Chemical modification of yeast 3-phosphoglycerate kinase.
نویسندگان
چکیده
منابع مشابه
Chemical modification of yeast 3-phosphoglycerate kinase.
Sulfhydryl reagents, as well as mild hydrogen peroxide oxidation, do not inhibit the activity of yeast phosphoglycerate kinase, indicating that the single thiol group and 3 methionine residues present in the enzyme are not essential for activity. Nitration of phosphoglycerate kinase by tetranitromethane inhibits the enzyme by reaction with a single tyrosine residue. Substrates provide partial p...
متن کاملThe active site of yeast phosphoglycerate kinase.
Eby, D. & Kirtley, M. E. (1971) Biochemistry 10,2677-2682 Fuller-Noel, J. K. & Schumaker, V. W. (1972) J. Mol. Biol. 68,523-532 Gennis, L. S. (1976) Proc. Natl. Acad. Sci. U.S.A. 73, 3928-3932 Harrigan, P. J. & Trenthami, D. R. (1971) Biochem. J . 124, 573-580 Hams, J. I. & Polgar, L. (1965) J. Mol. Biol. 14, 630-633 Harris, J. I. & Waters, M. (1976) Enzymes 3rd Ed. 23, 1-50 Kirschner, K. (1971...
متن کاملHuman, yeast and hybrid 3-phosphoglycerate kinase gene expression in yeast.
When the gene for yeast 3-phosphoglycerate kinase (PGK) is present on a high copy number plasmid in Saccharomyces cerevisiae, 30-40 percent of yeast protein is produced as PGK. However, when the structural part of this gene is replaced by as many as twenty different heterologous genes, production of gene products is greatly reduced--usually by more than 20 fold. This decrease in protein product...
متن کاملCrystalline 3-phosphoglycerate kinase from skeletal muscle.
1. A procedure for preparing crystalline 3-phosphoglycerate kinase from rabbit or pig skeletal muscle is presented. 2. The preparation phosphorylates up to 975mumoles of 3-phosphoglycerate/min./mg. at 30 degrees and is not contaminated with myokinase. 3. The enzyme has an estimated molecular weight of 36500+/-1000, and contains three residues each of tyrosine and tryptophan. 4. The preparation ...
متن کاملConversion of yeast phosphoglycerate kinase into amyloid-like structure.
Yeast phosphoglycerate kinase is a structurally well-characterized enzyme consisting of 415 amino acids without disulfide bonds. Anion-induced refolding from its acid-unfolded state gives rise to the formation of worm-like amyloid fibrils with a persistence length of 73 nm. Electron microscopy and small-angle X-ray scattering data indicate that the fibrils have an elliptical cross-section with ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1975
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)41814-0