The mechanism of the phosphoglycerate mutase reaction
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چکیده
منابع مشابه
The active site of yeast phosphoglycerate mutase.
Amdt, U. W., Champness, J. N., Phizackerley, R. P. & Wonawtt, A. J. (1973)J. Appl. Crystallogr. 6,457-463 Banner, D. W., Bloomer, A. C., Petsko, G. A., Phillips, D. C., Pogson, C. I., Wilson, I. A,. Corran, P. H., Furth, A. J., Milman, J. D., Offord, R. E., Priddle, J. D. & Whaley, S. G. (1975) Nature (London) 255,609-614 Harkins, R. N. & Fothergill, L. A. (1977) Biochem. SOC. Trans. 5,772-774 ...
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Rabbit muscle phosphoglycerate mutase, presumed to manifest an absolute cofactor requirement for activity, has been found to express catalysis (3 +/- 1% of optimum) in the absence of added D-glycerate-2,3-P2. Isotope experiments indicate that this catalysis proceeds through a binary phosphoryl enzyme-glycerate intermediate which dissociates into free enzyme and monophosphoglycerate. 32P-Labeled...
متن کاملMechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate.
The structure of the complex between the 2, 3-diphosphoglycerate-independent phosphoglycerate mutase (iPGM) from Bacillus stearothermophilus and its 3-phosphoglycerate substrate has recently been solved, and analysis of this structure allowed formulation of a mechanism for iPGM catalysis. In order to obtain further evidence for this mechanism, we have solved the structure of this iPGM complexed...
متن کاملMuscle phosphoglycerate mutase deficiency revisited.
BACKGROUND Phosphoglycerate mutase (PGAM) deficiency (glycogen storage disease type X) has been reported in 12 patients of whom 9 were African American. OBJECTIVE To describe 2 patients, 1 of Pakistani and 1 of Italian ethnic origin, with typical clinical and biochemical changes of glycogen storage disease type X and novel mutations in the gene encoding the muscle subunit of PGAM (PGAM2). D...
متن کاملThe role of the C-terminal region in phosphoglycerate mutase.
Removal of the C-terminal seven residues from phosphoglycerate mutase from Saccharomyces cerevisiae by limited proteolysis is associated with loss of mutase activity, but no change in phosphatase activity. The presence of the cofactor 2, 3-bisphosphoglycerate, or of the cofactor and substrate 3-phosphoglycerate together, confers protection against proteolysis. The substrate alone offers no prot...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1969
ISSN: 0306-3283
DOI: 10.1042/bj1120010pb