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. 1972 Feb;109(2):751–756. doi: 10.1128/jb.109.2.751-756.1972

3-Phosphoglycerate Kinase from Hydrogenomonas facilis

Bruce A McFadden a, Erwin Schuster a,1
PMCID: PMC285201  PMID: 4621685

Abstract

Phosphoglycerate kinase levels in Hydrogenomonas facilis were reasonably constant whether cells were utilizing or synthesizing hexose during growth. Specific enzyme activities (micromoles of 3-phosphoglycerate disappearing per minute per milligram of protein) at 30 C were 0.234, 0.391, 0.300, and 0.229 in the “soluble” fraction derived from cells grown on fructose, lactate, succinate, and glutamate, respectively. The enzyme was purified 300-fold from succinate-grown cells. The final preparation, which was not homogenous but was free from glyceraldehyde-3-phosphate dehydrogenase and adenylate kinase, had a specific activity at 30 C of 90 μmoles of 3-phosphoglycerate per min per mg of protein. Km values for adenosine triphosphate (ATP), 3-phosphoglycerate, and Mg++ were 0.16, 0.83, and 0.4 mm, respectively, at pH 7.4 and 30 C. Adenosine monophosphate (AMP) inhibited 23% at a ratio of AMP to ATP of 2.4, and the possible physiological implications of this inhibition are discussed. No evidence was found for an enzyme which catalyzes ATP-dependent conversion of 3-phosphoglycerate to 1,3-diphosphoglycerate, AMP, and phosphate.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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