical and molecular aspects
    • Roy S, Packer L. 1998. Redox regulation of cell functions by alphalipoate: biochemical and molecular aspects. Biofactors 7:263-267. http://dx.doi.org/10.1002/biof.5520070324.
    • (1998) Biofactors , vol.7 , pp. 263-267
    • Roy, S.1    Packer, L.2
  • 155
    • 84911930913 scopus 로고    scopus 로고
    • An evolutionary perspective on protein moonlighting
    • Copley SD. 2014. An evolutionary perspective on protein moonlighting. Biochem Soc Trans 42:1684-1691. http://dx.doi.org/10.1042/BST20140245.
    • (2014) Biochem Soc Trans , vol.42 , pp. 1684-1691
    • Copley, S.D.1
  • 156
    • 84940104582 scopus 로고    scopus 로고
    • Why study moonlighting proteins?
    • Jeffery CJ. 2015. Why study moonlighting proteins? Front Genet 6:211. http://dx.doi.org/10.3389/fgene.2015.00211.
    • (2015) Front Genet , vol.6 , pp. 211
    • Jeffery, C.J.1
  • 157
    • 84874028131 scopus 로고    scopus 로고
    • Essential nontranslational functions of tRNA synthetases
    • Guo M, Schimmel P. 2013. Essential nontranslational functions of tRNA synthetases. Nat Chem Biol 9:145-153. http://dx.doi.org/10.1038/nchembio.1158.
    • (2013) Nat Chem Biol , vol.9 , pp. 145-153
    • Guo, M.1    Schimmel, P.2
  • 158
    • 84940100456 scopus 로고    scopus 로고
    • Gene duplication and the evolution of moonlighting proteins
    • Espinosa-Cantú A, Ascencio D, Barona-Gómez F, DeLuna A. 2015. Gene duplication and the evolution of moonlighting proteins. Front Genet 6:227 http://dx.doi.org/10.3389/fgene.2015.00227.
    • (2015) Front Genet , vol.6 , pp. 227
    • Espinosa-Cantú, A.1    Ascencio, D.2    Barona-Gómez, F.3    De Luna, A.4
  • 159
    • 0027463576 scopus 로고
    • Expression and lipoylation in Escherichia coli of the inner lipoyl domain of the E2 component of the human pyruvate dehydrogenase complex
    • Quinn J, Diamond AG, Masters AK, Brookfield DE, Wallis NG, Yeaman SJ. 1993. Expression and lipoylation in Escherichia coli of the inner lipoyl domain of the E2 component of the human pyruvate dehydrogenase complex. Biochem J 289:81-85. http://dx.doi.org/10.1042/bj2890081.
    • (1993) Biochem J , vol.289 , pp. 81-85
    • Quinn, J.1    Diamond, A.G.2    Masters, A.K.3    Brookfield, D.E.4    Wallis, N.G.5    Yeaman, S.J.6
  • 160
    • 0026757052 scopus 로고
    • Expression of mature bovine H-protein of the glycine cleavage system in Escherichia coli and in vitro lipoylation of the apoform
    • Fujiwara K, Okamura-Ikeda K, Motokawa Y. 1992. Expression of mature bovine H-protein of the glycine cleavage system in Escherichia coli and in vitro lipoylation of the apoform. J Biol Chem 267:20011-20016.
    • (1992) J Biol Chem , vol.267 , pp. 20011-20016
    • Fujiwara, K.1    Okamura-Ikeda, K.2    Motokawa, Y.3
  • 161
    • 2542508756 scopus 로고    scopus 로고
    • Reaction medium engineering in enzymatic peptide fragment condensation: Synthesis of eledoisin and LH-RH
    • Bjorup P, Torres JL, Adlercreutz P, Clapes P. 1998. Reaction medium engineering in enzymatic peptide fragment condensation: synthesis of eledoisin and LH-RH. Bioorg Med Chem 6:891-901. http://dx.doi.org/10.1016/S0968-0896 (98) 00046-7.
    • (1998) Bioorg Med Chem , vol.6 , pp. 891-901
    • Bjorup, P.1    Torres, J.L.2    Adlercreutz, P.3    Clapes, P.4
  • 162
    • 0023788217 scopus 로고
    • The influence of water on protease-catalyzed peptide synthesis in acetonitrile/water mixtures
    • Reslow M, Adlercreutz P, Mattiasson B. 1988. The influence of water on protease-catalyzed peptide synthesis in acetonitrile/water mixtures. Eur J Biochem 177:313-318. http://dx.doi.org/10.1111/j.1432-1033.1988.tb14378.x.
    • (1988) Eur J Biochem , vol.177 , pp. 313-318
    • Reslow, M.1    Adlercreutz, P.2    Mattiasson, B.3
  • 163
    • 0023362434 scopus 로고
    • Using proteases in peptide synthesis
    • Morihara K. 1987. Using proteases in peptide synthesis. Trends Biotechnol 5:163-170.
    • (1987) Trends Biotechnol , vol.5 , pp. 163-170
    • Morihara, K.1
  • 164
    • 35448931669 scopus 로고    scopus 로고
    • LplA1-dependent utilization of host lipoyl peptides enables Listeria cytosolic growth and virulence
    • Keeney KM, Stuckey JA, O'Riordan MX. 2007. LplA1-dependent utilization of host lipoyl peptides enables Listeria cytosolic growth and virulence. Mol Microbiol 66:758-770. http://dx.doi.org/10.1111/j.1365-2958.2007.05956.x.
    • (2007) Mol Microbiol , vol.66 , pp. 758-770
    • Keeney, K.M.1    Stuckey, J.A.2    O'Riordan, M.X.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.