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Volumn 1784, Issue 9, 2008, Pages 1248-1255

Physical, kinetic and spectrophotometric studies of a NAD(P)-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633

Author keywords

Aldehyde dehydrogenase; Catalytic thiol; Gene cloning; Mandelate pathway; pH dependence; pKa

Indexed keywords

BENZALDEHYDE DEHYDROGENASE; BENZOIC ACID; CYSTEINE; DISULFIDE; BACTERIAL DNA; BACTERIAL PROTEIN; PRIMER DNA; RECOMBINANT PROTEIN;

EID: 53149151882     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.04.015     Document Type: Article
Times cited : (9)

References (56)
  • 1
    • 0023890672 scopus 로고
    • Microbial metabolism of mandelate: A microcosm of diversity
    • C.A. Fewson, Microbial metabolism of mandelate: a microcosm of diversity, FEMS Microbiol. Rev. 4 (1988) 85-110.
    • (1988) FEMS Microbiol. Rev , vol.4 , pp. 85-110
    • Fewson, C.A.1
  • 2
    • 0001667709 scopus 로고
    • The enzymatic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the soluble enzymes
    • C.F. Gunsalus, R.Y. Stanier, I.C. Gunsalus, The enzymatic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the soluble enzymes, J. Bacteriol. 66 (1953) 548-553.
    • (1953) J. Bacteriol , vol.66 , pp. 548-553
    • Gunsalus, C.F.1    Stanier, R.Y.2    Gunsalus, I.C.3
  • 3
    • 0013892853 scopus 로고
    • Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. I. Synthesis of enzymes by the wild type
    • G.D. Hegeman, Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. I. Synthesis of enzymes by the wild type, J. Bacteriol. 91 (1966) 1140-1154.
    • (1966) J. Bacteriol , vol.91 , pp. 1140-1154
    • Hegeman, G.D.1
  • 4
    • 0024297512 scopus 로고
    • Cloning, DNA sequence analysis, and expression in Escherichia coli of the gene for mandelate racemase from Pseudomonas putida
    • S.C. Ransom, J.A. Gerlt, V.M. Powers, G.L. Kenyon, Cloning, DNA sequence analysis, and expression in Escherichia coli of the gene for mandelate racemase from Pseudomonas putida, Biochemistry 27 (1988) 540-545.
    • (1988) Biochemistry , vol.27 , pp. 540-545
    • Ransom, S.C.1    Gerlt, J.A.2    Powers, V.M.3    Kenyon, G.L.4
  • 5
    • 0025013451 scopus 로고
    • Mandelate pathway of Pseudomonas putida: Sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli
    • A.Y. Tsou, S.C. Ransom, J.A. Gerlt, D.D. Buechter, P.C. Babbitt, G.L. Kenyon, Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli, Biochemistry 29 (1990) 9856-9862.
    • (1990) Biochemistry , vol.29 , pp. 9856-9862
    • Tsou, A.Y.1    Ransom, S.C.2    Gerlt, J.A.3    Buechter, D.D.4    Babbitt, P.C.5    Kenyon, G.L.6
  • 6
    • 85030577685 scopus 로고    scopus 로고
    • A.Y. Tsou, A Study of the Genes Encoding the Enzymes in the Mandelate Pathway in Pseudomonas putida, Department of Chemistry and Biochemistry, University of Maryland, College Park, 1990.
    • A.Y. Tsou, A Study of the Genes Encoding the Enzymes in the Mandelate Pathway in Pseudomonas putida, Department of Chemistry and Biochemistry, University of Maryland, College Park, 1990.
  • 9
    • 0032516465 scopus 로고    scopus 로고
    • The crystal structure of benzoylformate decarboxylase at 1.6 Å resolution: Diversity of catalytic residues in thiamin diphosphate-dependent enzymes
    • M.S. Hasson, A. Muscate, M.J. McLeish, L.S. Polovnikova, J.A. Gerlt, G.L. Kenyon, G.A. Petsko, D. Ringe, The crystal structure of benzoylformate decarboxylase at 1.6 Å resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes, Biochemistry 37 (1998) 9918-9930.
    • (1998) Biochemistry , vol.37 , pp. 9918-9930
    • Hasson, M.S.1    Muscate, A.2    McLeish, M.J.3    Polovnikova, L.S.4    Gerlt, J.A.5    Kenyon, G.L.6    Petsko, G.A.7    Ringe, D.8
  • 10
    • 0025989437 scopus 로고
    • Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-Å resolution: Identification of the active site and possible catalytic residues
    • D.J. Neidhart, P.L. Howell, G.A. Petsko, V.M. Powers, R.S. Li, G.L. Kenyon, J.A. Gerlt, Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-Å resolution: identification of the active site and possible catalytic residues, Biochemistry 30 (1991) 9264-9273.
    • (1991) Biochemistry , vol.30 , pp. 9264-9273
    • Neidhart, D.J.1    Howell, P.L.2    Petsko, G.A.3    Powers, V.M.4    Li, R.S.5    Kenyon, G.L.6    Gerlt, J.A.7
  • 11
    • 0035928723 scopus 로고    scopus 로고
    • Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase
    • N. Sukumar, Y. Xu, D.L. Gatti, B. Mitra, F.S. Mathews, Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase, Biochemistry 40 (2001) 9870-9878.
    • (2001) Biochemistry , vol.40 , pp. 9870-9878
    • Sukumar, N.1    Xu, Y.2    Gatti, D.L.3    Mitra, B.4    Mathews, F.S.5
  • 12
    • 0025941721 scopus 로고
    • Mechanism of the reaction catalyzed by mandelate racemase. 1. Chemical and kinetic evidence for a two-base mechanism
    • V.M. Powers, C.W. Koo, G.L. Kenyon, J.A. Gerlt, J.W. Kozarich, Mechanism of the reaction catalyzed by mandelate racemase. 1. Chemical and kinetic evidence for a two-base mechanism, Biochemistry 30 (1991) 9255-9263.
    • (1991) Biochemistry , vol.30 , pp. 9255-9263
    • Powers, V.M.1    Koo, C.W.2    Kenyon, G.L.3    Gerlt, J.A.4    Kozarich, J.W.5
  • 13
    • 0028901756 scopus 로고
    • Mechanism of the reaction catalyzed by mandelate racemase: Structure and mechanistic properties of the K166R mutant
    • A.T. Kallarakal, B. Mitra, J.W. Kozarich, J.A. Gerlt, J.G. Clifton, G.A. Petsko, G.L. Kenyon, Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant, Biochemistry 34 (1995) 2788-2797.
    • (1995) Biochemistry , vol.34 , pp. 2788-2797
    • Kallarakal, A.T.1    Mitra, B.2    Kozarich, J.W.3    Gerlt, J.A.4    Clifton, J.G.5    Petsko, G.A.6    Kenyon, G.L.7
  • 14
    • 0033564297 scopus 로고    scopus 로고
    • Evidence that pcpA encodes 2,6-dichlorohydroquinone dioxygenase, the ring cleavage enzyme required for pentachlorophenol degradation in Sphingomonas chlorophenolica strain ATCC 39723
    • L. Xu, K. Resing, S.L. Lawson, P.C. Babbitt, S.D. Copley, Evidence that pcpA encodes 2,6-dichlorohydroquinone dioxygenase, the ring cleavage enzyme required for pentachlorophenol degradation in Sphingomonas chlorophenolica strain ATCC 39723, Biochemistry 38 (1999) 7659-7669.
    • (1999) Biochemistry , vol.38 , pp. 7659-7669
    • Xu, L.1    Resing, K.2    Lawson, S.L.3    Babbitt, P.C.4    Copley, S.D.5
  • 15
    • 0242424115 scopus 로고    scopus 로고
    • A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida
    • A.R. Dewanti, B. Mitra, A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida, Biochemistry 42 (2003) 12893-12901.
    • (2003) Biochemistry , vol.42 , pp. 12893-12901
    • Dewanti, A.R.1    Mitra, B.2
  • 16
    • 0034649456 scopus 로고    scopus 로고
    • Spectroscopic detection of transient thiamin diphosphate-bound intermediates on benzoylformate decarboxylase
    • E.A. Sergienko, J. Wang, L. Polovnikova, M.S. Hasson, M.J. McLeish, G.L. Kenyon, F. Jordan, Spectroscopic detection of transient thiamin diphosphate-bound intermediates on benzoylformate decarboxylase, Biochemistry 39 (2000) 13862-13869.
    • (2000) Biochemistry , vol.39 , pp. 13862-13869
    • Sergienko, E.A.1    Wang, J.2    Polovnikova, L.3    Hasson, M.S.4    McLeish, M.J.5    Kenyon, G.L.6    Jordan, F.7
  • 18
    • 2942724459 scopus 로고    scopus 로고
    • Mandelamide hydrolase from Pseudomonas putida: Characterization of a new member of the amidase superfamily
    • K.N. Gopalakrishna, B.H. Stewart, M.M. Kneen, A.D. Andricopulo, G.L. Kenyon, M.J. McLeish, Mandelamide hydrolase from Pseudomonas putida: characterization of a new member of the amidase superfamily, Biochemistry 43 (2004) 7725-7735.
    • (2004) Biochemistry , vol.43 , pp. 7725-7735
    • Gopalakrishna, K.N.1    Stewart, B.H.2    Kneen, M.M.3    Andricopulo, A.D.4    Kenyon, G.L.5    McLeish, M.J.6
  • 21
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • R. Luthy, J.U. Bowie, D. Eisenberg, Assessment of protein models with three-dimensional profiles, Nature 356 (1992) 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 22
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • G. Vriend, WHAT IF: a molecular modeling and drug design program, J. Mol. Graph. 8 (1990) 52-56.
    • (1990) J. Mol. Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying pH-dependent processes
    • K.J. Ellis, J.F. Morrison, Buffers of constant ionic strength for studying pH-dependent processes, Methods Enzymol. 87 (1982) 405-426.
    • (1982) Methods Enzymol , vol.87 , pp. 405-426
    • Ellis, K.J.1    Morrison, J.F.2
  • 28
  • 29
    • 0032534764 scopus 로고    scopus 로고
    • Sheep liver cytosolic aldehyde dehydrogenase: The structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases
    • S.A. Moore, H.M. Baker, T.J. Blythe, K.E. Kitson, T.M. Kitson, E.N. Baker, Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases, Structure 6 (1998) 1541-1551.
    • (1998) Structure , vol.6 , pp. 1541-1551
    • Moore, S.A.1    Baker, H.M.2    Blythe, T.J.3    Kitson, K.E.4    Kitson, T.M.5    Baker, E.N.6
  • 30
    • 0031570328 scopus 로고    scopus 로고
    • Structure of mitochondrial aldehyde dehydrogenase: The genetic component of ethanol aversion
    • C.G. Steinmetz, P. Xie, H. Weiner, T.D. Hurley, Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion, Structure 15 (1997) 701-711.
    • (1997) Structure , vol.15 , pp. 701-711
    • Steinmetz, C.G.1    Xie, P.2    Weiner, H.3    Hurley, T.D.4
  • 32
    • 0032872782 scopus 로고    scopus 로고
    • Differences in the roles of conserved glutamic acid residues in the active site of human class 3 and class 2 aldehyde dehydrogenases
    • C.J. Mann, H. Weiner, Differences in the roles of conserved glutamic acid residues in the active site of human class 3 and class 2 aldehyde dehydrogenases, Protein Sci. 8 (1999) 1922-1929.
    • (1999) Protein Sci , vol.8 , pp. 1922-1929
    • Mann, C.J.1    Weiner, H.2
  • 33
    • 0035969884 scopus 로고    scopus 로고
    • Order and disorder in mitochondrial aldehyde dehydrogenase
    • T.D. Hurley, S. Perez-Miller, H. Breen, Order and disorder in mitochondrial aldehyde dehydrogenase, Chem.-Biol. Interact. 130-132 (2001) 3-14.
    • (2001) Chem.-Biol. Interact , vol.130-132 , pp. 3-14
    • Hurley, T.D.1    Perez-Miller, S.2    Breen, H.3
  • 34
    • 33947424367 scopus 로고    scopus 로고
    • Crystal structures of the carboxyl terminal domain of rat 10-formyltetrahydrofolate dehydrogenase: Implications for the catalytic mechanism of aldehyde dehydrogenases
    • Y. Tsybovsky, H. Donato, N.I. Krupenko, C. Davies, S.A. Krupenko, Crystal structures of the carboxyl terminal domain of rat 10-formyltetrahydrofolate dehydrogenase: implications for the catalytic mechanism of aldehyde dehydrogenases, Biochemistry 46 (2007) 2917-2929.
    • (2007) Biochemistry , vol.46 , pp. 2917-2929
    • Tsybovsky, Y.1    Donato, H.2    Krupenko, N.I.3    Davies, C.4    Krupenko, S.A.5
  • 36
    • 0028958160 scopus 로고
    • Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida
    • J. Inoue, J.P. Shaw, M. Rekik, S. Harayama, Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida, J. Bacteriol. 177 (1995) 1196-1201.
    • (1995) J. Bacteriol , vol.177 , pp. 1196-1201
    • Inoue, J.1    Shaw, J.P.2    Rekik, M.3    Harayama, S.4
  • 37
    • 0027525666 scopus 로고
    • Aldehyde dehydrogenases: Widespread structural and functional diversity within a shared framework
    • J. Hempel, H. Nicholas, R. Lindahl, Aldehyde dehydrogenases: widespread structural and functional diversity within a shared framework, Protein Sci. 2 (1993) 1890-1900.
    • (1993) Protein Sci , vol.2 , pp. 1890-1900
    • Hempel, J.1    Nicholas, H.2    Lindahl, R.3
  • 38
    • 0034817730 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase. Maintaining critical active site geometry at motif 8 in the class 3 enzyme
    • J. Hempel, I. Kuo, J. Perozich, B.C. Wang, R. Lindahl, H. Nicholas, Aldehyde dehydrogenase. Maintaining critical active site geometry at motif 8 in the class 3 enzyme, Eur. J. Biochem. 268 (2001) 722-726.
    • (2001) Eur. J. Biochem , vol.268 , pp. 722-726
    • Hempel, J.1    Kuo, I.2    Perozich, J.3    Wang, B.C.4    Lindahl, R.5    Nicholas, H.6
  • 39
    • 10344242388 scopus 로고    scopus 로고
    • T. Wymore, J. Hempel, S.S. Cho, A.D. Mackerell Jr., H.B. Nicholas Jr., D.W. Deerfield II, Molecular recognition of aldehydes by aldehyde dehydrogenase and mechanism of nucleophile activation, Proteins 57 (2004) 758-771.
    • T. Wymore, J. Hempel, S.S. Cho, A.D. Mackerell Jr., H.B. Nicholas Jr., D.W. Deerfield II, Molecular recognition of aldehydes by aldehyde dehydrogenase and mechanism of nucleophile activation, Proteins 57 (2004) 758-771.
  • 40
    • 34548067148 scopus 로고    scopus 로고
    • Mechanistic implications of the cysteine-nicotinamide adduct in aldehyde dehydrogenase based on quantum mechanical/molecular mechanical simulations
    • T. Wymore, D.W. Deerfield II, J. Hempel, Mechanistic implications of the cysteine-nicotinamide adduct in aldehyde dehydrogenase based on quantum mechanical/molecular mechanical simulations, Biochemistry 46 (2007) 9495-9506.
    • (2007) Biochemistry , vol.46 , pp. 9495-9506
    • Wymore, T.1    Deerfield II, D.W.2    Hempel, J.3
  • 43
    • 0024990842 scopus 로고
    • Purification and characterisation of TOL plasmid-encoded benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase of Pseudomonas putida
    • J.P. Shaw, S. Harayama, Purification and characterisation of TOL plasmid-encoded benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase of Pseudomonas putida, Eur. J. Biochem. 191 (1990) 705-714.
    • (1990) Eur. J. Biochem , vol.191 , pp. 705-714
    • Shaw, J.P.1    Harayama, S.2
  • 44
    • 0024464690 scopus 로고
    • Characterization of rat cornea aldehyde dehydrogenase
    • S. Evces, R. Lindahl, Characterization of rat cornea aldehyde dehydrogenase, Arch. Biochem. Biophys. 274 (1989) 518-524.
    • (1989) Arch. Biochem. Biophys , vol.274 , pp. 518-524
    • Evces, S.1    Lindahl, R.2
  • 45
    • 0034672347 scopus 로고    scopus 로고
    • +-dependent reactions catalysed by betaine aldehyde dehydrogenase from Pseudomonas aeruginosa
    • +-dependent reactions catalysed by betaine aldehyde dehydrogenase from Pseudomonas aeruginosa, Biochem. J. 352 (2000) 675-683.
    • (2000) Biochem. J , vol.352 , pp. 675-683
    • Velasco-Garcia, R.1    Gonzalez-Segura, L.2    Munoz-Clares, R.A.3
  • 46
    • 0031921608 scopus 로고    scopus 로고
    • Cloning and characterization of the Pseudomonas aeruginosa zwf gene encoding glucose-6-phosphate dehydrogenase, an enzyme important in resistance tomethyl viologen (paraquat)
    • J.F. Ma, P.W. Hager, M.L. Howell, P.V. Phibbs, D.J. Hassett, Cloning and characterization of the Pseudomonas aeruginosa zwf gene encoding glucose-6-phosphate dehydrogenase, an enzyme important in resistance tomethyl viologen (paraquat), J. Bacteriol. 180 (1998) 1741-1749.
    • (1998) J. Bacteriol , vol.180 , pp. 1741-1749
    • Ma, J.F.1    Hager, P.W.2    Howell, M.L.3    Phibbs, P.V.4    Hassett, D.J.5
  • 47
    • 0026657646 scopus 로고
    • Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary structure, and expression in Escherichia coli
    • L.C. Hsu, W.C. Chang, A. Shibuya, A. Yoshida, Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary structure, and expression in Escherichia coli, J. Biol. Chem. 267 (1992) 3030-3037.
    • (1992) J. Biol. Chem , vol.267 , pp. 3030-3037
    • Hsu, L.C.1    Chang, W.C.2    Shibuya, A.3    Yoshida, A.4
  • 48
    • 0014430269 scopus 로고
    • Solvent deuterium isotope effects on the glyceraldehyde 3-phosphate dehydrogenase-catalyzed hydrolysis of p-nitrophenyl acetate
    • R.N. Lindquist, E.H. Cordes, Solvent deuterium isotope effects on the glyceraldehyde 3-phosphate dehydrogenase-catalyzed hydrolysis of p-nitrophenyl acetate, J. Biol. Chem. 243 (1968) 5837-5842.
    • (1968) J. Biol. Chem , vol.243 , pp. 5837-5842
    • Lindquist, R.N.1    Cordes, E.H.2
  • 49
    • 0023050188 scopus 로고
    • Studies on the mechanism of sheep liver cytosolic aldehyde dehydrogenase. The effect of pH on the aldehyde binding reactions and a re-examination of the problem of the site of proton release in the mechanism
    • F.M. Dickinson, Studies on the mechanism of sheep liver cytosolic aldehyde dehydrogenase. The effect of pH on the aldehyde binding reactions and a re-examination of the problem of the site of proton release in the mechanism, Biochem. J. 238 (1986) 75-82.
    • (1986) Biochem. J , vol.238 , pp. 75-82
    • Dickinson, F.M.1
  • 51
    • 0033613108 scopus 로고    scopus 로고
    • Evidence for the chemical activation of essential Cys-302 upon cofactor binding to nonphosphorylating glyceraldehyde 3-phosphate dehydrogenase from Streptococcus mutans
    • S. Marchal, G. Branlant, Evidence for the chemical activation of essential Cys-302 upon cofactor binding to nonphosphorylating glyceraldehyde 3-phosphate dehydrogenase from Streptococcus mutans, Biochemistry 38 (1999) 12950-12958.
    • (1999) Biochemistry , vol.38 , pp. 12950-12958
    • Marchal, S.1    Branlant, G.2
  • 53
    • 0015962432 scopus 로고
    • Spectrophotometric determination of mercaptide ion, an activated form of SH-group in thiol enzymes
    • L. Polgár, Spectrophotometric determination of mercaptide ion, an activated form of SH-group in thiol enzymes, FEBS Lett. 38 (1974) 187-190.
    • (1974) FEBS Lett , vol.38 , pp. 187-190
    • Polgár, L.1
  • 54
    • 0036001159 scopus 로고    scopus 로고
    • a values of catalytic groups in enzyme active sites
    • a values of catalytic groups in enzyme active sites, IUBMB Life 53 (2002) 85-98.
    • (2002) IUBMB Life , vol.53 , pp. 85-98
    • Harris, T.K.1    Turner, G.J.2
  • 55
    • 33845743960 scopus 로고    scopus 로고
    • Invariant Thr244 is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans
    • A. Pailot, K. D'Ambrosio, C. Corbier, F. Talfournier, G. Branlant, Invariant Thr244 is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans, Biochem. J. 400 (2006) 521-530.
    • (2006) Biochem. J , vol.400 , pp. 521-530
    • Pailot, A.1    D'Ambrosio, K.2    Corbier, C.3    Talfournier, F.4    Branlant, G.5
  • 56
    • 0037329838 scopus 로고    scopus 로고
    • Ligand-induced conformational changes of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves affecting the reactivity of the catalytic thiol
    • R.A. Muñoz-Clares, L. González-Segura, C. Mújica-Jiménez, L. Contreras-Díaz, Ligand-induced conformational changes of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves affecting the reactivity of the catalytic thiol, Chem.-Biol. Interactions 143-144 (2003) 129-137.
    • (2003) Chem.-Biol. Interactions , vol.143-144 , pp. 129-137
    • Muñoz-Clares, R.A.1    González-Segura, L.2    Mújica-Jiménez, C.3    Contreras-Díaz, L.4


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