Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gene Review:

gapC - extracellular glyceraldehyde-3-phosphate...

Streptococcus mutans UA159

Pailot, A. et al., Marchal, S. et al., Rahuel-Clermont, S. et al., Habenicht, A. et al., Iwami, Y. et al., et al.

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Disease relevance of gapC

Thermal destabilization of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans upon phosphate binding in the active site [1].

High impact information on gapC

Characterization of the amino acids involved in substrate specificity of nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans [2].
The NADP-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans (abbreviated Sm-ALDH) belongs to the aldehyde dehydrogenase (ALDH) family [3].
A cDNA-library has been constructed from Nicotiana plumbaginifolia seedlings, and the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GapN, EC 1.2.1.9) was isolated by plaque hybridization using the cDNA from pea as a heterologous probe [4].
Quantitative analysis of various glycolytic intermediates revealed that the steps inhibited by sucrose monolaurate were the reactions catalyzed by phosphofructokinase and glyceraldehyde 3-phosphate dehydrogenase and/or phosphoglycerate kinase [5].
Invariant Thr(244) is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans [6].

Chemical compound and disease context of gapC

In order to address the molecular basis of the specificity of aldehyde dehydrogenase for aldehyde substrates, enzymatic characterization of the glyceraldehyde 3-phosphate (G3P) binding site of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) from Streptococcus mutans has been undertaken [2].
Catalysis by the NADP-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) from Streptococcus mutans, a member of the aldehyde dehydrogenase (ALDH) family, relies on a local conformational reorganization of the active site [1].
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 [6].

Biological context of gapC

Quantification of glycolytic intermediates revealed that the steps in glycolysis inhibited by chlorhexidine were the reactions catalyzed by phosphofructokinase and glyceraldehyde 3-phosphate dehydrogenase and/or phosphoglycerate kinase [7].

References

Thermal destabilization of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans upon phosphate binding in the active site. Rahuel-Clermont, S., Arutyunov, D., Marchal, S., Orlov, V., Muronetz, V., Branlant, G. J. Biol. Chem. (2005) [Pubmed]
Characterization of the amino acids involved in substrate specificity of nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans. Marchal, S., Branlant, G. J. Biol. Chem. (2002) [Pubmed]
Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans. Cobessi, D., Tête-Favier, F., Marchal, S., Branlant, G., Aubry, A. J. Mol. Biol. (2000) [Pubmed]
Sequence of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Nicotiana plumbaginifolia and phylogenetic origin of the gene family. Habenicht, A., Quesada, A., Cerff, R. Gene (1997) [Pubmed]
Effect of sucrose monolaurate on acid production, levels of glycolytic intermediates, and enzyme activities of Streptococcus mutans NCTC 10449. Iwami, Y., Schachtele, C.F., Yamada, T. J. Dent. Res. (1995) [Pubmed]
Invariant Thr(244) is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans. Pailot, A., D'ambrosio, K., Corbier, C., Talfournier, F., Branlant, G. Biochem. J. (2006) [Pubmed]
Mechanism of inhibition of glycolysis in Streptococcus mutans NCIB 11723 by chlorhexidine. Iwami, Y., Schachtele, C.F., Yamada, T. Oral Microbiol. Immunol. (1995) [Pubmed]

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