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
-
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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Cofactor
Cofactor on EC 1.1.1.88 - hydroxymethylglutaryl-CoA reductase
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NADP+
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NAD+ is 600000fold more efficient than NADP+ in wild-type enzyme
NAD+
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NADH
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reverse reaction
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very detailed kinetic studies of mutants concerning NAD+/NADP+-affinities, the best specificity improvement is achieved by the D146A/L148R-mutant
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additional information
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sequence comparisons of several species with class II (NAD(H)) and class I (NADP(H)) HMG-CoA reductases for analysis of cofactor binding, overview
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additional information
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sequence comparisons of several species with class II (NAD(H)) and class I (NADP(H)) HMG-CoA reductases for analysis of cofactor binding, overview
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additional information
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sequence comparisons of several species with class II (NAD(H)) and class I (NADP(H)) HMG-CoA reductases for analysis of cofactor binding, specificity-determining residue of HMGR from Pseudomonas mevalonii is D646, overview
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additional information
the enzyme prefers NAD(H) over NADP(H) as a cofactor, suggesting an oxidative physiological role for the enzyme
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