Thiol-dependent metallo-endopeptidase characteristics of Pz-peptidase in rat and rabbit.
Pz-peptidase was purified from rat testis and rabbit muscle. Zinc was detectable in the rat enzyme. The activity of the enzyme from both species was slowly but completely abolished by EDTA and restored by Zn2+. Free thiol groups were also important for the catalytic activity of rat Pz-peptidase, as previously reported for the rabbit enzyme. We conclude that in both species Pz-peptidase has the characteristics of a thiol-dependent metallo-endopeptidase.
Department of Biochemistry, Strangeways Research Laboratory, Cambridge, U.K.
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Tisljar
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Barrett
D000595:Amino Acid Sequence; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004229:Dithiothreitol / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D005033:Ethylmaleimide / Q000494:pharmacology; D007700:Kinetics; D008297:Male; D008666:Metalloendopeptidases / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology; D011817:Rabbits; D051381:Rats; D013379:Substrate Specificity
D010450:Endopeptidases; D008666:Metalloendopeptidases; C022510:thimet oligopeptidase; D005033:Ethylmaleimide; D004229:Dithiothreitol