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
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General Information
General Information on EC 1.1.1.88 - hydroxymethylglutaryl-CoA reductase
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evolution
a key enzyme in endogenous cholesterol biosynthesis in mammals and isoprenoid biosynthesis via the mevalonate pathway in other eukaryotes, archaea and some eubacteria
physiological function
additional information
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HMG-CoAR increase is crucial for muscle differentiation induction. p21waf, whose increase is a necessary requisite for differentiation to occur, rises downstream HMG-CoAR activation, while p38/MAPK has a role as key regulator also for HMG-CoAR
physiological function
the enzyme prefers NAD(H) over NADP(H) as a cofactor, suggesting an oxidative physiological role for the enzyme. Also, the Burkholderia cenocepacia genome lacks the genes for the downstream enzymes of the mevalonate pathway, but the organism clearly possesses the genes for all the DXP pathway enzymes, further supporting a nonreductive, non-biosynthetic role for BcHMGR
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sequence comparisons of several species with class II and class I HMG-CoA reductases for analysis of cofactor binding, overview
additional information
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sequence comparisons of several species with class II and class I HMG-CoA reductases for analysis of cofactor binding, overview
additional information
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sequence comparisons of several species with class II and class I HMG-CoA reductases for analysis of cofactor binding, overview