Half-of-the-sites reactivity of yeast glyceraldehyde 3-phosphate dehydrogenase
作者： W.B. Stallcup , D.E. Koshland
DOI: 10.1016/0006-291X(72)90327-0
关键词:
摘要: Abstract Yeast glyceraldehyde 3-phosphate dehydrogenase is shown to exhibit a half-of-the-sites reactivity with both alkylating and acylating reagents. The shape of the inactivation profiles indicates that disubstituted enzyme inactive monosubstituted has approximately 10% activity native enzyme.
elsevier.com
sci-hub.se 参考文章(22)
Margaret T.A. Behme, Eugene H. Cordes, Kinetics of the Glyceraldehyde 3-Phosphate Dehydrogenase-catalyzed Hydrolysis of p-Nitrophenyl Acetate Journal of Biological Chemistry. ,vol. 242, pp. 5500- 5509 ,(1967) , 10.1016/S0021-9258(18)99387-7
O P Malhotra, S A Bernhard, Spectrophotometric identification of an active site-specific acyl glyceraldehyde 3-phosphate dehydrogenase. The regulation of its kinetic and equilibrium properties by coenzyme. Journal of Biological Chemistry. ,vol. 243, pp. 1243- 1252 ,(1968) , 10.1016/S0021-9258(19)56979-4
J. Ieuan Harris, R.N. Perham, Glyceraldehyde 3-phosphate dehydrogenases: I. The protein chains in glyceraldehyde 3-phosphate dehydrogenase from pig muscle Journal of Molecular Biology. ,vol. 13, ,(1965) , 10.1016/S0022-2836(65)80151-6
Kasper Kirschner, Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase Journal of Molecular Biology. ,vol. 58, pp. 51- 68 ,(1971) , 10.1016/0022-2836(71)90231-2
Athel Cornish-Bowden, D.E. Koshland, The Influence of Binding Domains on the Nature of Subunit Interactions in Oligomeric Proteins: APPLICATION TO UNUSUAL KINETIC AND BINDING PATTERNS Journal of Biological Chemistry. ,vol. 245, pp. 6241- 6250 ,(1970) , 10.1016/S0021-9258(18)62600-6
Kasper Kirschner, Ernesto Gallego, Inge Schuster, David Goodall, Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase Journal of Molecular Biology. ,vol. 58, pp. 29- 50 ,(1971) , 10.1016/0022-2836(71)90230-0
A. Lewis Farr, Oliver H. Lowry, Rose J. Randall, Nira J. Rosebrough, Protein Measurement with the Folin Phenol Reagent Journal of Biological Chemistry. ,vol. 193, pp. 265- 275 ,(1951)
D. R. Trentham, Rate-determining processes and the number of simultaneously active sites of d-glyceraldehyde 3-phosphate dehydrogenase Biochemical Journal. ,vol. 122, pp. 71- 77 ,(1971) , 10.1042/BJ1220071
Robert A. Cook, Daniel E. Koshland, Positive and negative cooperativity in yeast glyceraldehyde 3-phosphate dehydrogenase. Biochemistry. ,vol. 9, pp. 3337- 3342 ,(1970) , 10.1021/BI00819A007
Alexander Levitzki, William B. Stallcup, D. E. Koshland, Half-of-the-sites reactivity and conformational states of cytidine triphosphate synthetase Biochemistry. ,vol. 10, pp. 3371- 3378 ,(1971) , 10.1021/BI00794A009