MECHANISM OF THE PHOSPHOGLYCERIC MUTASE REACTION
نویسندگان
چکیده
منابع مشابه
Distribution of two types of phosphoglyceric acid mutase, diphosphoglycerate mutase, and D-2,3-diphosphoglyceric acid.
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 (3-5). For clarity, in this paper the enzymes catalyzing these reactions are called 2,3DPGA dependent mutase and 2,3-DPGA independent mutase. We observed previously that the phosphoglyceric acid mu&se from several tis...
متن کاملStructure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A.
The crystal structure of the tetrameric glycolytic enzyme phosphoglycerate mutase from the yeast Saccharomyces cerevisiae has been determined to 1.7 A resolution in complex with the sugar substrate. The difference map indicates that 3-phosphoglycerate is bound at the base of a 12 A cleft, positioning C2 of the substrate within 3.5 A of the primary catalytic residue, histidine 8.
متن کاملStereochemistry of the glutamate mutase reaction.
4-Deuterioglutamic acid was prepared by incubation in DzO of ammonium mesaconate with an extract of Clostri&urn tetanomorphum. In these extracts, methylaspartase catalyzed the formation of threo-3-methyl-L-aspartate-3-D, which was then rearranged to glutamate by the cobamide coenzyme-dependent glutamate mutase. The monodeuteriosuccinate obtained by chloramine-T oxidation of the glutamate showed...
متن کاملThe mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme.
Molecular dynamics studies of the Escherichia coli chorismate mutase (EcCM), containing at the active site chorismate and in turn the transition state (TS), have been performed. The simulations show that TS is not bound any tighter than chorismate. Comparison of average polar interactions show they are virtually identical for interactions of EcCM with chorismate and the TS, whereas hydrophobic ...
متن کاملPhosphoglyceric acid mutase activity without added 2,3-diphosphoglycerate in preparations purified from wheat germ.
The phosphoglyceric acid mutases from Baker’s yeast and rabbit skeletal muscle have been crystallized or highly purified in this laboratory, and a comparative study of the kinetic and molecular properties has been conducted (l-3). The phosphoglyceric acid mutases from these two sources as well as from many others (2, 4) are stimulated by catalytic amounts of 2,3-diphosphoglyceric acid, as was o...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1949
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)56636-9