The active site of yeast phosphoglycerate mutase.
نویسندگان
چکیده
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 Kayne, F. J. (1973) Enzymes 3rd Ed. 8, 353-382 Levitt, M. & Chothia, C. (1976) Nature (London) 261, 552-558 Mildvan, A. S., Sloan, D. L., Fung, C. H., Gupta, R. K. & Melamud, E. (1976)J. Biol. Chem.
منابع مشابه
Active site phosphohistidine peptides from red cell bisphosphoglycerate synthase and yeast phosphoglycerate mutase.
Bisphosphoglycerate synthase (glycerate-1,3-P2 yields glycerate-2,3-P2) and phosphoglycerate mutase (glycerate-3-P formed from glycerate-2-P) are both phosphorylated by substrates at a histidine residue forming covalent intermediates which have been shown to function in the phosphoryl transfer reactions catalyzed by these enzymes (Rose, Z. B., and Dube, S. (1976) J. Biol. Chem. 251, 4817--4822)...
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To date no definite and undisputed treatment has been found for sickle cell anemia, which is characterized by polymerization of a deoxygenated hemoglobin mutant (HbS) giving rise to deformed erythrocytes and vasoocclusive complications. Since the erythrocyte glycerate 2,3-bisphosphate (2,3-DPG) has been shown to facilitate this polymerization, one therapeutic approach would be to decrease the i...
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The human 2,3-bisphosphoglycerate mutase gene was isolated from genomic libraries and analyzed by Southern blots and DNA sequencing. The transcription initiation site was localized by primer extension as well as by S1 protection of the mRNA. The gene extends over 22 kilobase pairs; it is composed of two introns (8.8 and 11.5 kilobase pairs long) and three exons (84, 662, and 965 base pairs long...
متن کاملThe amino acid sequence of the small monomeric phosphoglycerate mutase from the fission yeast Schizosaccharomyces pombe.
The amino acid sequence of the monomeric 2,3-bisphosphoglycerate (BPG)-dependent phosphoglycerate mutase (PGAM) from the fission yeast Schizosaccharomyces pombe has been determined. Amino acid sequencing of proteolytic fragments of the enzyme showed the S. pombe mutase to be similar in sequence to the tetrameric enzyme of baker's yeast (Saccharomyces cerevisiae). An S. pombe cDNA library was sc...
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ورودعنوان ژورنال:
- Biochemical Society transactions
دوره 5 3 شماره
صفحات -
تاریخ انتشار 1977