Search KM Value [mM]

1.1.1.88

-999

more

kinetic analysis, overview. The enzyme exhibits positive cooperativity toward the substrates of the reductive reaction, but the oxidative reaction exhibits unusual double-saturation kinetics, distinctive among characterized HMG-CoA reductases. The unusual kinetics may arise from the presence of multiple active oligomeric states, each with different Vmax values

1.1.1.88

0.00734

3-hydroxy-3-methylglutaryl-CoA

at pH 7.4, temperature not specified in the publication

1.1.1.88

0.0285

NADH

at pH 7.4, temperature not specified in the publication

1.1.1.88

0.03

CoASH

H381A mutant, oxidative acylation of mevalonate

1.1.1.88

0.032

NADH

reductive deacylation to mevalonate

287496, 287497

1.1.1.88

0.039

CoA

oxidative acylation of mevalonate

287496, 287497

1.1.1.88

0.046

CoA

mevaldate oxidation

287496, 287497

1.1.1.88

0.05

CoASH

oxidative acylation of mevalonate

1.1.1.88

0.05

CoASH

wild-type enzyme, oxidative acylation of mevalonate

1.1.1.88

0.05

DL-3-hydroxy-3-methylglutaryl-CoA

reductive deacylation to mevalonate

287496, 287497