Inactivation of phosphoenolpyruvate carboxykinase by the guanosine nucleotide analogue, 5'-p-fluorosulfonylbenzoyl guanosine |
| |
Authors: | M Jadus R W Hanson R F Colman |
| |
Institution: | 1. Chemistry Department, University of Delaware, Newark, DE 19711 USA;2. Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106 USA |
| |
Abstract: | Rat liver cytosolic phosphoenolpyruvate carboxykinase is inactivated by incubation with 0.84 mM 5′-p-fluorosulfonylbenzoyl guanosine, but is not appreciably affected by the adenosine analogue, 5′-p-fluorosulfonylbenzoyl adenosine, in correspondance with the known nucleotide specificity of this enzyme. Marked protection against inactivation by 5′-p-fluorosulfonylbenzoyl guanosine is provided (either in the presence or absence of divalent metal cation) by GTP or GDP but not by ATP or phosphoenolpyruvate. The inactivation appears to be due to covalent reaction since radioactive reagent remains associated with the enzyme after extensive dialysis and gel filtration on Sephadex G-25. These results are consistent with affinity labeling of the nucleotide binding site of phosphoenolpyruvate carboxykinase by the guanosine nucleotide analogue 5′-p-fluorosulfonylbenzoyl guanosine. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|