Invariant Thr(244) is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans
Invariant Thr(244) is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans(259 views visite) Pailot A, D'Ambrosio K, Corbier C, Talfournier F, Branlant G
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
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Perez-Miller, S. J., Hurley, T. D., Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase (2003) Biochemistry, 42, pp. 7100-7109
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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
Invariant Thr(244) is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans
Kim YH, Shin SW, Pellicano R, Fagoonee S, Choi IJ, Kim YI, Park B, Choi JM, Kim SG, Choi J, Park JY, Oh S, Yang HJ, Lim JH, Im JP, Kim JS, Jung HC, Ponzetto A, Figura N, Malfertheiner P, Choi IJ, Kook MC, Kim YI, Cho SJ, Lee JY, Kim CG, Park B, Nam BH, Bae SE, Choi KD, Choe J, Kim SO, Na HK, Choi JY, Ahn JY, Jung KW, Lee J, Kim DH, Chang HS, Song HJ, Lee GH, Jung HY, Seta T, Takahashi Y, Noguchi Y, Shikata S, Sakai T, Sakai K, Yamashita Y, Nakayama T, Leja M, Park JY, Murillo R, Liepniece-karele I, Isajevs S, Kikuste I, Rudzite D, Krike P, Parshutin S, Polaka I, Kirsners A, Santare D, Folkmanis V, Daugule I, Plummer M, Herrero R, Tsukamoto T, Nakagawa M, Kiriyama Y, Toyoda T, Cao X, Corral JE, Mera R, Dye CW, Morgan DR, Lee YC, Lin JT, Garcia Martin R, Matia Cubillo A, Lee SH, Park JM, Han YM, Ko WJ, Hahm KB, Leontiadis GI, Ford AC, Ichinose M, Sugano K, Jeong M, Park JM, Han YM, Park KY, Lee DH, Yoo JH, Cho JY, Hahm KB, Bang CS, Baik GH, Shin IS, Kim JB, Suk KT, Yoon JH, Kim YS, Kim DJ * Helicobacter pylori Eradication for Prevention of Metachronous Recurrence after Endoscopic Resection of Early Gastric Cancer(204 visite) N Engl J Med (ISSN: 0028-4793, 0028-4793linking, 1533-4406electronic), 2015 Jun; 30642104201566393291: 749-756. Impact Factor:59.558 DettagliEsporta in BibTeXEsporta in EndNote
246 Records (245 escludendo Abstract e Conferenze). Impact factor totale: 983.053 (978.702 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 997.863 (993.48 escludendo Abstract e Conferenze).
Last modified by Ultima modifica di Marco Comerci on in data Sunday 12 July 2020, 13:15:06 259 views visite. Last view on Ultima visita in data Friday 18 December 2020, 11:52:47