Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans

The NADP-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans (abbreviated Sm-ALDH) belongs to the aldehyde dehydrogenase (ALDH) family. Its catalytic mechanism proceeds via two steps, acylation and deacylation. Its high catalytic efficiency at neutral pH...

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Veröffentlicht in:	Journal of molecular biology 2000-06, Vol.300 (1), p.141-152
Hauptverfasser:	Cobessi, David, Tête-Favier, Frédérique, Marchal, Stéphane, Branlant, Guy, Aubry, André
Format:	Artikel
Sprache:	eng
Schlagworte:	Acylation Aldehyde Dehydrogenase Aldehyde Dehydrogenase - chemistry Aldehyde Dehydrogenase - genetics Aldehyde Dehydrogenase - metabolism ALDH X-ray structure Amino Acid Substitution Amino Acid Substitution - genetics Apoenzymes Apoenzymes - chemistry Apoenzymes - genetics Apoenzymes - metabolism Binding Sites Biochemistry, Molecular Biology Catalysis Crystallography, X-Ray Cysteine Cysteine - genetics Cysteine - metabolism Glutamic Acid Glutamic Acid - metabolism glyceraldehyde-3-phosphate dehydrogenase Holoenzymes Holoenzymes - chemistry Holoenzymes - genetics Holoenzymes - metabolism Hydrogen Bonding Hydrogen-Ion Concentration isotope effect Kinetics Life Sciences Models, Molecular Molecular Sequence Data Mutation Mutation - genetics NADP NADP - metabolism NADP flexibility oxyanion hole Pliability Protein Conformation Streptococcus mutans Streptococcus mutans - enzymology Structural Biology Sulfates Sulfates - metabolism ternary complex
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