메뉴 건너뛰기




Volumn 468, Issue 3, 2015, Pages 475-484

Cofactor specificity motifs and the induced fit mechanism in class I ketol-acid reductoisomerases

Author keywords

Acetohydroxyacid isomeroreductase (AHAIR); Cofactor binding; Conformational change; Crystal structure; Ketol acid reductoisomerase (KARI)

Indexed keywords

CLASS I KETOL ACID REDUCTOISOMERASE; KETOL ACID REDUCTOISOMERASE; NICOTINAMIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG; ADENOSINE DIPHOSPHATE RIBOSE; BACTERIAL PROTEIN; COENZYME; MAGNESIUM; MUTANT PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RECOMBINANT PROTEIN;

EID: 84935015129     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20150183     Document Type: Article
Times cited : (18)

References (50)
  • 1
    • 0024977333 scopus 로고
    • Mechanism of ketol acid reductoisomerase - Steady-state analysis and metal-ion requirement
    • Chunduru, S. K., Mrachko, G. T. and Calvo, K. C. (1989) Mechanism of ketol acid reductoisomerase - steady-state analysis and metal-ion requirement. Biochemistry 28, 486-493
    • (1989) Biochemistry , vol.28 , pp. 486-493
    • Chunduru, S.K.1    Mrachko, G.T.2    Calvo, K.C.3
  • 2
    • 84907939387 scopus 로고    scopus 로고
    • Uncovering rare NADH-preferring ketol-acid reductoisomerases
    • Brinkmann-Chen, S., Cahn, J. K. B. and Arnold, F. H. (2014) Uncovering rare NADH-preferring ketol-acid reductoisomerases. Metab. Eng. 26, 17-22
    • (2014) Metab. Eng. , vol.26 , pp. 17-22
    • Brinkmann-Chen, S.1    Cahn, J.K.B.2    Arnold, F.H.3
  • 3
    • 0034868638 scopus 로고    scopus 로고
    • Enzymology, structure, and dynamics of acetohydroxy acid isomeroreductase
    • Dumas, R., Biou, V., Halgand, F., Douce, R. and Duggleby, R. G. (2001) Enzymology, structure, and dynamics of acetohydroxy acid isomeroreductase. Acc. Chem. Res. 34, 399-408
    • (2001) Acc. Chem. Res. , vol.34 , pp. 399-408
    • Dumas, R.1    Biou, V.2    Halgand, F.3    Douce, R.4    Duggleby, R.G.5
  • 4
    • 0029010594 scopus 로고
    • Evidence for 2 catalytically different magnesium-binding sites in acetohydroxy acid isomeroreductase by site-directed mutagenesis
    • Dumas, R., Butikofer, M. C., Job, D. and Douce, R. (1995) Evidence for 2 catalytically different magnesium-binding sites in acetohydroxy acid isomeroreductase by site-directed mutagenesis. Biochemistry 34, 6026-6036
    • (1995) Biochemistry , vol.34 , pp. 6026-6036
    • Dumas, R.1    Butikofer, M.C.2    Job, D.3    Douce, R.4
  • 5
    • 0033545907 scopus 로고    scopus 로고
    • Characterization of the conformational changes of acetohydroxy acid isomeroreductase induced by the binding of Mg2+ ions, NADPH, and a competitive inhibitor
    • Halgand, F., Dumas, R., Biou, V., Andrieu, JP., Thomazeau, K., Gagnon, J., Douce, R. and Forest, E. (1999) Characterization of the conformational changes of acetohydroxy acid isomeroreductase induced by the binding of Mg2+ ions, NADPH, and a competitive inhibitor. Biochemistry 38, 6025-6034
    • (1999) Biochemistry , vol.38 , pp. 6025-6034
    • Halgand, F.1    Dumas, R.2    Biou, V.3    Andrieu, J.P.4    Thomazeau, K.5    Gagnon, J.6    Douce, R.7    Forest, E.8
  • 6
    • 0026690916 scopus 로고
    • The pH-dependence of the kinetic parameters of ketol acid reductoisomerase indicates a proton shuttle mechanism for alkyl migration
    • Mrachko, G. T., Chunduru, S. K. and Calvo, K. C. (1992) The pH-dependence of the kinetic parameters of ketol acid reductoisomerase indicates a proton shuttle mechanism for alkyl migration. Arch. Biochem. Biophys. 294, 446-453
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 446-453
    • Mrachko, G.T.1    Chunduru, S.K.2    Calvo, K.C.3
  • 7
    • 12544251400 scopus 로고    scopus 로고
    • Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site
    • Tyagi, R., Lee, Y. T., Guddat, L. W. and Duggleby, R. G. (2005) Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site. FEBS J 272, 593-602
    • (2005) FEBS J , vol.272 , pp. 593-602
    • Tyagi, R.1    Lee, Y.T.2    Guddat, L.W.3    Duggleby, R.G.4
  • 8
    • 84856138130 scopus 로고    scopus 로고
    • Improvement of the redox balance increases L-valine production by Corynebacterium glutamicum under oxygen deprivation conditions
    • Hasegawa, S., Uematsu, K., Natsuma, Y., Suda, M., Hiraga, K., Jojima, T., Inui, M. and Yukawa, H. (2012) Improvement of the redox balance increases L-valine production by Corynebacterium glutamicum under oxygen deprivation conditions. Appl. Environ. Microbiol. 78, 865-875
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 865-875
    • Hasegawa, S.1    Uematsu, K.2    Natsuma, Y.3    Suda, M.4    Hiraga, K.5    Jojima, T.6    Inui, M.7    Yukawa, H.8
  • 9
    • 74149089019 scopus 로고    scopus 로고
    • Fermentative production of branched chain amino acids: A focus on metabolic engineering
    • Park, J. H. and Lee, S. Y. (2010) Fermentative production of branched chain amino acids: a focus on metabolic engineering. Appl. Microbiol. Biotechnol. 85, 491-506
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 491-506
    • Park, J.H.1    Lee, S.Y.2
  • 10
    • 34249934691 scopus 로고    scopus 로고
    • Metabolic engineering of Escherichia coli for the production of L-valine based on transcriptome analysis and in silico gene knockout simulation
    • Park, J. H., Lee, K. H., Kim, T. Y. and Lee, S. Y. (2007) Metabolic engineering of Escherichia coli for the production of L-valine based on transcriptome analysis and in silico gene knockout simulation. Proc. Natl. Acad. Sci. U. S. A. 104, 7797-7802
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 7797-7802
    • Park, J.H.1    Lee, K.H.2    Kim, T.Y.3    Lee, S.Y.4
  • 11
    • 84892459391 scopus 로고    scopus 로고
    • Pushing product formation to its limit: Metabolic engineering of Corynebacterium glutamicum for L-leucine overproduction
    • Vogt, M., Haas, S., Klaffl, S., Polen, T., Eggeling, L., Van Ooyen, J. and Bott, M. (2014) Pushing product formation to its limit: metabolic engineering of Corynebacterium glutamicum for L-leucine overproduction. Metab. Eng. 22, 40-52
    • (2014) Metab. Eng. , vol.22 , pp. 40-52
    • Vogt, M.1    Haas, S.2    Klaffl, S.3    Polen, T.4    Eggeling, L.5    Van Ooyen, J.6    Bott, M.7
  • 12
    • 0028018345 scopus 로고
    • Interactions of plant acetohydroxy acid isomeroreductase with reaction intermediate analogs - Correlation of the slow, competitive, inhibition-kinetics of enzyme-activity and herbicidal effects
    • Dumas, R., Cornillon-Bertrand, C., Guigue-Talet, P., Genix, P., Douce, R. and Job, D. (1994) Interactions of plant acetohydroxy acid isomeroreductase with reaction intermediate analogs - correlation of the slow, competitive, inhibition-kinetics of enzyme-activity and herbicidal effects. Biochem. J. 301, 813-820 PubMed
    • (1994) Biochem. J. , vol.301 , pp. 813-820
    • Dumas, R.1    Cornillon-Bertrand, C.2    Guigue-Talet, P.3    Genix, P.4    Douce, R.5    Job, D.6
  • 13
    • 0030025785 scopus 로고    scopus 로고
    • Metabolic effects of inhibitors of two enzymes of the branched-chain amino acid pathway in Salmonella typhimurium
    • Epelbaum, S., Chipman, D. M. and Barak, Z. (1996) Metabolic effects of inhibitors of two enzymes of the branched-chain amino acid pathway in Salmonella typhimurium. J. Bacteriol. 178, 1187-1196 PubMed
    • (1996) J. Bacteriol. , vol.178 , pp. 1187-1196
    • Epelbaum, S.1    Chipman, D.M.2    Barak, Z.3
  • 14
    • 13944269884 scopus 로고    scopus 로고
    • Cyclopropane-1, 1-dicarboxylate is a slow-, tight-binding inhibitor of rice ketol-acid reductoisomerase
    • Lee, Y. T., Ta, H. T. and Duggleby, R. G. (2005) Cyclopropane-1, 1-dicarboxylate is a slow-, tight-binding inhibitor of rice ketol-acid reductoisomerase. Plant Sci 168, 1035-1040
    • (2005) Plant Sci , vol.168 , pp. 1035-1040
    • Lee, Y.T.1    Ta, H.T.2    Duggleby, R.G.3
  • 15
    • 34250219961 scopus 로고    scopus 로고
    • Synthesis, bioactivity, theoretical and molecular docking study of 1-cyano-N-substituted-cyclopropanecarboxamide as ketol-acid reductoisomerase inhibitor
    • Liu, X. H., Liu, X. H., Chen, P. Q., Wang, B. L., Li, Y. H., Wang, S. H. and Li, Z. M. (2007) Synthesis, bioactivity, theoretical and molecular docking study of 1-cyano-N-substituted-cyclopropanecarboxamide as ketol-acid reductoisomerase inhibitor. Bioorg. Med. Chem. Lett. 17, 3784-3788
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 3784-3788
    • Liu, X.H.1    Liu, X.H.2    Chen, P.Q.3    Wang, B.L.4    Li, Y.H.5    Wang, S.H.6    Li, Z.M.7
  • 16
    • 57449106562 scopus 로고    scopus 로고
    • Progress in KARI and its inhibitors
    • Liu, X. H. (2008) Progress in KARI and its inhibitors. Progr. Chem. 20, 1788-1797
    • (2008) Progr. Chem. , vol.20 , pp. 1788-1797
    • Liu, X.H.1
  • 17
    • 38049001166 scopus 로고    scopus 로고
    • Non-fermentative pathways for synthesis of branched-chain higher alcohols as biofuels
    • Atsumi, S., Hanai, T. and Liao, J. C. (2008) Non-fermentative pathways for synthesis of branched-chain higher alcohols as biofuels. Nature 451, 86-89
    • (2008) Nature , vol.451 , pp. 86-89
    • Atsumi, S.1    Hanai, T.2    Liao, J.C.3
  • 18
    • 0037466290 scopus 로고    scopus 로고
    • Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa
    • Ahn, H. J., Eom, S. J., Yoon, H. J., Lee, B. I., Cho, H. and Suh, S. W. (2003) Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa. J. Mol. Biol. 328, 505-515
    • (2003) J. Mol. Biol. , vol.328 , pp. 505-515
    • Ahn, H.J.1    Eom, S.J.2    Yoon, H.J.3    Lee, B.I.4    Cho, H.5    Suh, S.W.6
  • 19
    • 0034710671 scopus 로고    scopus 로고
    • A deeply knotted protein structure and how it might fold
    • Taylor, W. R. (2000) A deeply knotted protein structure and how it might fold. Nature 406, 916-919
    • (2000) Nature , vol.406 , pp. 916-919
    • Taylor, W.R.1
  • 20
    • 78651511523 scopus 로고    scopus 로고
    • Structures and folding pathways of topologically knotted proteins
    • Virnau, P., Mallam, A. and Jackson, S. (2011) Structures and folding pathways of topologically knotted proteins. J. Phys. Condens. Matter 23, 033101
    • (2011) J. Phys. Condens. Matter , vol.23 , pp. 033101
    • Virnau, P.1    Mallam, A.2    Jackson, S.3
  • 23
    • 79955164750 scopus 로고    scopus 로고
    • Engineered ketol-acid reductoisomerase and alcohol dehydrogenase enable anaerobic 2-methylpropan-1-ol production at theoretical yield in Escherichia coli
    • Bastian, S., Liu, X., Meyerowitz, J. T., Snow, C. D., Chen, M. M. and Arnold, F. H. (2011) Engineered ketol-acid reductoisomerase and alcohol dehydrogenase enable anaerobic 2-methylpropan-1-ol production at theoretical yield in Escherichia coli. Metab. Eng. 13, 345-352
    • (2011) Metab. Eng. , vol.13 , pp. 345-352
    • Bastian, S.1    Liu, X.2    Meyerowitz, J.T.3    Snow, C.D.4    Chen, M.M.5    Arnold, F.H.6
  • 24
    • 67349187292 scopus 로고    scopus 로고
    • Conformational changes in a plant ketol-acid reductoisomerase upon Mg2+ and NADPH binding as revealed by two crystal structures
    • Leung, E. W. W. and Guddat, L. W. (2009) Conformational changes in a plant ketol-acid reductoisomerase upon Mg2+ and NADPH binding as revealed by two crystal structures. J. Mol. Biol. 389, 167-182
    • (2009) J. Mol. Biol. , vol.389 , pp. 167-182
    • Leung, E.W.W.1    Guddat, L.W.2
  • 25
    • 84869084004 scopus 로고    scopus 로고
    • Bacterial and plant ketol-acid reductoisomerases have different mechanisms of induced fit during the catalytic cycle
    • Wong, S.-H., Lonhienne, T. G., Winzor, D. J., Schenk, G. and Guddat, L. W. (2012) Bacterial and plant ketol-acid reductoisomerases have different mechanisms of induced fit during the catalytic cycle. J. Mol. Biol. 424, 168-179
    • (2012) J. Mol. Biol. , vol.424 , pp. 168-179
    • Wong, S.-H.1    Lonhienne, T.G.2    Winzor, D.J.3    Schenk, G.4    Guddat, L.W.5
  • 26
    • 0027056012 scopus 로고
    • Isolation and kinetic properties of acetohydroxy acid isomeroreductase from spinach (Spinacia oleracea) chloroplasts overexpressed in Escherichia coli
    • Dumas, R., Job, D., Ortholand, J. Y., Emeric, G., Greiner, A. and Douce, R. (1992) Isolation and kinetic properties of acetohydroxy acid isomeroreductase from spinach (Spinacia oleracea) chloroplasts overexpressed in Escherichia coli. Biochem. J. 288, 865-874 PubMed
    • (1992) Biochem. J. , vol.288 , pp. 865-874
    • Dumas, R.1    Job, D.2    Ortholand, J.Y.3    Emeric, G.4    Greiner, A.5    Douce, R.6
  • 27
    • 0032479434 scopus 로고    scopus 로고
    • Characterization of a variant iron protein of nitrogenase that is impaired in its ability to adopt the MgATP-induced conformational change
    • Bursey, E. H. and Burgess, B. K. (1998) Characterization of a variant iron protein of nitrogenase that is impaired in its ability to adopt the MgATP-induced conformational change. J. Biol. Chem. 273, 16927-16934
    • (1998) J. Biol. Chem. , vol.273 , pp. 16927-16934
    • Bursey, E.H.1    Burgess, B.K.2
  • 33
    • 0036793095 scopus 로고    scopus 로고
    • Substructure solution with SHELXD
    • Schneider, T. R. and Sheldrick, G. M. (2002) Substructure solution with SHELXD. Acta Cryst. 58, 1772-1779
    • (2002) Acta Cryst. , vol.58 , pp. 1772-1779
    • Schneider, T.R.1    Sheldrick, G.M.2
  • 38
    • 84871241613 scopus 로고    scopus 로고
    • HELANAL-Plus: A web server for analysis of helix geometry in protein structures
    • Kumar, P. and Bansal, M. (2012) HELANAL-Plus: a web server for analysis of helix geometry in protein structures. J. Biomol. Struct. Dyn. 30, 773-783
    • (2012) J. Biomol. Struct. Dyn. , vol.30 , pp. 773-783
    • Kumar, P.1    Bansal, M.2
  • 39
    • 0030996769 scopus 로고    scopus 로고
    • The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 angstrom resolution
    • Biou, V., Dumas, R., Cohen-Addad, C., Douce, R., Job, D. and Pebay-Peyroula, E. (1997) The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 angstrom resolution. EMBO J. 16, 3405-3415
    • (1997) EMBO J. , vol.16 , pp. 3405-3415
    • Biou, V.1    Dumas, R.2    Cohen-Addad, C.3    Douce, R.4    Job, D.5    Pebay-Peyroula, E.6
  • 40
    • 0034111648 scopus 로고    scopus 로고
    • Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose
    • Thomazeau, K., Dumas, R., Halgand, F., Forest, E., Douce, R. and Biou, V. (2000) Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose. Acta Crystallogr. D Biol. Crystallogr. 56, 389-397
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 389-397
    • Thomazeau, K.1    Dumas, R.2    Halgand, F.3    Forest, E.4    Douce, R.5    Biou, V.6
  • 41
    • 0035014019 scopus 로고    scopus 로고
    • NADP (+) and NAD (+) binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: Different interdomain hinge angles are seen in different binary and ternary complexes
    • Naylor, C. E., Gover, S., Basak, A. K., Cosgrove, M. S., Levy, H. R. and Adams, M. J. (2001) NADP (+) and NAD (+) binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes. Acta Crystallogr. D Biol. Crystallogr. 57, 635-648
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 635-648
    • Naylor, C.E.1    Gover, S.2    Basak, A.K.3    Cosgrove, M.S.4    Levy, H.R.5    Adams, M.J.6
  • 42
    • 0042371815 scopus 로고    scopus 로고
    • Structure of xylose reductase bound to NAD (+) and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases
    • Kavanagh, K. L., Klimacek, M., Nidetzky, B. and Wilson, D. K. (2003) Structure of xylose reductase bound to NAD (+) and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases. Biochem. J. 373, 319-326
    • (2003) Biochem. J. , vol.373 , pp. 319-326
    • Kavanagh, K.L.1    Klimacek, M.2    Nidetzky, B.3    Wilson, D.K.4
  • 43
    • 0037472091 scopus 로고    scopus 로고
    • Dual coenzyme specificity of photosynthetic glyceraldehyde-3-phosphate dehydrogenase interpreted by the crystal structure of A (4) isoform complexed with NAD
    • Falini, G., Fermani, S., Ripamonti, A., Sabatino, P., Sparla, F., Pupillo, P. and Trost, P. (2003) Dual coenzyme specificity of photosynthetic glyceraldehyde-3-phosphate dehydrogenase interpreted by the crystal structure of A (4) isoform complexed with NAD. Biochemistry 42, 4631-4639
    • (2003) Biochemistry , vol.42 , pp. 4631-4639
    • Falini, G.1    Fermani, S.2    Ripamonti, A.3    Sabatino, P.4    Sparla, F.5    Pupillo, P.6    Trost, P.7
  • 44
    • 42949141570 scopus 로고    scopus 로고
    • Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: A structural analysis of dual NAD (P) H specificity
    • Wallen, J. R., Paige, C., Mallett, T. C., Karplus, P. A. and Claiborne, A. (2008) Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD (P) H specificity. Biochemistry 47, 5182-5193
    • (2008) Biochemistry , vol.47 , pp. 5182-5193
    • Wallen, J.R.1    Paige, C.2    Mallett, T.C.3    Karplus, P.A.4    Claiborne, A.5
  • 45
  • 46
    • 84875601072 scopus 로고    scopus 로고
    • Protein insertions and deletions enabled by neutral roaming in sequence space
    • Tóth-Petróczy, Á. and Tawfik, D. S. (2013) Protein insertions and deletions enabled by neutral roaming in sequence space. Mol. Biol. Evol. 30, 761-771
    • (2013) Mol. Biol. Evol. , vol.30 , pp. 761-771
    • Tóth-Petróczy Á.1    Tawfik, D.S.2
  • 47
    • 33845318295 scopus 로고
    • Interaction of pyrophosphate moieties with α-helixes in dinucleotide-binding proteins
    • Wierenga, R. K., De Maeyer, M. C. H. and Hol, W. G. J. (1985) Interaction of pyrophosphate moieties with α-helixes in dinucleotide-binding proteins. Biochemistry 24, 1346-1357
    • (1985) Biochemistry , vol.24 , pp. 1346-1357
    • Wierenga, R.K.1    De Maeyer, M.C.H.2    Hol, W.G.J.3
  • 48
    • 0030906828 scopus 로고    scopus 로고
    • Reversal of the nucleotide specificity of ketol acid reductoisomerase by site-directed mutagenesis identifies the NADPH binding site
    • Rane, M. J. and Calvo, K. C. (1997) Reversal of the nucleotide specificity of ketol acid reductoisomerase by site-directed mutagenesis identifies the NADPH binding site. Arch. Biochem. Biophys. 338, 83-89
    • (1997) Arch. Biochem. Biophys. , vol.338 , pp. 83-89
    • Rane, M.J.1    Calvo, K.C.2
  • 49
    • 28844506786 scopus 로고    scopus 로고
    • The crystal structure of a bacterial class II ketol-acid reductoisomerase: Domain conservation and evolution
    • Tyagi, R., Duquerroy, S., Navaza, J., Guddat, L. W. and Duggleby, R. G. (2005) The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution. Protein Sci. 14, 3089-3100
    • (2005) Protein Sci. , vol.14 , pp. 3089-3100
    • Tyagi, R.1    Duquerroy, S.2    Navaza, J.3    Guddat, L.W.4    Duggleby, R.G.5
  • 50
    • 0037314068 scopus 로고    scopus 로고
    • TopDraw: A sketchpad for protein structure topology cartoons
    • Bond, C. S. (2003) TopDraw: a sketchpad for protein structure topology cartoons. Bioinformatics 19, 311-312
    • (2003) Bioinformatics , vol.19 , pp. 311-312
    • Bond, C.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.