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Information on EC 1.1.1.34 - hydroxymethylglutaryl-CoA reductase (NADPH) and Organism(s) Rattus norvegicus and UniProt Accession P51639
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1.1.1.34 hydroxymethylglutaryl-CoA reductase (NADPH)IUBMB Comments
The enzyme is inactivated by EC 2.7.11.31 {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} and reactivated by EC 3.1.3.47 {[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase}.
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Word Map
- 1.1.1.34
- cholesterol
- statin
- lipoprotein
- simvastatin
- sterol
- cardiovascular
- triglyceride
-
low-density
- hypercholesterolemia
- lovastatin
- pravastatin
- coronary
-
lipid-lowering
- bile
- endothelial
- artery
- atorvastatin
- atherosclerosis
-
isoprenoids
- hdl
-
cholesterol-lowering
- hyperlipidemia
-
ldl-cholesterol
-
placebo
- squalene
-
apolipoproteins
- myopathy
-
hypocholesterolemic
-
farnesylation
-
geranylgeranylation
-
hypolipidemic
- rosuvastatin
- dyslipidemias
-
high-density
-
fibrates
- cyp7a1
- cholestyramine
- rhabdomyolysis
-
7alpha-hydroxylase
- drug development
- medicine
- nutrition
-
acyl-coa:cholesterol
- molecular biology
- 25-hydroxycholesterol
- lanosterol
- gemfibrozil
- pcsk9
- ezetimibe
- biotechnology
- dolichols
-
isoprenylation
- srebp-2
-
statin-induced
-
lipoprotein-cholesterol
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
+
2
=
+
2
+
2
Synonyms
hmg-coa reductase, hmgcr, 3-hydroxy-3-methylglutaryl coenzyme a reductase, hmgr, hmg coa reductase, 3-hydroxy-3-methylglutaryl-coa reductase, 3-hydroxy-3-methylglutaryl-coenzyme a reductase, hmgcoa reductase, 3-hydroxy-3-methylglutaryl coa reductase, hmg-coar, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-hydroxy-3-methylglutaryl-CoA reductase
-
-
-
-
3-hydroxy-3-methylglutaryl-CoA reductase (NADPH)
-
-
-
-
beta-hydroxy-beta-methylglutaryl coenzyme A reductase
-
-
-
-
beta-hydroxy-beta-methylglutaryl-Co A reductase
-
-
-
-
HMG-CoA reductase
HMG2.2
-
-
-
-
HMG3.3
-
-
-
-
HMGCoA reductase-mevalonate:NADP-oxidoreductase (acetylating CoA)
-
-
-
-
HMGR
HMGR1
-
-
-
-
HMGR2
-
-
-
-
hydroxymethylglutaryl CoA reductase (NADPH)
-
-
-
-
hydroxymethylglutaryl-coenzyme A reductase (reduced nicotinamide adenine dinucleotide phosphate)
-
-
-
-
mevalonate:NADP+ oxidoreductase (acetylating CoA)
-
-
-
-
NADPH-hydroxymethylglutaryl-CoA reductase
-
-
-
-
S-3-hydroxy-3-methylglutaryl-CoA reductase
-
-
-
-
HMG-CoA reductase
-
-
-
-
HMGR
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(R)-mevalonate:NADP+ oxidoreductase (CoA-acylating)
The enzyme is inactivated by EC 2.7.11.31 {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} and reactivated by EC 3.1.3.47 {[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase}.
CAS REGISTRY NUMBER
COMMENTARY
9028-35-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevalonate + CoA + NADP+
-
-
-
-
?
DL-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonolactone + CoA + 2 NADP+ + H2O
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonolactone + CoA + 2 NADP+ + H2O
-
rate-limiting step of cholesterol biosynthesis
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonolactone + CoA + 2 NADP+ + H2O
-
rate-limiting step of cholesterol biosynthesis
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3R,5R)-7-(1-ethyl-3-(4-fluorophenyl)-4-methyl-5-[(5-methyl-pyrazin-2-ylmethyl)-carbamoyl]-1H-pyrrol-2-yl)-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-4-methyl-5-phenylcarbamoyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
-
-
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-5-(4-methoxybenzylcarbamoyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-5-(4-methoxycarbonyl-benzylcarbamoyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[3-(4-fluoro-phenyl)-1-isopropyl-5-phenylcarbamoyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[3-(4-fluorophenyl)-1-isopropyl-4-phenyl-5-phenylcarbamoyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[5-(4-carboxy-benzylcarbamoyl)-ethyl-3-(4-fluorophenyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid disodium salt
-
-
(3R,5R)-7-[5-benzylcarbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid
-
-
(3R,5R)-7-[5-carbamoyl-1-ethyl-3-(4-fluorophenyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[5-carbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid sodium salt
-
-
(3R,5R)-7-[5-cyano-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
-
-
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoic acid
-
competitive inhibitor, shows slight inhibitory activity
7-[5-ethylcarbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
-
-
adenosine-2'-monophospho-5'-diphosphoribose
-
competitive inhibitor for NADPH binding site
GFPDGG
-
designed on the basis of the rigid peptide backbone, increases the inhibitory potency more than 300 times compared to the first isolated LPYP from soybean, overview
sodium (E,3R,5S)-7-(2-(2-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
-
has almost no effect on the activity
sodium (E,3R,5S)-7-(2-(3-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
-
-
sodium (E,3R,5S)-7-(2-(4-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
-
shows the most potent inhibitory activity among compounds comparable with that of clinically useful mevastatin
sodium (E,3R,5S)-7-(2-phenyl-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxyhept-6-enoate
-
has almost no effect on the activity
sodium (E,3R,5S)-7-(4-(3-(2-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
-
-
sodium (E,3R,5S)-7-(4-(3-(3-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
-
-
sodium (E,3R,5S)-7-(4-(3-phenylpentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
-
-
GFPTGG
-
competitive, effects on enzyme Michaelis-Menten kinetics, overview
additional information
-
design, synthesis and evaluation of structure-based peptide inhibitors, computational methods, overview
-
additional information
-
discovery, synthesis, and optimization of substituted pyrrole-based hepatoselective ligands as potent inhibitors of HMG-CoA reductase for reducing low density lipoprotein cholesterol (LDL-c) in the treatment of hypercholesterolemia
-
additional information
-
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)phenyl)-3,5-dihydroxyhept-6-enoic acid shows no apparent HMGR inhibitory activity even at 100 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
supernatant protein factor
-
i.e. SPF, a 46 kDa cytosolic protein, stimulation of squalene monooxygenase and cholesterol biosynthesis in hepatoma cell culture, acts directly on the enzyme, not by increasing the enzyme amount
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000035
(3R,5R)-7-(1-ethyl-3-(4-fluorophenyl)-4-methyl-5-[(5-methyl-pyrazin-2-ylmethyl)-carbamoyl]-1H-pyrrol-2-yl)-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000029
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-4-methyl-5-phenylcarbamoyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000024
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-5-(4-methoxybenzylcarbamoyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000028
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-5-(4-methoxycarbonyl-benzylcarbamoyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000017
(3R,5R)-7-[3-(4-fluoro-phenyl)-1-isopropyl-5-phenylcarbamoyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000043
(3R,5R)-7-[3-(4-fluorophenyl)-1-isopropyl-4-phenyl-5-phenylcarbamoyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000011
(3R,5R)-7-[5-(4-carboxy-benzylcarbamoyl)-ethyl-3-(4-fluorophenyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid disodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000015
(3R,5R)-7-[5-benzylcarbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid
Rattus norvegicus
-
37°C, hepatocytes
0.000032
(3R,5R)-7-[5-carbamoyl-1-ethyl-3-(4-fluorophenyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.0000049
(3R,5R)-7-[5-carbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.0000021
(3R,5R)-7-[5-cyano-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
2.2 - 26
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoic acid
0.0000051
7-[5-ethylcarbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.003
fluvastatin
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
0.04
mevastatin
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
0.82
sodium (E,3R,5S)-7-(2-(2-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
1.2
sodium (E,3R,5S)-7-(2-(3-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
0.15
sodium (E,3R,5S)-7-(2-(4-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
0.85
sodium (E,3R,5S)-7-(2-phenyl-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxyhept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
7.4
sodium (E,3R,5S)-7-(4-(3-(2-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
92
sodium (E,3R,5S)-7-(4-(3-(3-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (3.7 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
1.8
sodium (E,3R,5S)-7-(4-(3-phenylpentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
2.2
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoic acid
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
26
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoic acid
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (3.7 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
-
HMG-CoA reductase activity is higher in both female and male Nagase analbumimetic rats than in Sprague-Dwwley rats. Ovariectomy results in no significant changes in total hepatic HMG-CoA reductase in female Sprague-Dawley rats
-
modified HMG-CoA reductase and low density lipoprotein receptor regulation is deeply involved in age-related hypercholesterolemia
-
the enzyme is fully activated both in acute and in chronic thioacetamide-treated animals, while no modifications are detected in its KM and in its short-term regulatory enzymes
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HMDH_RAT
887
5
96688
Swiss-Prot
Secretory Pathway (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
activity is regulated by phosphorylation and dephosphorylation
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19
-
below 19°C reversible inactivation of enzyme activity, prevented by NADPH and NADP+
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, after quick freezing in acetone/solid CO2 at -80°C, one week, 10% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
the cholesterol absorption inhibitor ezetimibe profoundly lowers serum cholesterol levels in animals expressing very low rates of hepatic cholesterol synthesis and produces large compensatory increases in hepatic HMG-CoA reductase expression without signifucantly affecting expression of hepatic low density lipoprotein receptors. This indicates that ezitimibe should be most effective in lowering serum cholesterol levels in peaple with low rates of cholesterol synthesis/High rates of cholesterol absorption
drug development
-
inhibitors of HMG-CoA reductase for reducing low density lipoprotein cholesterol in the treatment of hypercholesterolemia
medicine
medicine
-
dual therapy with the HMG-CoA reductase inhibitor pravastatin and the angiotensin receptor antagonist olmesartan, which produce an additive reduction in cardiomyocyte hypertrophy and cardiac fibrosis after myocardial infarction through different mechanisms, decreases the propensity of the heart to arrhythmogenesis
medicine
-
treatment with the inhibitor atorvastatin exerts early nephroprotective effects in a rat model of chronic inhibition of nitric axide synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bucher, N.L.R.; Overath, P.; Lynen, F.
beta-Hydroxy-beta-methylglutaryl coenzyme A reductase, cleavage and condensing enzymes in relation to cholesterol formation in rat liver
Biochim. Biophys. Acta
40
491-501
1960
Rattus norvegicus
Kawachi, T.; Rudney, H.
Solubilization and purification of beta-hydroxy-beta-methylglutaryl coenzyme A reductase from rat liver
Biochemistry
9
1700-1705
1970
Rattus norvegicus
Madhosingh, C.; Migicovski, B.B.; Wood, I.M.
Inhibition of yeast hydroxymethylglutaryl-CoA reductase by a rat liver mitochondrial preperation
FEBS Lett.
46
20-22
1974
Saccharomyces cerevisiae, Rattus norvegicus
Heller, R.A.; Gould, R.G.
Prevention of cold inactivation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by NADPH
Biochim. Biophys. Acta
388
254-259
1975
Rattus norvegicus
Ingebritsen, T.S.; Parker, R.A.; Gibson, D.M.
Regulation of liver hydroxymethylglutaryl-CoA reductase by a bicyclic phosphorylation system
J. Biol. Chem.
256
1138-1144
1981
Rattus norvegicus
Young, N.L.; Saudek, C.D.; Crawford, S.A.; Zuckerbrod, S.L.
Recovery and activation from hydroxymethylglutaryl coenzyme A reductase from rat small intestine
J. Lipid Res.
23
257-265
1982
Rattus norvegicus
Sipat, A.P.
Hydroxymethylglutaryl CoA reductase (NADPH) in the latex of Hevea brasiliensis
Phytochemistry
21
2613-2618
1982
Hevea brasiliensis, Pisum sativum, Rattus norvegicus
-
Van Heusden, G.P.H.; Wirtz, K.W.A.
Hydroxymethylglutaryl CoA reductase and the modulation of microsomal cholesterol content by the none specific lipid transfer protein
J. Lipid Res.
25
27-32
1984
Rattus norvegicus
Ness, G.C.; Eales, S.J.; Pendleton, L.C.; Smith, M.
Activation of rat liver microsomal 3-hydroxy-3-methylglutaryl coenzyme A reductase by NADPH
J. Biol. Chem.
260
12391-12393
1985
Rattus norvegicus
Feingold, K.R.; Moser, A.H.
The effect of substrates and competitive inhibitors on the phosphatase dependent activation of hepatic hydroxymethylglutaryl CoA reductase
Arch. Biochem. Biophys.
249
46-51
1986
Rattus norvegicus
Gibson, D.M.; Parker, R.A.
Hydroxymethylglutaryl-coenzyme A reductase
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
18
179-215
1987
Rattus norvegicus
-
Mokashi, V.; Singh, D.K.; Porter, T.D.
Supernatant protein factor stimulates HMG-CoA reductase in cell culture and in vitro
Arch. Biochem. Biophys.
433
474-480
2005
Rattus norvegicus
Shin, Y.; Vaziri, N.D.; Willekes, N.; Kim, C.H.; Joles, J.A.
Effects of gender on hepatic HMG-CoA reductase, cholesterol 7alpha-hydroxylase, and LDL receptor in hereditary analbuminemia
Am. J. Physiol. Endocrinol. Metab.
289
E993-E998
2005
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Lee, T.M.; Lin, M.S.; Chou, T.F.; Chang, N.C.
Additive effects of combined blockade of AT1 receptor and HMG-CoA reductase on left ventricular remodeling in infarcted rats
Am. J. Physiol. Heart Circ. Physiol.
291
H1281-H1289
2006
Rattus norvegicus
Ness, G.C.; Holland, R.C.; Lopez, D.
Selective compensatory induction of hepatic HMG-CoA reductase in response to inhibition of cholesterol absorption
Exp. Biol. Med.
231
559-565
2006
Rattus norvegicus (P51639)
Pallottini, V.; Martini, C.; Cavallini, G.; Donati, A.; Bergamini, E.; Notarnicola, M.; Caruso, M.G.; Trentalance, A.
Modified HMG-CoA reductase and LDLr regulation is deeply involved in age-related hypercholesterolemia
J. Cell. Biochem.
98
1044-1053
2006
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Pallottini, V.; Martini, C.; Bassi, A.M.; Romano, P.; Nanni, G.; Trentalance, A.
Rat HMGCoA reductase activation in thioacetamide-induced liver injury is related to an increased reactive oxygen species content
J. Hepatol.
44
368-374
2006
Rattus norvegicus
Lecian, D.; Demova, H.; Lodererova, A.; Zdychova, J.; Kluckova, H.; Teplan, V.; Voska, L.; Komers, R.
Renal effects of HMG-CoA reductase inhibition in a rat model of chronic inhibition of nitric oxide synthesis
Kidney Blood Press. Res.
29
135-143
2006
Rattus norvegicus
Bratton, L.D.; Auerbach, B.; Choi, C.; Dillon, L.; Hanselman, J.C.; Larsen, S.D.; Lu, G.; Olsen, K.; Pfefferkorn, J.A.; Robertson, A.; Sekerke, C.; Trivedi, B.K.; Unangst, P.C.
Discovery of pyrrole-based hepatoselective ligands as potent inhibitors of HMG-CoA reductase
Bioorg. Med. Chem.
15
5576-5589
2007
Rattus norvegicus
Pak, V.V.; Koo, M.; Kim, M.J.; Yun, L.; Kwon, D.Y.
Binding effect and design of a competitive inhibitory peptide for HMG-CoA reductase through modeling of an active peptide backbone
Bioorg. Med. Chem.
16
1309-1318
2008
Rattus norvegicus
Pak, V.V.; Koo, M.; Kim, M.J.; Yang, H.J.; Yun, L.; Kwon, D.Y.
Modeling an active conformation for linear peptides and design of a competitive inhibitor for HMG-CoA reductase
J. Mol. Recognit.
21
224-232
2008
Rattus norvegicus
EXTERNAL LINKS (specific for EC-Number 1.1.1.34)
Transporter Classification Database (TCDB): 2.A.6.6.5, 2.A.6.6.10
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