메뉴 건너뛰기




Volumn 12, Issue 3, 2008, Pages 461-469

Characterization of a thermostable dihydrodipicolinate synthase from Thermoanaerobacter tengcongensis

Author keywords

Dihydrodipicolinate synthase; Enzymes; Lysine biosynthesis; Thermoanaerobacter tengcongensis; Thermophile

Indexed keywords

ASPARTIC ACID; ASPARTIC SEMIALDEHYDE; BACTERIAL PROTEIN; DIHYDRODIPICOLINATE SYNTHASE; DRUG DERIVATIVE; HYDROLYASE; LYSINE; PYRUVIC ACID; RECOMBINANT PROTEIN;

EID: 43049158129     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-008-0152-z     Document Type: Article
Times cited : (18)

References (38)
  • 2
    • 0031566028 scopus 로고    scopus 로고
    • Structure of dihydrodipicolinate synthase of Nicotiana sylvestris reveals novel quaternary structure
    • Blickling S, Beisel HG, Bozic D, Knablein J, Laber B, Huber R (1997a) Structure of dihydrodipicolinate synthase of Nicotiana sylvestris reveals novel quaternary structure. J Mol Biol 274:608-621
    • (1997) J Mol Biol , vol.274 , pp. 608-621
    • Blickling, S.1    Beisel, H.G.2    Bozic, D.3    Knablein, J.4    Laber, B.5    Huber, R.6
  • 3
    • 0031012162 scopus 로고    scopus 로고
    • Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy
    • Blickling S, Renner C, Laber B, Pohlenz HD, Holak TA, Huber R (1997b) Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy. Biochemistry 36:24-33
    • (1997) Biochemistry , vol.36 , pp. 24-33
    • Blickling, S.1    Renner, C.2    Laber, B.3    Pohlenz, H.D.4    Holak, T.A.5    Huber, R.6
  • 4
    • 30744458839 scopus 로고    scopus 로고
    • Regulation of aspartokinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase in Lactobacillus plantarum
    • Cahyanto MN, Kawasaki H, Nagashio M, Fujiyama K, Seki T (2006) Regulation of aspartokinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase in Lactobacillus plantarum. Microbiology 152:105-112
    • (2006) Microbiology , vol.152 , pp. 105-112
    • Cahyanto, M.N.1    Kawasaki, H.2    Nagashio, M.3    Fujiyama, K.4    Seki, T.5
  • 5
    • 33746078101 scopus 로고    scopus 로고
    • New superfamily members identified for Schiff-base enzymes based on verification of catalytically essential residues
    • Choi KH, Lai V, Foster CE, Morris AJ, Tolan DR, Allen KN (2006) New superfamily members identified for Schiff-base enzymes based on verification of catalytically essential residues. Biochemistry 45:8546-8555
    • (2006) Biochemistry , vol.45 , pp. 8546-8555
    • Choi, K.H.1    Lai, V.2    Foster, C.E.3    Morris, A.J.4    Tolan, D.R.5    Allen, K.N.6
  • 7
    • 0024145176 scopus 로고
    • Regulation of enzymes of lysine biosynthesis in Corynebacterium glutamicum
    • Cremer J, Treptow C, Eggeling L, Sahm H (1988) Regulation of enzymes of lysine biosynthesis in Corynebacterium glutamicum. J Gen Microbiol 134:3221-3229
    • (1988) J Gen Microbiol , vol.134 , pp. 3221-3229
    • Cremer, J.1    Treptow, C.2    Eggeling, L.3    Sahm, H.4
  • 8
    • 0001692779 scopus 로고
    • Purification and characterization of dihydrodipicolinate synthase from pea
    • Dereppe C, Bold G, Ghisalba O, Ebert E, Schar HP (1992) Purification and characterization of dihydrodipicolinate synthase from pea. Plant Physiol 98:813-821
    • (1992) Plant Physiol , vol.98 , pp. 813-821
    • Dereppe, C.1    Bold, G.2    Ghisalba, O.3    Ebert, E.4    Schar, H.P.5
  • 9
    • 1242337331 scopus 로고    scopus 로고
    • Dihydrodipicolinate synthase is not inhibited by its substrate, (S)-aspartate beta-semialdehyde
    • Dobson RC, Gerrard JA, Pearce FG (2004a) Dihydrodipicolinate synthase is not inhibited by its substrate, (S)-aspartate beta-semialdehyde. Biochem J 377:757-762
    • (2004) Biochem J , vol.377 , pp. 757-762
    • Dobson, R.C.1    Gerrard, J.A.2    Pearce, F.G.3
  • 10
    • 1842452651 scopus 로고    scopus 로고
    • The crystal structure of three site-directed mutants of Escherichia coli dihydrodipicolinate synthase: Further evidence for a catalytic triad
    • Dobson RC, Valegard K, Gerrard JA (2004b) The crystal structure of three site-directed mutants of Escherichia coli dihydrodipicolinate synthase: further evidence for a catalytic triad. J Mol Biol 338:329-339
    • (2004) J Mol Biol , vol.338 , pp. 329-339
    • Dobson, R.C.1    Valegard, K.2    Gerrard, J.A.3
  • 11
    • 25144446271 scopus 로고    scopus 로고
    • The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance
    • Dobson RC, Griffin MD, Jameson GB, Gerrard JA (2005) The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance. Acta crystallogr Sect D 61:1116-1124
    • (2005) Acta Crystallogr Sect D , vol.61 , pp. 1116-1124
    • Dobson, R.C.1    Griffin, M.D.2    Jameson, G.B.3    Gerrard, J.A.4
  • 13
    • 0029394916 scopus 로고
    • A dinucleotide mutation in dihydrodipicolinate synthase of Nicotiana sylvestris leads to lysine overproduction
    • Ghislain M, Frankard V, Jacobs M (1995) A dinucleotide mutation in dihydrodipicolinate synthase of Nicotiana sylvestris leads to lysine overproduction. Plant J 8:733-743
    • (1995) Plant J , vol.8 , pp. 733-743
    • Ghislain, M.1    Frankard, V.2    Jacobs, M.3
  • 15
    • 0016656134 scopus 로고
    • Regulation of dihydrodipicolinate synthase during growth and sporulation of Bacillus cereus
    • Hoganson DA, Stahly DP (1975) Regulation of dihydrodipicolinate synthase during growth and sporulation of Bacillus cereus. J Bacteriol 124:1344-1350
    • (1975) J Bacteriol , vol.124 , pp. 1344-1350
    • Hoganson, D.A.1    Stahly, D.P.2
  • 16
    • 0000146015 scopus 로고
    • The extinction coefficients of the reduced band of pyridin nucleotides
    • Horecker BL, Kornberg A (1948) The extinction coefficients of the reduced band of pyridin nucleotides. J Biol Chem 175:385-390
    • (1948) J Biol Chem , vol.175 , pp. 385-390
    • Horecker, B.L.1    Kornberg, A.2
  • 17
    • 0031037267 scopus 로고    scopus 로고
    • Dihydrodipicolinate synthase from Escherichia coli: PH dependent changes in the kinetic mechanism and kinetic mechanism of allosteric inhibition by l-lysine
    • Karsten WE (1997) Dihydrodipicolinate synthase from Escherichia coli: pH dependent changes in the kinetic mechanism and kinetic mechanism of allosteric inhibition by l-lysine. Biochemistry 36:1730-1739
    • (1997) Biochemistry , vol.36 , pp. 1730-1739
    • Karsten, W.E.1
  • 18
    • 0001285394 scopus 로고
    • Purification and characterization of dihydrodipicolinate synthase from wheat suspension cultures
    • Kumpaisal R, Hashimoto T, Yamada Y (1987) Purification and characterization of dihydrodipicolinate synthase from wheat suspension cultures. Plant Physiol 85:145-151
    • (1987) Plant Physiol , vol.85 , pp. 145-151
    • Kumpaisal, R.1    Hashimoto, T.2    Yamada, Y.3
  • 19
    • 0026486643 scopus 로고
    • Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization
    • Pt 2
    • Laber B, Gomis-Ruth FX, Romao MJ, Huber R (1992) Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization. Biochem J 288(Pt 2):691-695
    • (1992) Biochem J , vol.288 , pp. 691-695
    • Laber, B.1    Gomis-Ruth, F.X.2    Romao, M.J.3    Huber, R.4
  • 20
    • 0037166314 scopus 로고    scopus 로고
    • Metabolic channeling of carbamoyl phosphate, a thermolabile intermediate: Evidence for physical interaction between carbamate kinase-like carbamoyl-phosphate synthetase and ornithine carbamoyltransferase from the hyperthermophile Pyrococcus furiosus
    • Massant J, Verstreken P, Durbecq V, Kholti A, Legrain C, Beeckmans S, Cornelis P, Glansdorff N (2002) Metabolic channeling of carbamoyl phosphate, a thermolabile intermediate: evidence for physical interaction between carbamate kinase-like carbamoyl-phosphate synthetase and ornithine carbamoyltransferase from the hyperthermophile Pyrococcus furiosus. J Biol Chem 277:18517-18522
    • (2002) J Biol Chem , vol.277 , pp. 18517-18522
    • Massant, J.1    Verstreken, P.2    Durbecq, V.3    Kholti, A.4    Legrain, C.5    Beeckmans, S.6    Cornelis, P.7    Glansdorff, N.8
  • 21
    • 0017668490 scopus 로고
    • The enzymology of lysine biosynthesis in higher plants. the occurrence, characterization and some regulatory properties of dihydrodipicolinate synthase
    • Mazelis M, Whatley FR, Whatley J (1977) The enzymology of lysine biosynthesis in higher plants. The occurrence, characterization and some regulatory properties of dihydrodipicolinate synthase. FEBS Lett 84:236-240
    • (1977) FEBS Lett , vol.84 , pp. 236-240
    • Mazelis, M.1    Whatley, F.R.2    Whatley, J.3
  • 22
    • 0028907826 scopus 로고
    • The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 a resolution
    • Mirwaldt C, Korndorfer I, Huber R (1995) The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution. J Mol Biol 246:227-239
    • (1995) J Mol Biol , vol.246 , pp. 227-239
    • Mirwaldt, C.1    Korndorfer, I.2    Huber, R.3
  • 24
    • 1842837780 scopus 로고    scopus 로고
    • The preparation of (S)-aspartate semi-aldehyde appropriate for use in biochemical studies
    • Roberts SJ, Morris JC, Dobson RC, Gerrard JA (2003) The preparation of (S)-aspartate semi-aldehyde appropriate for use in biochemical studies. Bioorg Med Chem Lett 13:265-267
    • (2003) Bioorg Med Chem Lett , vol.13 , pp. 265-267
    • Roberts, S.J.1    Morris, J.C.2    Dobson, R.C.3    Gerrard, J.A.4
  • 25
    • 0030725699 scopus 로고    scopus 로고
    • Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate
    • Scapin G, Reddy SG, Zheng R, Blanchard JS (1997) Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate. Biochemistry 36:15081-15088
    • (1997) Biochemistry , vol.36 , pp. 15081-15088
    • Scapin, G.1    Reddy, S.G.2    Zheng, R.3    Blanchard, J.S.4
  • 26
    • 0014961724 scopus 로고
    • The pyruvate-aspartic semialdehyde condensing enzyme of Escherichia coli
    • Shedlarski JG, Gilvarg C (1970) The pyruvate-aspartic semialdehyde condensing enzyme of Escherichia coli. J Biol Chem 245:1362-1373
    • (1970) J Biol Chem , vol.245 , pp. 1362-1373
    • Shedlarski, J.G.1    Gilvarg, C.2
  • 27
    • 0014664053 scopus 로고
    • Dihydrodipicolinic acid synthase of Bacillus licheniformis
    • Stahly DP (1969) Dihydrodipicolinic acid synthase of Bacillus licheniformis. Biochim Biophys Acta 191:439-451
    • (1969) Biochim Biophys Acta , vol.191 , pp. 439-451
    • Stahly, D.P.1
  • 28
    • 0346366812 scopus 로고    scopus 로고
    • MosA, a protein implicated in rhizopine biosynthesis in Sinorhizobium meliloti L5-30, is a dihydrodipicolinate synthase
    • Tam PH, Phenix CP, Palmer DR (2004) MosA, a protein implicated in rhizopine biosynthesis in Sinorhizobium meliloti L5-30, is a dihydrodipicolinate synthase. J Mol Biol 335:393-397
    • (2004) J Mol Biol , vol.335 , pp. 393-397
    • Tam, P.H.1    Phenix, C.P.2    Palmer, D.R.3
  • 29
    • 33745205636 scopus 로고    scopus 로고
    • L-Lysine biosynthetic pathway of Methylophilus methylotrophus and construction of an l-Lysine producer
    • Tsujimoto N, Gunji Y, Ogawa-Miyata Y, Shimaoka M, Yasueda H (2006) l-Lysine biosynthetic pathway of Methylophilus methylotrophus and construction of an l-Lysine producer. J Biotechnol 124:327-337
    • (2006) J Biotechnol , vol.124 , pp. 327-337
    • Tsujimoto, N.1    Gunji, Y.2    Ogawa-Miyata, Y.3    Shimaoka, M.4    Yasueda, H.5
  • 30
    • 0027443220 scopus 로고
    • Synthesis of the Trifluoroacetate salt of aspartic-acid beta-semialdehyde, an intermediate in the biosynthesis of L-Lysine, L-Threonine, and L-Methionine
    • Tudor DW, Lewis T, Robins DJ (1993) Synthesis of the Trifluoroacetate salt of aspartic-acid beta-semialdehyde, an intermediate in the biosynthesis of L-Lysine, L-Threonine, and L-Methionine. Synthesis-Stuttgart: 1061-1062
    • (1993) Synthesis-Stuttgart , pp. 1061-1062
    • Tudor, D.W.1    Lewis, T.2    Robins, D.J.3
  • 31
    • 0028447770 scopus 로고
    • Isolation of a poplar and an Arabidopsis thaliana dihydrodipicolinate synthase cDNA clone
    • Vauterin M, Jacobs M (1994) Isolation of a poplar and an Arabidopsis thaliana dihydrodipicolinate synthase cDNA clone. Plant Mol Biol 25:545-550
    • (1994) Plant Mol Biol , vol.25 , pp. 545-550
    • Vauterin, M.1    Jacobs, M.2
  • 32
    • 0029018981 scopus 로고
    • XylA cloning and sequencing and biochemical characterization of xylose isomerase from Thermotoga neapolitana
    • Vieille C, Hess JM, Kelly RM, Zeikus JG (1995) xylA cloning and sequencing and biochemical characterization of xylose isomerase from Thermotoga neapolitana. Appl Environ Microbiol 61:1867-1875
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1867-1875
    • Vieille, C.1    Hess, J.M.2    Kelly, R.M.3    Zeikus, J.G.4
  • 33
    • 0030992108 scopus 로고    scopus 로고
    • Hydrogen exchange/electrospray ionization mass spectrometry studies of substrate and inhibitor binding and conformational changes of Escherichia coli dihydrodipicolinate reductase
    • Wang F, Blanchard JS, Tang XJ (1997) Hydrogen exchange/electrospray ionization mass spectrometry studies of substrate and inhibitor binding and conformational changes of Escherichia coli dihydrodipicolinate reductase. Biochemistry 36:3755-3759
    • (1997) Biochemistry , vol.36 , pp. 3755-3759
    • Wang, F.1    Blanchard, J.S.2    Tang, X.J.3
  • 34
    • 0024452352 scopus 로고
    • Enantiospecific synthesis of l-alpha-aminosuberic acid-synthetic applications in preparation of atrial natriuretic factor analogs
    • Wernic D, Dimaio J, Adams J (1989) Enantiospecific synthesis of l-alpha-aminosuberic acid-synthetic applications in preparation of atrial natriuretic factor analogs. J Org Chem 54:4224-4228
    • (1989) J Org Chem , vol.54 , pp. 4224-4228
    • Wernic, D.1    Dimaio, J.2    Adams, J.3
  • 36
    • 0034884397 scopus 로고    scopus 로고
    • Thermoanaerobacter tengcongensis sp. nov., a novel anaerobic, saccharolytic, thermophilic bacterium isolated from a hot spring in Tengcong, China
    • Xue Y, Xu Y, Liu Y, Ma Y, Zhou P (2001) Thermoanaerobacter tengcongensis sp. nov., a novel anaerobic, saccharolytic, thermophilic bacterium isolated from a hot spring in Tengcong, China. Int J Syst Evol Microbiol 51:1335-1341
    • (2001) Int J Syst Evol Microbiol , vol.51 , pp. 1335-1341
    • Xue, Y.1    Xu, Y.2    Liu, Y.3    Ma, Y.4    Zhou, P.5
  • 37
    • 0013827137 scopus 로고
    • The condensation step in diaminopimelate synthesis
    • Yugari Y, Gilvarg C (1965) The condensation step in diaminopimelate synthesis. J Biol Chem 240:4710-4716
    • (1965) J Biol Chem , vol.240 , pp. 4710-4716
    • Yugari, Y.1    Gilvarg, C.2
  • 38
    • 0017283326 scopus 로고
    • Molar absorptivities of beta-NADH and beta-NADPH
    • Ziegenhorn J, Senn M, Bucher T (1976) Molar absorptivities of beta-NADH and beta-NADPH. Clin Chem 22:151-160
    • (1976) Clin Chem , vol.22 , pp. 151-160
    • Ziegenhorn, J.1    Senn, M.2    Bucher, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.