Purification, characterization and inhibition by MK-401 of Fasciola hepatica phosphoglyceromutase.
Phosphoglyceromutase (EC 2.7.5.3) of Fasciola hepatica was purified 1390-fold to homogeneity. The enzyme had a molecular weight of 120 000 and was a tetramer composed of identical 30 000 molecular weight subunits. The enzyme was 2,3-dephosphoglyceric acid dependent, possessed reactive sulfhydryl groups and was inhibited irreversibly by iodoacetamide, and N-ethylmaleimide and reversibly by p-chloromercuribenzoate and 5,5'-dithiobis(2-nitrobenzoic acid). Initial velocity studies suggest that reaction occurred via a sequential mechanism and that MK-401 was a competitive inhibitor versus both 3-phosphoglyceric acid and 2,3-diphosphoglyceric acid.
D019794:2,3-Diphosphoglycerate; D000818:Animals; D002729:Chloromercuribenzoates / Q000494:pharmacology; D004163:Diphosphoglyceric Acids / Q000494:pharmacology; D005033:Ethylmaleimide / Q000494:pharmacology; D005210:Fasciola hepatica / Q000201:enzymology*; D007460:Iodoacetamide / Q000494:pharmacology; D007700:Kinetics; D008970:Molecular Weight; D010736:Phosphoglycerate Mutase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D010770:Phosphotransferases / Q000378:metabolism*
D002729:Chloromercuribenzoates; D004163:Diphosphoglyceric Acids; D019794:2,3-Diphosphoglycerate; D010770:Phosphotransferases; D010736:Phosphoglycerate Mutase; D005033:Ethylmaleimide; D007460:Iodoacetamide