Rhodanese from Cercopithecus aethiops (vervet monkey) liver. II. Aspects of enzyme kinetics and mechanism of action.
Initial velocity kinetic studies were undertaken and certain kinetic parameters ( KmSSO2 -3 = 3.1 X 10(-3) M and Vmax = 153.85 U/ml/min.) were determined and the mechanism identified as a ping-pong (double displacement) mechanism. Competitive inhibition of rhodanese by both substrates, viz. thiosulphate and cyanide, provides additional evidence of Ping-Pong Bi-Bi mechanism for this transferase.
D000818:Animals; D002521:Cercopithecus / Q000378:metabolism*; D002522:Chlorocebus aethiops / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D013466:Sulfurtransferases / Q000032:analysis*; D013884:Thiosulfate Sulfurtransferase / Q000032:analysis* / Q000037:antagonists & inhibitors; D013885:Thiosulfates / Q000494:pharmacology
D013885:Thiosulfates; D013466:Sulfurtransferases; D013884:Thiosulfate Sulfurtransferase