Geobacillus stearothermophilus6-phosphogluconate dehydrogenase complexed with 6-phosphogluconate

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Geobacillus stearothermophilus 6-phosphogluconate dehydrogenase complexed with 6-phosphogluconate

Two crystal structures of recombinant Geobacillus stearothermophilus 6-phosphogluconate dehydrogenase (Gs6PDH) in complex with the substrate 6-phosphogluconate have been determined at medium resolution. Gs6PDH shares significant sequence identity and structural similarity with the enzymes from Lactococcus lactis, sheep liver and the protozoan parasite Trypanosoma brucei, for which a range of st...

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6-Phosphogluconate dehydrogenase from leuconostoc mesenteroides.

The pathways for degradation of 6-phosphogluconate have been rather clearly defined for several organisms, the most notable of which are yeast (Horecker, 1953), Escherichia coli (Cohen, 1951), Pseudomonas saccharophila (Entner and Doudoroff, 1952; MacGee and Doudoroff, 1954), and Pseudomonas fluorescens (Kovachevich and Wood, 1954). The enzymes from yeast and E. coli appear to be similar, if no...

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Dietary regulation of 6-phosphogluconate dehydrogenase synthesis.

The relative rates of synthesis and degradation for rat liver 6-phosphogluconate dehydrogenase have been determined in animals maintained at several dietary states. Relative rates of synthesis were determined by pulse-labeling the enzyme either in live rats and determining the radioactivity in the purified enzyme or in whole cell suspensions of hepatocytes followed by precipitation of the enzym...

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6-Phosphogluconate dehydrogenase mechanism: evidence for allosteric modulation by substrate.

The reductive carboxylation of ribulose-5-phosphate (Ru5P) by 6-phosphogluconate dehydrogenase (6PGDH) from Candida utilis was investigated using kinetic isotope effects. The intrinsic isotope effect for proton abstraction from Ru5P was found at 4.9 from deuterium isotope effects on V and V/K and from tritium isotope effects on V/K. The presence of 6-phosphogluconate (6PG) in the assay mixture ...

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The Mechanism of Action of 6-phosphogluconate Dehydrogenase.

6-Phosphogluconate dehydrogenase from Candida utilis catalyzes the oxidative decarboxylation of 2-deoxy-6-phosphogluconate. The 3-keto-2-deoxy-6-phosphogluconate, an intermediate of the reaction, is reduced to 2-deoxy-6-phosphogluconate and decarboxylated to I-deoxyribulose 5-phosphate when incubated with the enzyme and TPNH. The decarboxylation process does not occur in the absence of the redu...

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ژورنال

عنوان ژورنال: Acta Crystallographica Section F Structural Biology and Crystallization Communications

سال: 2009

ISSN: 1744-3091

DOI: 10.1107/s1744309109012767