1uxt

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spinqualitylabelsall models 1uxt, resolution 2.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURAL BASIS FOR ALLOSTERIC REGULATION AND SUBSTRATE SPECIFICITY OF THE NON-PHOSPHORYLATING GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE (GAPN) FROM THERMOPROTEUS TENAX

Overview

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 Structure

1UXT is a [Single protein] structure of sequence from [Thermoproteus tenax] with G1P, NA and NAD as [ligands]. Active as [[1]], with EC number [1.2.1.9]. Full crystallographic information is available from [OCA].

Reference

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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