Substrate binding order in mevalonate 5-diphosphate decarboxylase from chicken liver.
The substrate binding order of chicken liver mevalonate 5-diphosphate decarboxylase was investigated by using competitive inhibitors of the substrates. Mevalonate and mevalonate 5-phosphate showed mixed inhibition when ATP was the varied substrate. Both analogues of ATP, adenosine 5'-O-(3-thiotriphosphate) and beta-tau methylene adenosine 5'-triphosphate showed uncompetitive inhibition against mevalonate 5-diphosphate. These results are in accordance with an ordered sequential mechanism with mevalonate 5-diphosphate as the first substrate to bind to the enzyme.
Jabalquinto
A M
AM
Departamento de Quimica, Facultad de Ciencia, Universidad de Santiago de Chile, Casilla.
Cardemil
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E
D000818:Animals; D002262:Carboxy-Lyases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002645:Chickens; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008798:Mevalonic Acid / Q000031:analogs & derivatives* / Q000378:metabolism; D013379:Substrate Specificity
C046285:5-diphosphomevalonic acid; D002262:Carboxy-Lyases; C022503:pyrophosphomevalonate decarboxylase; D008798:Mevalonic Acid