1uxq
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STRUCTURAL BASIS FOR ALLOSTERIC REGULATION AND SUBSTRATE SPECIFICITY OF THE NON-PHOSPHORYLATING GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE (GAPN) FROM THERMOPROTEUS TENAX
OverviewOverview
The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) of, the hyperthermophilic Archaeum Thermoproteus tenax is a member of the, superfamily of aldehyde dehydrogenases (ALDH). GAPN catalyses the, irreversible oxidation of glyceraldehyde 3-phosphate (GAP) to, 3-phosphoglycerate in the modified glycolytic pathway of this organism. In, contrast to other members of the ALDH superfamily, GAPN from T.tenax, (Tt-GAPN) is regulated by a number of intermediates and metabolites. In, the NAD-dependent oxidation of GAP, glucose 1-phosphate, fructose, 6-phosphate, AMP and ADP increase the affinity for the cosubstrate, whereas ATP, NADP, NADPH and NADH decrease it leaving, however, the, catalytic rate virtually unaltered. As we show here, the enzyme also uses, NADP as a cosubstrate, ... [(full description)]
About this StructureAbout this Structure
1UXQ is a [Single protein] structure of sequence from [Thermoproteus tenax] with G1P, NA and NAP as [ligands]. Active as [[1]], with EC number [1.2.1.9]. Full crystallographic information is available from [OCA].
ReferenceReference
Structural Basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-Phosphate dehydrogenase from Thermoproteus tenax., Lorentzen E, Hensel R, Knura T, Ahmed H, Pohl E, J Mol Biol. 2004 Aug 13;341(3):815-28. PMID:15288789
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