The properties and purification from chicken breast muscle of the enzyme diphosphoglycerate mutase which catalyzes the synthesis of D-2,3-diphosphoglyceric acid from D-1,3-diphospho-glyceric acid, are presented in the companion paper (1). Phosphoglyceric acid mutases have been found to be of two types, the better known phosphoglyceric acid mutase which catalyzes Reaction and the recently described (2, 3) mutase which catalyzes Reaction 2, 3-PGA the difference between the two types being in their requirement for 2,3-DPGA. Reactions 1 and 2 have been studied recently with crystalline and highly purified enzyme preparations For clarity, in this paper the enzymes catalyzing these reactions are called 2,3-DPGA dependent mutase and 2,3-DPGA independent mutase. We observed previously that the phosphoglyceric acid mu&se from several tissues, with the exception of that from wheat germ, was stimulated and we found when studying the enzyme diphosphoglycerate mutase that there appeared to be a correlation in several sources between the activity for 2,3-DPGA biosynthesis and the stimulation
Distribution of two types of phosphoglyceric acid mutase, diphosphoglycerate mutase, and D-2,3-diphosphoglyceric acid.
Published 1959 in Journal of Biological Chemistry
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- Publication year
1959
- Venue
Journal of Biological Chemistry
- Publication date
1959-06-01
- Fields of study
Biology, Medicine, Chemistry
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- Source metadata
Semantic Scholar, PubMed
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