1.1.1.88: hydroxymethylglutaryl-CoA reductase
This is an abbreviated version!
For detailed information about hydroxymethylglutaryl-CoA reductase, go to the full flat file.
Word Map on EC 1.1.1.88
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1.1.1.88
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cholesterol
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statin
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lipoprotein
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simvastatin
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sterol
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low-density
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coronary
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cardiovascular
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lovastatin
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hypercholesterolemia
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pravastatin
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atorvastatin
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lipid-lowering
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cholesterol-lowering
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3-hydroxy-3-methylglutaryl-coa
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cerivastatin
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mevinolin
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alpha-hydroxylase
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statin-induced
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compactin
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mevalonolactone
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cholestyramine
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mevalonii
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lipoprotein-deficient
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medicine
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25-hydroxycholesterol
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fibric
- 1.1.1.88
- cholesterol
- statin
- lipoprotein
- simvastatin
- sterol
-
low-density
- coronary
- cardiovascular
- lovastatin
- hypercholesterolemia
- pravastatin
- atorvastatin
-
lipid-lowering
-
cholesterol-lowering
- 3-hydroxy-3-methylglutaryl-coa
- cerivastatin
- mevinolin
-
alpha-hydroxylase
-
statin-induced
- compactin
- mevalonolactone
- cholestyramine
- mevalonii
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lipoprotein-deficient
- medicine
- 25-hydroxycholesterol
-
fibric
Reaction
Synonyms
3-hydroxy-3-methylglutaryl CoA reductase 1, 3-hydroxy-3-methylglutaryl coenzyme A reductase, 3-hydroxy-3-methylglutaryl-CoA reductase, 3-hydroxy-3-methylglutaryl-coenzyme-A reductase, beta-hydroxy-beta-methylglutaryl CoA-reductase, beta-hydroxy-beta-methylglutaryl coenzyme A reductase, HMG-CoA reductase, HMGCoAR, HMGR, hydroxymethylglutaryl coenzyme A reductase, Mt HMGR1, mvaA, NADH-dependent HMG-CoA reductase, NADH-HMGR
ECTree
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KM Value
KM Value on EC 1.1.1.88 - hydroxymethylglutaryl-CoA reductase
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0.078
(S)-3-hydroxy-3-methylglutaryl-CoA
pH and temperature not specified in the publication
0.00734
3-hydroxy-3-methylglutaryl-CoA
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at pH 7.4, temperature not specified in the publication
additional information
additional information
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
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0.27
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H381A mutant, oxidative acylation of mevalonate
0.45
(R,S)-mevalonate
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wild-type enzyme, oxidative acylation of mevalonate
0.71
(R,S)-mevalonate
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H381Q mutant, oxidative acylation of mevalonate
0.75
(R,S)-mevalonate
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H381K mutant, oxidative acylation of mevalonate
0.05
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reductive deacylation to mevalonate
0.3
DL-3-hydroxy-3-methylglutaryl-CoA
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reductive deacylation to mevalonate
0.072
NADH
pH and temperature not specified in the publication