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Information on EC 1.1.1.34 - hydroxymethylglutaryl-CoA reductase (NADPH) and Organism(s) Homo sapiens and UniProt Accession P04035

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EC Tree
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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This record set is specific for:
Homo sapiens
UNIPROT: P04035
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-hydroxy-3-methylglutaryl coenzyme A reductase
-
3-hydroxy-3-methylglutaryl-CoA reductase
-
3-hydroxy-3-methylglutaryl-coenzyme A reductase
-
HMG-CoA reductase
-
HMG-CoA-R
-
3-hydroxy-3-methyl-glutaryl CoA reductase
-
-
3-hydroxy-3-methylglutaryl CoA reductase
-
-
3-hydroxy-3-methylglutaryl-CoA reductase
-
-
-
-
3-hydroxy-3-methylglutaryl-CoA reductase (NADPH)
-
-
-
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3-hydroxymethylglutaryl coenzyme A reductase
-
-
beta-hydroxy-beta-methylglutaryl coenzyme A reductase
-
-
-
-
beta-hydroxy-beta-methylglutaryl-Co A reductase
-
-
-
-
HMG CoA reductase
-
-
HMG-CoA reductase
HMG-CoAR
-
-
HMG1
-
-
HMG2
-
-
HMG2.2
-
-
-
-
HMG3.3
-
-
-
-
HMGCoA reductase-mevalonate:NADP-oxidoreductase (acetylating CoA)
-
-
-
-
HMGCR
-
-
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
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
show the reaction diagram
reaction mechanism, modelling of three different systems, detailed overview. Formation of a mevaldyl-CoA intermediate protonated by a conserved active site lysine, Lys691. The conserved active site glutamate and aspartate residues, Glu559 and Asp767, along with the ribose moiety of NADPH, form a hydrogen bond network crucial to the increase of the stabilizing effect of Lys691 over the transition state. A charged His752 forms an oxyanion hole with Lys691 to stabilize the negative charge developed in the thioester oxygen
(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
show the reaction diagram
Glu559 and His866 are involved in catalysis
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
-
-
-
-
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 hide
9028-35-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
show the reaction diagram
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
show the reaction diagram
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
show the reaction diagram
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
show the reaction diagram
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
show the reaction diagram
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevaldyl-CoA + NADP+
show the reaction diagram
-
first step reaction
-
-
?
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
show the reaction diagram
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
show the reaction diagram
-
-
-
-
?
mevaldehyde + NADPH + H+
(R)-mevalonate + NADP+
show the reaction diagram
-
-
-
-
?
mevaldyl-CoA + NADPH + H+ + H2O
(R)-mevalonate + CoA + NADP+
show the reaction diagram
-
second step reaction
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
show the reaction diagram
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
show the reaction diagram
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
show the reaction diagram
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
show the reaction diagram
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevaldyl-CoA + NADP+
show the reaction diagram
-
first step reaction
-
-
?
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
show the reaction diagram
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
show the reaction diagram
-
-
-
-
?
mevaldyl-CoA + NADPH + H+ + H2O
(R)-mevalonate + CoA + NADP+
show the reaction diagram
-
second step reaction
-
-
?
additional information
?
-
-
the reaction is a highly regulated process within the cholesterol biosynthetic pathway
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
atorvastatin
-
brutieridin
i.e. hesperetin 7-(2''-alpha-rhamnosyl-6''-(3''''-hydroxy-3''''-methylglutaryl)-beta-D-glucoside), a flavonoid conjugate from bergamot fruit extract, structural analogue of statins, computational study, overview
cerivastatin
-
fluvastatin
lovastatin
-
melitidin
i.e. naringenin 7-(2''-alpha-rhamnosyl-6''-(3''''-hydroxy-3''''-methylglutaryl)-beta-D-glucoside), a flavonoid conjugate from bergamot fruit extract, structural analogue of statins, computational study, overview
mevastatin
-
pravastatin
rosuvastatin
-
simvastatin
-
(S)-4-carboxy-3-hydroxy-3-methylbutyryl-CoA
-
competitive inhibitor
(S)-4-carboxy-3-hydroxybutyryl-CoA
-
competitive inhibitor
3,3-dimethylglutaryl-CoA
-
competitive inhibitor
3-hydroxyglutaryl-CoA
-
competitive inhibitor
3-methylglutaryl-CoA
-
competitive inhibitor
AFGYVAE
-
-
atorvastatin
ceramide
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treatment with exogenous ceramides, or increasing the endogenous ceramide levels inhibits HMGCR by 60–80%
cerivastatin
-
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cycloheximide
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downregulation of protein synthesis, synergistic with eicosapentanoic acid and myristic acid
DFGYVAE
-
-
EFGYVAE
-
-
eicosapentaenoic acid
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inhibits translation of the enzyme about 50% at 0.15 mM, downregulation, slightly increases downregulation of protein synthesis by cycloheximide
FFGYVAE
-
-
FFYVAE
-
-
FG-(4-fluoro)FVAE
-
-
FGYVAE
-
-
fluvastatin
FPYVAE
-
-
GFGYVAE
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-
IAVPTGVA
-
-
IFGYVAE
-
-
Ile-Ala-Val-Glu
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-
Ile-Ala-Val-Pro-Gly-Glu-Val-Ala
-
-
Ile-Val-Ala-Glu
-
-
Leu-Pro-Tyr-Pro
-
-
LFGYVAE
-
-
PFGYVAE
-
-
pravastatin
-
-
rosuvastatin
-
thermodynamics of binding and inhibition mechanism, Glu559 is involved, reversible, 2-step complex formation, competitive with respect to 3-hydroxy-3-methylglutaryl-CoA, non-competitive to NADPH
SFGYVAE peptide
simvastatin
SMase C
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treatment of fibroblasts with SMase C results in a 90% inhibition of HMGCR
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SMase D
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treatment of fibroblasts with SMase D inhibits by 29%
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TFGYVAE
-
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Tyr-Ala-Val-Glu
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Tyr-Val-Ala-Glu
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-
VFGYVAE
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
myristic acid
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stimulates translation of the enzyme about 1.8fold at 0.15 mM, upregulation
additional information
-
phosphorylation of HMGCR is stimulated by SMase C or exogenous ceramide
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
3-hydroxy-3-methylglutaryl-CoA
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0.021
NADPH
-
0.6
3-hydroxy-3-methylglutaryl-CoA
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pH 7.5, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000014
atorvastatin
pH 6.8, 37°C
0.0000057
cerivastatin
pH 6.8, 37°C
0.000256
fluvastatin
pH 6.8, 37°C
0.000103
pravastatin
pH 6.8, 37°C
0.0000023
rosuvastatin
pH 6.8, 37°C
0.000008
atorvastatin
-
-
0.00001
cerivastatin
-
-
0.000028
fluvastatin
-
-
0.000044
pravastatin
-
-
0.0000035
rosuvastatin
-
-
0.000012
SFGYVAE peptide
-
pH and temperature not specified in the publication
0.000011
simvastatin
-
-
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00049
AFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.00016
DFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.00024
EFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.00032
FFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.0025
FFYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.0085
FG-(4-fluoro)FVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.0004
FGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.0014
FPYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.00027
GFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.152
IAVPTGVA
Homo sapiens
-
pH and temperature not specified in the publication
0.00035
IFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.075
Ile-Ala-Val-Glu
Homo sapiens
-
pH and temperature not specified in the publication
0.201
Ile-Ala-Val-Pro-Gly-Glu-Val-Ala
Homo sapiens
-
pH and temperature not specified in the publication
0.052
Ile-Val-Ala-Glu
Homo sapiens
-
pH and temperature not specified in the publication
0.484
Leu-Pro-Tyr-Pro
Homo sapiens
-
pH and temperature not specified in the publication
0.00037
LFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.00043
PFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.000033
SFGYVAE peptide
Homo sapiens
-
pH and temperature not specified in the publication
0.00026
TFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.044
Tyr-Ala-Val-Glu
Homo sapiens
-
pH and temperature not specified in the publication
0.041
Tyr-Val-Ala-Glu
Homo sapiens
-
pH and temperature not specified in the publication
0.00045
VFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
assay at
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
samples of patients with cardiovascular disorders
Manually annotated by BRENDA team
-
recombinant enzyme
Manually annotated by BRENDA team
-
colon cancer cell line
Manually annotated by BRENDA team
-
NCTC 2544 cells. HMG-CoA reductase and peroxisome proliferator-activated receptor alpha are involved in clofibrate-induced apoptosis in human keratinocytes
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
transmembrane protein
Manually annotated by BRENDA team
-
transmembrane protein
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
within cells, the concentration of mevalonate and therefore that of its metabolic products is tightly controlled through the activity of HMGR, an enzyme that catalyzes the four-electron reduction of 3-hydroxy-3-methylglutaryl-CoA to mevalonate
metabolism
-
part of cholesterol synthesis pathway
physiological function
-
the enzyme is the major regulatory enzyme of cholesterol biosynthesis and the target enzyme of many investigations aimed at lowering the rate of cholesterol biosynthesis
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HMDH_HUMAN
888
5
97476
Swiss-Prot
Secretory Pathway (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000 - 56000
-
proteolytically cleaved soluble enzyme fragment
96000
-
intact membrane protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
the catalytic portion of human HMG-CoA, after cleavage of the probable dimeric form found in the endoplasmic reticulum, 18 crystallized as a dimer of dimers. However, the dimer-dimer interface is distant from the active site and only the dimer of the molecule seems crucial for catalysis
homotetramer
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
the enzyme is phosphorylated at Ser872 by AMP-activated protein kinase and reversibly dephosphorylated by phosphatase 2A
glycoprotein
-
-
phosphoprotein
-
activity is regulated by phosphorylation and dephosphorylation
proteolytic modification
-
proteolysis releases a soluble, active fragment of 52-56 kDa
additional information
-
genistein, eicosapentaenoic acid and docosahexaenoic acid down-regulate reductase activity, primarily through posttranscriptional effects
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of the enzyme crystal structure (PDV ID 1DQA) at 2.0 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S872D
the mutation reduces the catalytic activity of the enzyme similarly to that of the phosphorylated enzyme
Q766H
-
restores viability of Saccharomyces cerevisiae strains lacking the HMG1 and HMG2 genes, thus is catalytically active in yeast cells. Q766H mutation, which affects the structure of the catalytic domain, increases the sensitivity of the enzyme towards statin treatment
R393Q
-
restores viability of Saccharomyces cerevisiae strains lacking the HMG1 and HMG2 genes, thus is catalytically active in yeast cells. R393Q mutation does not change the properties of the enzyme towards statin treatment
additional information
-
expression of human HMG-CoA reductase in yeast complements the lethal phenotype of Saccharomyces cerevisiae strains lacking the HMG1 and HMG2 genes
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA encoding the wild-type and mutant forms of human HMG-CoA reductase expressed under control of the yeast MET25 promoter in a Saccharomyces cerevisiae strain with deletions of both HMG1 and HMG2
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased Hmgcr mRNA levels after serum starvation
increased Hmgcr mRNA levels after serum starvation are suppressed by 25-hydroxycholesterol. The suppressive effect of 25-hydroxycholesterol on mRNA transcription is ameliorated by trichostatin A. Anacardic acid, 25-hydroxycholesterol and 24(S)-hydroxycholesterol suppress the transcription by inhibiting H3K27 acetylation in the promoter. 27-Hydroxycholesterol, 22(S)-hydroxycholesterol and 22(R)-hydroxycholesterol suppress the transcription
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
a yeast expression system can serve to study the influence of selected mutations in human HMG-CoA reductase on the sensitivity of the enzyme to commonly prescribed statins, thus this model system is suitable for the development and selection of lipid-lowering drugs as well as for the examination of DNA sequence variations in the context of statin therapy
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Harwood, Jr., H.J.; Schneider, M.; Stacpool, P.W.
Regulation of human leukocyte microsomal hydroxymethylglutaryl-CoA reductase activity by a phosphorylation and dephosphorylation mechanism
Biochim. Biophys. Acta
805
245-251
1984
Homo sapiens
Manually annotated by BRENDA team
Hupperich, M.; Thomer, A.; Kratz, K.; Eggerer, H.
Substrate and inhibitor specificity of 3-hydroxy-3-methylglutaryl-CoA reductase determined with substrate-analogue CoA-thioesters and CoA-thioethers
Biol. Chem. Hoppe-Seyler
372
857-863
1991
Homo sapiens
Manually annotated by BRENDA team
Holdgate, G.A.; Ward, W.H.; McTaggart, F.
Molecular mechanism for inhibition of 3-hydroxy-3-methylglutaryl CoA (HMG-CoA) reductase by rosuvastatin
Biochem. Soc. Trans.
31
528-531
2003
Homo sapiens
Manually annotated by BRENDA team
Garcia-Pelayo, M.C.; Garcia-Peregrin, E.; Martinez-Cayuela, M.
Differential translational effects of myristic acid and eicosapentaenoic acid on 3-hydroxy-3-methylglutaryl-CoA reductase from Reuber H35 hepatoma cells
Exp. Biol. Med.
229
781-786
2004
Homo sapiens
Manually annotated by BRENDA team
Muzio, G.; Martinasso, G.; Trombetta, A.; Di Simone, D.; Canuto, R.A.; Maggiora, M.
HMG-CoA reductase and PPARalpha are involved in clofibrate-induced apoptosis in human keratinocytes
Apoptosis
11
265-275
2006
Homo sapiens
Manually annotated by BRENDA team
Carbonell, T.; Freire, E.
Binding thermodynamics of statins to HMG-CoA reductase
Biochemistry
44
11741-11748
2005
Homo sapiens (P04035)
Manually annotated by BRENDA team
Duncan, R.E.; El-Sohemy, A.; Archer, M.C.
Regulation of HMG-CoA reductase in MCF-7 cells by genistein, EPA, and DHA, alone and in combination with mevastatin
Cancer Lett.
224
221-228
2005
Homo sapiens
Manually annotated by BRENDA team
Gueguen, Y.; Ferrari, L.; Souidi, M.; Batt, A.M.; Lutton, C.; Siest, G.; Visvikis, S.
Compared effect of immunosuppressive drugs cyclosporine A and rapamycin on cholesterol homeostasis key enzymes CYP27A1 and HMG-CoA reductase
Basic Clin. Pharmacol. Toxicol.
100
392-397
2007
Homo sapiens
Manually annotated by BRENDA team
Subbaiah, P.V.; Sowa, J.M.; Singh, D.K.
Sphingolipids and cellular cholesterol homeostasis. Effect of ceramide on cholesterol trafficking and HMG CoA reductase activity
Arch. Biochem. Biophys.
474
32-38
2008
Homo sapiens
Manually annotated by BRENDA team
Seiki, S.; Frishman, W.H.
Pharmacologic inhibition of squalene synthase and other downstream enzymes of the cholesterol synthesis pathway: a new therapeutic approach to treatment of hypercholesterolemia
Cardiol. Rev.
17
70-76
2009
Homo sapiens
Manually annotated by BRENDA team
Wysocka-Kapcinska, M.; Lutyk-Nadolska, J.; Kiliszek, M.; Plochocka, D.; Maciag, M.; Leszczynska, A.; Rytka, J.; Burzynska, B.
Functional expression of human HMG-CoA reductase in Saccharomyces cerevisiae: a system to analyse normal and mutated versions of the enzyme in the context of statin treatment
J. Appl. Microbiol.
106
895-902
2009
Homo sapiens
Manually annotated by BRENDA team
Perchellet, J.P.; Perchellet, E.M.; Crow, K.R.; Buszek, K.R.; Brown, N.; Ellappan, S.; Gao, G.; Luo, D.; Minatoya, M.; Lushington, G.H.
Novel synthetic inhibitors of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase activity that inhibit tumor cell proliferation and are structurally unrelated to existing statins
Int. J. Mol. Med.
24
633-643
2009
Homo sapiens (P04035), Homo sapiens
Manually annotated by BRENDA team
Gholamhoseinian, A.; Shahouzehi, B.; Sharifi-Far, F.
Inhibitory activity of some plant methanol extracts on 3-hydroxy-3-methylglutaryl coenzyme A reductase
Int. J. Pharmacol.
6
705-711
2010
Homo sapiens
-
Manually annotated by BRENDA team
Leopoldini, M.; Malaj, N.; Toscano, M.; Sindona, G.; Russo, N.
On the inhibitor effects of bergamot juice flavonoids binding to the 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) enzyme
J. Agric. Food Chem.
58
10768-10773
2010
Homo sapiens (P04035)
Manually annotated by BRENDA team
Mozzicafreddo, M.; Cuccioloni, M.; Eleuteri, A.; Angeletti, M.
Rapid reverse phase-HPLC assay of HMG-CoA reductase activity
J. Lipid Res.
51
2460-2463
2010
Homo sapiens
Manually annotated by BRENDA team
Pak, V.V.; Koo, M.; Kwon, D.Y.; Yun, L.
Design of a highly potent inhibitory peptide acting as a competitive inhibitor of HMG-CoA reductase
Amino Acids
43
2015-2025
2012
Homo sapiens
Manually annotated by BRENDA team
Oliveira, E.F.; Cerqueira, N.M.F.S.A.; Ramos, M.J.; Fernandes, P.A.
QM/MM study of the mechanism of reduction of 3-hydroxy-3-methylglutaryl coenzyme A catalyzed by human HMG-CoA reductase
Catal. Sci. Technol.
6
7172-7185
2016
Homo sapiens (P04035)
-
Manually annotated by BRENDA team
Costa, C.H.S.; Oliveira, A.R.S.; Dos Santos, A.M.; da Costa, K.S.; Lima, A.H.L.E.; Alves, C.N.; Lameira, J.
Computational study of conformational changes in human 3-hydroxy-3-methylglutaryl coenzyme reductase induced by substrate binding
J. Biomol. Struct. Dyn.
37
4374-4383
2019
Homo sapiens (P04035), Homo sapiens
Manually annotated by BRENDA team
Ando, H.; Horibata, Y.; Aoyama, C.; Shimizu, H.; Shinohara, Y.; Yamashita, S.; Sugimoto, H.
Side-chain oxysterols suppress the transcription of CTP phosphoethanolamine cytidylyltransferase and 3-hydroxy-3-methylglutaryl-CoA reductase by inhibiting the interaction of p300 and NF-Y, and H3K27 acetylation
J. Steroid Biochem. Mol. Biol.
195
105482
2019
Homo sapiens (P04035), Mus musculus (Q01237)
Manually annotated by BRENDA team