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 (338 views)

Pailot A, D'Ambrosio K, Corbier C, Talfournier F, Branlant G

Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2006 Dec 15; 400: 521-530.

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Paper type: Journal Article,

Impact factor: 4.1, 5-year impact factor: 4.95

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33845743960&partnerID=40&md5=08df48a13d4de21732b254eaf0e01ba6

Keywords: 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:
*** 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


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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.
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

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* The first crystal structure of a thioacylenzyme intermediate in the ALDH family: New coenzyme conformation and relevance to catalysis (388 views)
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Last modified by Marco Comerci on Sunday 12 July 2020, 13:15:06
338 views. Last view on Sunday 19 February 2023, 6:53:45