Invariant Thr(244) is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans (310 views visite)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2006 Dec 15; 400: 521-530.
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Paper type Tipo di articolo: Journal Article,
Impact factor: 4.1, 5-year impact factor Impact factor a 5 anni: 4.95
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33845743960&partnerID=40&md5=08df48a13d4de21732b254eaf0e01ba6
Keywords Parole chiave: Acylation Step, Aldehyde Dehydrogenase (aldh), Hydride Transfer, Nicotinamide Conformation, Streptococcus Mutans, X-Ray Structure, Bacteria, Complexation, Hydrogen Bonds, Stereochemistry, Enzymes, Alanine, Cysteine, Glyceraldehyde 3 Phosphate Dehydrogenase, Lysine, Serine, Threonine, Bipyridine, Dithiodipyridine, -Dipyridyl Disulfide, Drug Derivative, Isoenzyme, Nicotinamide Adenine Dinucleotide Phosphate, Amino Acid Substitution, Article, Controlled Study, Crystal Structure, Enzyme Conformation, Enzyme Kinetics, Enzyme Mechanism, Enzyme Phosphorylation, Mutational Analysis, Nonhuman, Ph Measurement, Priority Journal, Steady State, Stereospecificity, Amino Acid Sequence, Binding Site, Enzymology, Genetics, Metabolism, Protein Conformation, Glyceraldehyde-3-Phosphate Dehydrogenases, Hydrogen-Ion Concentration,
Affiliations Affiliazioni:
*** IBB - CNR ***
UMR 7567 Nancy-Université, CNRS, Faculté des Sciences, 54506 Vandoeuvre Cedex, France
Groupe Biocristallographie, UMR 7036 Nancy-Université, Faculté des Sciences, 54506 Vandoeuvre Cedex, France
Istituto di Biostrutture e Bioimmagini, CNR, 80134 Napoli, Italy
References Riferimenti:
Wang, X., Weiner, H., Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis (1995) Biochemistry, 34, pp. 237-24
Marchal, S., Rahuel-Clermont, S., Branlant, G., Role of glutamate-268 in the catalytic mechanism of nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans (2000) Biochemistry, 39, pp. 3327-3335
Vallari, R.C., Pietruszko, R., Kinetic mechanism of the human cytoplasmic aldehyde dehydrogenase E1 (1981) Arch. Biochem. Biophys., 212, pp. 9-19
Shone, C.C., Fromm, H.J., Steady-state and pre-steady-state kinetics of coenzyme A linked aldehyde dehydrogenase from Escherichia coli (1981) Biochemistry, 20, pp. 7494-7501
Söhling, B., Gottschalk, G., Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri (1993) Eur. J. Biochem., 212, pp. 121-127
Farres, J., Wang, T.T., Cunningham, S.J., Weiner, H., Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis (1995) Biochemistry, 34, pp. 2592-2598
Vedadi, M., Szittner, R., Smillie, L., Meighen, E., Involvement of cysteine 289 in the catalytic activity of an NADP +-specific fatty aldehyde dehydrogenase from Vibrio harveyi (1995) Biochemistry, 34, pp. 16725-16732
Vedadi, M., Meighen, E., Critical glutamic acid residues affecting the mechanism and nucleotide specificity of Vibrio harveyi aldehyde dehydrogenase (1997) Eur. J. Biochem., 246, pp. 698-704
Marchal, S., Branlant, G., Evidence for the chemical activation of essential Cys-302 upon cofactor binding to nonphosphorylating glyceraldehyde 3-phosphate dehydrogenase from Streptococcus mutans (1999) Biochemistry, 38, pp. 12950-12958
Steinmetz, C.G., Xie, P., Weiner, H., Hurley, D.T., Structure of mitochondrial aldehyde dehydrogenase: The genetic component of ethanol aversion (1997) Structure, 5, pp. 701-711
Johansson, K., El-Ahmad, M., Ramaswamy, S., Hjelmqvist, L., Jörnvall, H., Eklund, H., Structure of betaine aldehyde dehydrogenase at 2.1 Å resolution (1998) Protein Sci., 7, pp. 2106-2117
Cobessi, D., Tête Favier, F., Marchal, S., Branlant, G., Aubry, A., Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans (2000) J. Mol. Biol., 300, pp. 141-152
Marchal, S., Cobessi, D., Rahuel-Clermont, S., Tete-Favier, F., Aubry, A., Branlant, G., Chemical mechanism and substrate binding sites of NADP-dependent aldehyde dehydrogenase from Streptococcus mutans (2001) Chem. Biol. Interact., 130-132, pp. 15-28
Liu, Z.J., Sun, Y.J., Rose, J., Chung, Y.J., Hsiao, C.D., Chang, W.R., Kuo, I., Wang, B.C., The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold (1997) Nat. Struct. Biol., 4, pp. 317-326
Moore, S.A., Baker, H.M., Blythe, T.J., Kitson, K.E., Kitson, T.M., Baker, E.N., Sheep liver cytosolic aldehyde dehydrogenase: The structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases (1998) Structure, 6, pp. 1541-1551
Perez-Miller, S.J., Hurley, T.D., Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase (2003) Biochemistry, 42, pp. 7100-7109
D'Ambrosio, K., Pailot, A., Talfournier, F., Didierjean, C., Benedetti, E., Aubry, A., Branlant, G., Corbier, C., The first crystal structure of a thioacylenzyme intermediate in the ALDH family: New coenzyme conformation and relevance to catalysis (2006) Biochemistry, 45, pp. 2978-2986
Corbier, C., Mougin, A., Mely, Y., Adolph, H.W., Zeppezauer, M., Gérard, D., Wonacott, A., Branlant, G., The nicotinamide subsite of glyceraldehyde-3-phosphate dehydrogenase studied by site-directed mutagenesis (1990) Biochimie, 72, pp. 545-554
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods Enzymol., 276, pp. 307-326
Brünger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunsteleve, R.W., Jiang, J.S., Pannu, N.S., Crystallography & NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr. Sect. D Biol. Crystallogr., 54, pp. 905-921
noteLaskowsky, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., PROCHECK: A program to check the stereochemical quality of protein structures (1993) J. Appl. Crystallogr., 26, pp. 283-291
Koradi, R., Billeter, M., Wüthrich, K., MOLMOL: A program for display and analysis of macromolecular structures (1996) J. Mol. Graphics, 14, pp. 51-55
Esnouf, R.M., Further additions to MolScript version 1.4, including reading and contouring of electron-density maps (1999) Acta Crystallogr. Sect. D Biol. Crystallogr., 55, pp. 938-940
Stines-Chaumeil, C., Talfournier, F., Branlant, G., Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis (2006) Biochem. J., 395, pp. 107-115
Ni, L., Sheikh, S., Weiner, H., Involvement of glutamate 399 and lysine 192 in the mechanism of human liver mitochondrial aldehyde dehydrogenase (1997) J. Biol. Chem., 272, pp. 18823-18826
Vallari, R. C., Pietruszko, R., Kinetic mechanism of the human cytoplasmic aldehyde dehydrogenase E1 (1981) Arch. Biochem. Biophys., 212, pp. 9-19
Shone, C. C., Fromm, H. J., Steady-state and pre-steady-state kinetics of coenzyme A linked aldehyde dehydrogenase from Escherichia coli (1981) Biochemistry, 20, pp. 7494-7501
S hling, B., Gottschalk, G., Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri (1993) Eur. J. Biochem., 212, pp. 121-127
Steinmetz, C. G., Xie, P., Weiner, H., Hurley, D. T., Structure of mitochondrial aldehyde dehydrogenase: The genetic component of ethanol aversion (1997) Structure, 5, pp. 701-711
Cobessi, D., T te Favier, F., Marchal, S., Branlant, G., Aubry, A., Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans (2000) J. Mol. Biol., 300, pp. 141-152
Liu, Z. J., Sun, Y. J., Rose, J., Chung, Y. J., Hsiao, C. D., Chang, W. R., Kuo, I., Wang, B. C., The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold (1997) Nat. Struct. Biol., 4, pp. 317-326
Moore, S. A., Baker, H. M., Blythe, T. J., Kitson, K. E., Kitson, T. M., Baker, E. N., Sheep liver cytosolic aldehyde dehydrogenase: The structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases (1998) Structure, 6, pp. 1541-1551
Perez-Miller, S. J., Hurley, T. D., Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase (2003) Biochemistry, 42, pp. 7100-7109
Br nger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunsteleve, R. W., Jiang, J. S., Pannu, N. S., Crystallography & NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr. Sect. D Biol. Crystallogr., 54, pp. 905-921
noteLaskowsky, R. A., MacArthur, M. W., Moss, D. S., Thornton, J. M., PROCHECK: A program to check the stereochemical quality of protein structures (1993) J. Appl. Crystallogr., 26, pp. 283-291
Esnouf, R. M., Further additions to MolScript version 1. 4, including reading and contouring of electron-density maps (1999) Acta Crystallogr. Sect. D Biol. Crystallogr., 55, pp. 938-940
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2006 Dec 15; 400: 521-530.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 4.1, 5-year impact factor Impact factor a 5 anni: 4.95
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33845743960&partnerID=40&md5=08df48a13d4de21732b254eaf0e01ba6
Keywords Parole chiave: Acylation Step, Aldehyde Dehydrogenase (aldh), Hydride Transfer, Nicotinamide Conformation, Streptococcus Mutans, X-Ray Structure, Bacteria, Complexation, Hydrogen Bonds, Stereochemistry, Enzymes, Alanine, Cysteine, Glyceraldehyde 3 Phosphate Dehydrogenase, Lysine, Serine, Threonine, Bipyridine, Dithiodipyridine, -Dipyridyl Disulfide, Drug Derivative, Isoenzyme, Nicotinamide Adenine Dinucleotide Phosphate, Amino Acid Substitution, Article, Controlled Study, Crystal Structure, Enzyme Conformation, Enzyme Kinetics, Enzyme Mechanism, Enzyme Phosphorylation, Mutational Analysis, Nonhuman, Ph Measurement, Priority Journal, Steady State, Stereospecificity, Amino Acid Sequence, Binding Site, Enzymology, Genetics, Metabolism, Protein Conformation, Glyceraldehyde-3-Phosphate Dehydrogenases, Hydrogen-Ion Concentration,
Affiliations Affiliazioni:
*** IBB - CNR ***
UMR 7567 Nancy-Université, CNRS, Faculté des Sciences, 54506 Vandoeuvre Cedex, France
Groupe Biocristallographie, UMR 7036 Nancy-Université, Faculté des Sciences, 54506 Vandoeuvre Cedex, France
Istituto di Biostrutture e Bioimmagini, CNR, 80134 Napoli, Italy
References Riferimenti:
Wang, X., Weiner, H., Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis (1995) Biochemistry, 34, pp. 237-24
Marchal, S., Rahuel-Clermont, S., Branlant, G., Role of glutamate-268 in the catalytic mechanism of nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans (2000) Biochemistry, 39, pp. 3327-3335
Vallari, R.C., Pietruszko, R., Kinetic mechanism of the human cytoplasmic aldehyde dehydrogenase E1 (1981) Arch. Biochem. Biophys., 212, pp. 9-19
Shone, C.C., Fromm, H.J., Steady-state and pre-steady-state kinetics of coenzyme A linked aldehyde dehydrogenase from Escherichia coli (1981) Biochemistry, 20, pp. 7494-7501
Söhling, B., Gottschalk, G., Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri (1993) Eur. J. Biochem., 212, pp. 121-127
Farres, J., Wang, T.T., Cunningham, S.J., Weiner, H., Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis (1995) Biochemistry, 34, pp. 2592-2598
Vedadi, M., Szittner, R., Smillie, L., Meighen, E., Involvement of cysteine 289 in the catalytic activity of an NADP +-specific fatty aldehyde dehydrogenase from Vibrio harveyi (1995) Biochemistry, 34, pp. 16725-16732
Vedadi, M., Meighen, E., Critical glutamic acid residues affecting the mechanism and nucleotide specificity of Vibrio harveyi aldehyde dehydrogenase (1997) Eur. J. Biochem., 246, pp. 698-704
Marchal, S., Branlant, G., Evidence for the chemical activation of essential Cys-302 upon cofactor binding to nonphosphorylating glyceraldehyde 3-phosphate dehydrogenase from Streptococcus mutans (1999) Biochemistry, 38, pp. 12950-12958
Steinmetz, C.G., Xie, P., Weiner, H., Hurley, D.T., Structure of mitochondrial aldehyde dehydrogenase: The genetic component of ethanol aversion (1997) Structure, 5, pp. 701-711
Johansson, K., El-Ahmad, M., Ramaswamy, S., Hjelmqvist, L., Jörnvall, H., Eklund, H., Structure of betaine aldehyde dehydrogenase at 2.1 Å resolution (1998) Protein Sci., 7, pp. 2106-2117
Cobessi, D., Tête Favier, F., Marchal, S., Branlant, G., Aubry, A., Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans (2000) J. Mol. Biol., 300, pp. 141-152
Marchal, S., Cobessi, D., Rahuel-Clermont, S., Tete-Favier, F., Aubry, A., Branlant, G., Chemical mechanism and substrate binding sites of NADP-dependent aldehyde dehydrogenase from Streptococcus mutans (2001) Chem. Biol. Interact., 130-132, pp. 15-28
Liu, Z.J., Sun, Y.J., Rose, J., Chung, Y.J., Hsiao, C.D., Chang, W.R., Kuo, I., Wang, B.C., The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold (1997) Nat. Struct. Biol., 4, pp. 317-326
Moore, S.A., Baker, H.M., Blythe, T.J., Kitson, K.E., Kitson, T.M., Baker, E.N., Sheep liver cytosolic aldehyde dehydrogenase: The structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases (1998) Structure, 6, pp. 1541-1551
Perez-Miller, S.J., Hurley, T.D., Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase (2003) Biochemistry, 42, pp. 7100-7109
D'Ambrosio, K., Pailot, A., Talfournier, F., Didierjean, C., Benedetti, E., Aubry, A., Branlant, G., Corbier, C., The first crystal structure of a thioacylenzyme intermediate in the ALDH family: New coenzyme conformation and relevance to catalysis (2006) Biochemistry, 45, pp. 2978-2986
Corbier, C., Mougin, A., Mely, Y., Adolph, H.W., Zeppezauer, M., Gérard, D., Wonacott, A., Branlant, G., The nicotinamide subsite of glyceraldehyde-3-phosphate dehydrogenase studied by site-directed mutagenesis (1990) Biochimie, 72, pp. 545-554
Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods Enzymol., 276, pp. 307-326
Brünger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunsteleve, R.W., Jiang, J.S., Pannu, N.S., Crystallography & NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr. Sect. D Biol. Crystallogr., 54, pp. 905-921
noteLaskowsky, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., PROCHECK: A program to check the stereochemical quality of protein structures (1993) J. Appl. Crystallogr., 26, pp. 283-291
Koradi, R., Billeter, M., Wüthrich, K., MOLMOL: A program for display and analysis of macromolecular structures (1996) J. Mol. Graphics, 14, pp. 51-55
Esnouf, R.M., Further additions to MolScript version 1.4, including reading and contouring of electron-density maps (1999) Acta Crystallogr. Sect. D Biol. Crystallogr., 55, pp. 938-940
Stines-Chaumeil, C., Talfournier, F., Branlant, G., Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis (2006) Biochem. J., 395, pp. 107-115
Ni, L., Sheikh, S., Weiner, H., Involvement of glutamate 399 and lysine 192 in the mechanism of human liver mitochondrial aldehyde dehydrogenase (1997) J. Biol. Chem., 272, pp. 18823-18826
Vallari, R. C., Pietruszko, R., Kinetic mechanism of the human cytoplasmic aldehyde dehydrogenase E1 (1981) Arch. Biochem. Biophys., 212, pp. 9-19
Shone, C. C., Fromm, H. J., Steady-state and pre-steady-state kinetics of coenzyme A linked aldehyde dehydrogenase from Escherichia coli (1981) Biochemistry, 20, pp. 7494-7501
S hling, B., Gottschalk, G., Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri (1993) Eur. J. Biochem., 212, pp. 121-127
Steinmetz, C. G., Xie, P., Weiner, H., Hurley, D. T., Structure of mitochondrial aldehyde dehydrogenase: The genetic component of ethanol aversion (1997) Structure, 5, pp. 701-711
Cobessi, D., T te Favier, F., Marchal, S., Branlant, G., Aubry, A., Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans (2000) J. Mol. Biol., 300, pp. 141-152
Liu, Z. J., Sun, Y. J., Rose, J., Chung, Y. J., Hsiao, C. D., Chang, W. R., Kuo, I., Wang, B. C., The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold (1997) Nat. Struct. Biol., 4, pp. 317-326
Moore, S. A., Baker, H. M., Blythe, T. J., Kitson, K. E., Kitson, T. M., Baker, E. N., Sheep liver cytosolic aldehyde dehydrogenase: The structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases (1998) Structure, 6, pp. 1541-1551
Perez-Miller, S. J., Hurley, T. D., Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase (2003) Biochemistry, 42, pp. 7100-7109
Br nger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunsteleve, R. W., Jiang, J. S., Pannu, N. S., Crystallography & NMR system: A new software suite for macromolecular structure determination (1998) Acta Crystallogr. Sect. D Biol. Crystallogr., 54, pp. 905-921
noteLaskowsky, R. A., MacArthur, M. W., Moss, D. S., Thornton, J. M., PROCHECK: A program to check the stereochemical quality of protein structures (1993) J. Appl. Crystallogr., 26, pp. 283-291
Esnouf, R. M., Further additions to MolScript version 1. 4, including reading and contouring of electron-density maps (1999) Acta Crystallogr. Sect. D Biol. Crystallogr., 55, pp. 938-940
Invariant Thr(244) is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans
One of the most striking features of several X-ray structures of CoA-independent ALDHs (aldehyde dehydrogenases) in complex with NAD(P) is the conformational flexibility of the NMN moiety. However, the fact that the rate of the acylation step is high in GAPN (non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase) from Streptococcus mutans implies an optimal positioning of the nicotinamide ring relative to the hemithioacetal intermediate within the ternary GAPN complex to allow an efficient and stereospecific hydride transfer. Substitutions of serine for invariant Thr(244) and alanine for Lys(178) result in a drastic decrease of the efficiency of hydride transfer which becomes rate-limiting. The crystal structure of the binary complex T244S GAPN-NADP shows that the absence of the P-methyl group leads to a well-defined conformation of the NMN part, including the nicotinamide ring, clearly different from that depicted to be suitable for an efficient hydride transfer in the wild-type. The similar to 0.6-unit increase in pK(app) of the catalytic Cys(302) observed in the ternary complex for both mutated GAPNs is likely to be due to a slight difference in positioning of the nicotinamide ring relative to Cys(302) with respect to the wild-type ternary complex. Taken together, the data support a critical role of the Thr(244) beta-methyl group, held in position through a hydrogen-bond interaction between the Thr(244) beta-hydroxy group and the epsilon-amino group of Lys(178), in permitting the nicotinamide ring to adopt a conformation suitable for an efficient hydride transfer during the acylation step for all the members of the CoA-independent ALDH family.
One of the most striking features of several X-ray structures of CoA-independent ALDHs (aldehyde dehydrogenases) in complex with NAD(P) is the conformational flexibility of the NMN moiety. However, the fact that the rate of the acylation step is high in GAPN (non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase) from Streptococcus mutans implies an optimal positioning of the nicotinamide ring relative to the hemithioacetal intermediate within the ternary GAPN complex to allow an efficient and stereospecific hydride transfer. Substitutions of serine for invariant Thr(244) and alanine for Lys(178) result in a drastic decrease of the efficiency of hydride transfer which becomes rate-limiting. The crystal structure of the binary complex T244S GAPN-NADP shows that the absence of the P-methyl group leads to a well-defined conformation of the NMN part, including the nicotinamide ring, clearly different from that depicted to be suitable for an efficient hydride transfer in the wild-type. The similar to 0.6-unit increase in pK(app) of the catalytic Cys(302) observed in the ternary complex for both mutated GAPNs is likely to be due to a slight difference in positioning of the nicotinamide ring relative to Cys(302) with respect to the wild-type ternary complex. Taken together, the data support a critical role of the Thr(244) beta-methyl group, held in position through a hydrogen-bond interaction between the Thr(244) beta-hydroxy group and the epsilon-amino group of Lys(178), in permitting the nicotinamide ring to adopt a conformation suitable for an efficient hydride transfer during the acylation step for all the members of the CoA-independent ALDH family.
Invariant Thr(244) is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans
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Invariant Thr(244) is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans
Merlino A, Russo Krauss I, Rossi B, De Vendittis A, Marco S, De Vendittis E, Vergara A, Sica F
* Identification of an active dimeric intermediate populated during the unfolding process of the cambialistic superoxide dismutase from Streptococcus mutans (307 visite)
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2012 Mar; 94(3): 768-775.
Impact Factor: 3.142
Dettagli Esporta in BibTeX Esporta in EndNote
Pennacchio A, Giordano A, Esposito L, Langella E, Rossi M, Raia CA
* Insight into the stereospecificity of short-chain Thermus thermophilus alcohol dehydrogenase showing pro-S hydride transfer and Prelog enantioselectivity (427 visite)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2010 Apr; 17(4): 437-443.
Impact Factor: 1.849
Dettagli Esporta in BibTeX Esporta in EndNote
D'Ambrosio K, Pailot A, Talfournier F, Didierjean C, Benedetti E, Aubry A, Branlant G, Corbier C
* The first crystal structure of a thioacylenzyme intermediate in the ALDH family: New coenzyme conformation and relevance to catalysis (339 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2006 Mar 7; 45(9): 2978-2986.
Impact Factor: 3.633
Dettagli Esporta in BibTeX Esporta in EndNote
3 Records (3 escludendo Abstract e Conferenze).
Impact factor totale: 8.624 (8.624 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 8.109 (8.109 escludendo Abstract e Conferenze).
Vai a fine pagina Versione per copia e incolla facile Esporta tutto in BibTeX Esporta tutto in EndNote
Merlino A, Russo Krauss I, Rossi B, De Vendittis A, Marco S, De Vendittis E, Vergara A, Sica F
* Identification of an active dimeric intermediate populated during the unfolding process of the cambialistic superoxide dismutase from Streptococcus mutans (307 visite)
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2012 Mar; 94(3): 768-775.
Impact Factor: 3.142
Dettagli Esporta in BibTeX Esporta in EndNote
Pennacchio A, Giordano A, Esposito L, Langella E, Rossi M, Raia CA
* Insight into the stereospecificity of short-chain Thermus thermophilus alcohol dehydrogenase showing pro-S hydride transfer and Prelog enantioselectivity (427 visite)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2010 Apr; 17(4): 437-443.
Impact Factor: 1.849
Dettagli Esporta in BibTeX Esporta in EndNote
D'Ambrosio K, Pailot A, Talfournier F, Didierjean C, Benedetti E, Aubry A, Branlant G, Corbier C
* The first crystal structure of a thioacylenzyme intermediate in the ALDH family: New coenzyme conformation and relevance to catalysis (339 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2006 Mar 7; 45(9): 2978-2986.
Impact Factor: 3.633
Dettagli Esporta in BibTeX Esporta in EndNote
3 Records (3 escludendo Abstract e Conferenze).
Impact factor totale: 8.624 (8.624 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 8.109 (8.109 escludendo Abstract e Conferenze).
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