MgF3− and AlF4− transition state analogue complexes of yeast phosphoglycerate kinase
نویسندگان
چکیده
منابع مشابه
A Trojan horse transition state analogue generated by MgF3- formation in an enzyme active site.
Identifying how enzymes stabilize high-energy species along the reaction pathway is central to explaining their enormous rate acceleration. beta-Phosphoglucomutase catalyses the isomerization of beta-glucose-1-phosphate to beta-glucose-6-phosphate and appeared to be unique in its ability to stabilize a high-energy pentacoordinate phosphorane intermediate sufficiently to be directly observable i...
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A specific class of anions inhibit creatine kinase by stabilizing the dead-end complex, enzymedivalent cation*ADP*creatine (Watts, D. C. (1973) The Enzymes 8, 383-455). The inhibitory action o? the anions is attributed to the ability of the anions to mimic the equatorial PO3 plane formed by the migrating phosphoryl group in the transition state of the reaction. Infrared spectroscopy has been us...
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...
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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 کامل1H, 15N, 13C backbone resonance assignments of human phosphoglycerate kinase in a transition state analogue complex with ADP, 3-phosphoglycerate and magnesium trifluoride
Human phosphoglycerate kinase (PGK) is an energy generating glycolytic enzyme that catalyses the transfer of a phosphoryl group from 1,3-bisphosphoglycerate (BPG) to ADP producing 3-phosphoglycerate (3PG) and ATP. PGK is composed of two α/β Rossmann-fold domains linked by a central α-helix and the active site is located in the cleft formed between the N-domain which binds BPG or 3PG, and the C-...
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ژورنال
عنوان ژورنال: Biochemistry and Cell Biology
سال: 2017
ISSN: 0829-8211,1208-6002
DOI: 10.1139/bcb-2016-0067