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Enzyme Nomenclature
Information on EC 1.1.1.34 - hydroxymethylglutaryl-CoA reductase (NADPH)
for references in articles please use BRENDA:EC1.1.1.34
Word Map on EC 1.1.1.34
- 1.1.1.34
- cholesterol
- statin
- simvastatin
- sterol
- cardiovascular
- triglyceride
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low-density
- coronary
- hypercholesterolemia
- pravastatin
- lovastatin
- vascular
- bile
- atherosclerosis
- atorvastatin
- artery
- endothelial
-
lipid-lowering
- hyperlipidemia
-
cholesterol-lowering
-
isoprenoids
- diabetes
- squalene
-
apolipoproteins
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geranylgeranylation
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farnesylation
-
high-density
- rosuvastatin
-
hypocholesterolemic
- myopathy
-
ldl-cholesterol
-
placebo
- dyslipidemias
-
hypolipidemic
- gemfibrozil
- rhabdomyolysis
-
7alpha-hydroxylase
-
lipoprotein-cholesterol
-
cholestyramine
-
fibrates
-
oxysterols
- drug development
-
srebps
- ezetimibe
-
atherogenic
-
acyl-coa:cholesterol
- molecular biology
- medicine
- lanosterol
-
isoprenylation
- 25-hydroxycholesterol
- dolichols
- cyp7a1
- biotechnology
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
1.1.1.34
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RECOMMENDED NAME
GeneOntology No.
hydroxymethylglutaryl-CoA reductase (NADPH)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
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(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
via mevaldehyde as an intermediate product
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(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Glu559 and His866 are involved in catalysis
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(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
via mevaldehyde as an intermediate product, enzyme contains a catalytic His381, Lys267 is also involved in catalysis, active site structure
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(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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}.
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CAS REGISTRY NUMBER
COMMENTARY
9028-35-7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
dual-function enzyme with acetoacetyl-coenzyme A thiolase and 3-hydroxy-3-methylglutaryl-coenzyme A reductase activities
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lobster, 2 enzyme forms: a soluble and a membrane-bound enzyme
SwissProt
lobster, 2 enzyme forms: a soluble isozyme HMGR1 and a membrane-bound isozyme HMGR2
SwissProt
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286571, 286576, 654559, 655507, 667236, 668139, 684808, 695855, 697143, 698528, 712198, 712676, 721267
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
a key enzyme in endogenous cholesterol biosynthesis in mammals and isoprenoid biosynthesis via the mevalonate pathway in other eukaryotes, archaea and some eubacteria
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
Ochromonas malhamensis
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
evolution
-
not only the sequence of the catalytic domain of enzyme HMGR but also its quaternary structure is conserved in high eukaryotes. HMGR is encoded by a multigene family
metabolism
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HMGR catalyzes the first committed step in mevalonic acid pathway for biosynthesis of isoprenoids
metabolism
-
HMG-CoA reductase is the rate-limiting enzyme of cholesterol biosynthesis
metabolism
-
HMGR catalyzes the four-electron reduction of HMGCoA to mevalonate, the committed step in the biosynthesis of sterols. Mevalonate is a precursor of isoprenoids, a class of compounds involved in several cellular functions such as cholesterol synthesis and growth control
metabolism
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3-hydroxy-3-methylglutaryl CoA reductase catalyzes the first committed step in the mevalonic acid (MVA) pathway for the biosynthesis of isoprenoids
metabolism
-
3-hydroxy-3-methylglutaryl Co-A reductase is a rate-limiting enzyme in the eukaryotic mevalonate pathway
metabolism
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HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
Ochromonas malhamensis
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
-
HMG-CoA reductase (HMGR) catalyzes the first committed step of the mevalonate pathway for isoprenoid biosynthesis, consisting in the NADPH-mediated reductive deacylation of HMG-CoA to mevalonic acid. The enzyme exerts a key regulatory role on the flux of the mevalonate pathway in all eukaryotes
metabolism
rate limiting enzyme of the ergosterol biosynthetic pathway
metabolism
the enzyme a key enzyme in the synthetic pathway of protostane triterpenes, including Alisol B 23-acetate and its derivatives
metabolism
-
3-hydroxy-3-methylglutaryl Co-A reductase is a rate-limiting enzyme in the eukaryotic mevalonate pathway
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metabolism
-
rate limiting enzyme of the ergosterol biosynthetic pathway
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physiological function
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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
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
physiological function
rate-limiting enzyme for cholesterol synthesis, regulated via a negative feedback mechanism through sterols and non-sterol metabolites derived from mevalonate
physiological function
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HMG1 is highly associated with the cell division during the early stage of fruit development which determines the final fruit size in Litchi chinensis. LcHMG2 is involved in the late stage of fruit development, in association with biosynthesis of isoprenoid compounds required for later cell enlargement
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
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated. Protein phosphatase 2A (PP2A) is both a transcriptional and a posttranslational regulator of HMGR in Arabidopsis thaliana
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
Ochromonas malhamensis
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
-
in plants, the enzyme is critical not only for normal growth and development but also for the adaptation to diverse challenging conditions. Plant HMGR is controlled at transcriptional and posttranslational levels in response to many developmental and environmental signals such as phytohormones, calcium, calmodulin, light, wounding, elicitor treatment, and pathogen attack. Protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant HMGR is posttranslationally modulated
physiological function
the enzyme plays an important role in catalyzing the first committed step of isoprenoid biosynthesis in the mevalonic acid pathway catalyzing the conversion of HMG-CoA to mevalonic acid in plants
additional information
-
modelling of the active site using crystal stucture of the enzyme with bound inhibitor simvastatin, PDB ID 1HW9, overview
additional information
structure-function analysis, overview. Identification of three characteristic sites of hydroxymethylglutaryl-CoA reductase
additional information
-
devlopment of three molecular models of human enzyme with different active site protonation states, and reaction mechanism analysis by molecular dynamics and quantum mechanics/molecular mechanics (QM/MM) calculations to detail the first reduction step, the rate-limiting step, of HMG-CoA-R
additional information
-
structure-function analysis of HMGR, homology modelling using human HMGR, PDB ID 1DQ8A, as template, overview
additional information
structure-function analysis of HMGR, homology modelling using human HMGR, PDB ID 1DQ8A, as template, overview
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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 + NADPH
mevaldehyde + CoA + NADP+
-
first step reaction
-
-
r
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
DL-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
mevaldyl-CoA + NADPH + H+ + H2O
(R)-mevalonate + CoA + NADP+
-
second step reaction
-
-
?
(R)-mevaldehyde + NADPH + H+
(R)-mevalonate + NADP+
second step of the reaction
-
-
?
(R)-mevaldehyde + NADPH + H+
(R)-mevalonate + NADP+
second step of the reaction
-
-
?
(R)-mevalonate + CoA + 2 NAD+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NAD+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
NAD(H) is the preferred cofactor
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Ochromonas malhamensis
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R,S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(R,S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + 2 NADP+ + CoA
-
-
-
-
-
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + 2 NADP+ + CoA
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + 2 NADP+ + CoA
-
HMGR is a key enzyme in the mevalonate pathway of isoprenoid biosynthesis, the sole route in haloarchaea for lipid and carotenoid production
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
overall reaction
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
overall reaction
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
Ochromonas malhamensis
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
enzyme is essential for sterol biosynthesis
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
involved in isopentenyl diphosphate biosynthesis, mevalonate pathway overview
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
overall reaction
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
overall reaction
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
the reduction of 3-hydroxy-3-methylglutaryl-CoA is preferred over oxidation of mevalonate
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevaldyl-CoA + NADP+
-
first step reaction
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevaldyl-CoA + NADP+
-
first step reaction
-
-
r
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
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
-
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
-
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
ir
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?, r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
first step reaction
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
substrate is (S)-isomer of HMG-CoA
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
substrate is (S)-isomer of HMG-CoA
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
up- and down-regulation of HMGR activity in response to changes in the flux of the mevalonate pathway occur via post-translational control
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
key enzyme of the mevalonic acid pathway catalysing the first committed step with NADPH as cofactor, overview
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
HMGR is the key regulatory enzyme of the mevalonate pathway and also the iridoid biosynthesis, it is highly regulated itself, HMGR may represent a regulator in maintenance of homeostasis between de novo produced and sequestered intermediates of iridoid metabolism, overview
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
the enzyme utilizes two molecules of NADPH to mediate the four-electron reduction of HMG-CoA to the carboxylic acid mevalonate, homology modeling of the catalytic domain
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
mevaldehyde + NADPH
(R)-mevalonate + NADP+
-
second step reaction
-
-
r
additional information
?
-
the enzyme is involved in the synthesis of the protostane triterpene Alisol B 23-acetate
-
-
-
additional information
?
-
-
phytosterol biosynthetic pathway, overview
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
the substrates of the reductive reaction, HMG-CoA and NADH, both demonstrate sigmoidal behavior typical of positive cooperativity
-
-
-
additional information
?
-
-
the substrates of the reductive reaction, HMG-CoA and NADH, both demonstrate sigmoidal behavior typical of positive cooperativity
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
HMGR can accelerate the biosynthesis of carotenoids in the Escherichia coli transformant, it plays an influential role in isoprenoid biosynthesis
-
-
-
additional information
?
-
-
HMGR can accelerate the biosynthesis of carotenoids in the Escherichia coli transformant, it plays an influential role in isoprenoid biosynthesis
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
HMG-CoA reductase is regulated by salinity at the level of transcription
-
-
-
additional information
?
-
-
the expression of HMGR is regulated in response to non-optimal salinity in the halophilic archaeon
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
enzyme plays a central role in sterol biosynthesis, investigation of the physiological regulation, 3-hydroxy-3-methylglutaryl CoA reductase and C24-sterol methyltransferase type 1 work in concert to control carbon flux into end-product sterols
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
the reaction is a highly regulated process within the cholesterol biosynthetic pathway
-
-
-
additional information
?
-
-
method development for rapid and versatile reverse phase -HPLC monitoring for assaying HMGR activity capable of monitoring the levels of both substrates HMG-CoA and NADPH, and products CoA, mevalonate, and NADP+, method evaluation, overview
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
ubiquitination and proteasomal degradation of microsomal, but not mitochondrial, HMGR isozymes depends on environmental salinity, overview
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
rate-limiting enzyme in the biosynthesis of cholesterol in mammals
-
-
-
additional information
?
-
-
small heterodimer partner nuclear receptor directly regulates cholesterol biosynthesis through inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase
-
-
-
additional information
?
-
-
biphasic regulation of HMG-CoA reductase expression and activity during wound healing and its functional role in the control of keratinocyte angiogenic and proliferative responses, overview
-
-
-
additional information
?
-
-
biphasic regulation of HMG-CoA reductase expression and activity during wound healing and its functional role in the control of keratinocyte angiogenic and proliferative responses, overview
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
Ochromonas malhamensis
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
HMGR activity is not only diminished in iridoid producers but most likely prevalent within the Chrysomelina subtribe and also within the insecta
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
enzyme undergoes endoplasmic reticulum-associated degradation which is physiologically regulated by sterol pathway signals, determination of structural features leading to modification and degradation by the quality control system of the endoplasmic reticulum, overview
-
-
-
additional information
?
-
enzyme in the pathway for production of prenyl alcohols. Almost all Saccharomyces cerevisiae strains tend to produce mainly squalene and low amount of prenyl alcohols. Among these ATCC strains, relatively large amounts of prenyl alcohols in the cultures of two recombinants (ATCC201741 and ATCC 200027). Amounts are quite low compared to the case of ATCC 200589 recombinant. These differences possibly depend on the difference in the squalene synthase activity. If the enzyme activity is weaker in ATCC 200589, the activation of the pathways will result in the accumulation of (E,E)-farnesyl diphosphate, the substrate of the enzyme, and following production of (E,E)-farnesol through hydrolysis of (E,E)-farnesyl diphosphate. Recombinant AURGG101 derived from ATCC 200589 produces large amounts of prenyl alcohols. In particular, (E,E)-farnesol in AURGG101 reaches 35.6 mg/l, which is approximately 4fold higher than that in ATCC 200589. HMG1 expression in strain ATCC 200589 increases the production of squalene, (E)-nerolidol, (E,E)-farnesol, and (E,E,E)-geranylgeraniol, whereas that in ATCC 76625 causes high squalene production, low production of (E,E)-farnesol and (E,E,E)-geranylgeraniol, and no (E)-nerolidol production
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
additional information
?
-
-
assay method development: the eukaryotic enzyme HMGR catalyzes the stereospecific NADPH-dependent reductive deacylation of (3S)-HMG-CoA to (3R)-mevalonic acid. The HMGR assay reaction product is subsequently converted to mevalonolactone by heating in acid medium. The heat treatment also hydrolyses (S)-3-hydroxy-3-methylglutaryl-CoA to free hydroxy-3-methylglutaric acid and CoASH, analysis by TLC
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
(R)-mevalonate + CoA + 2 NAD+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
B4EKH5
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + 2 NADP+ + CoA
-
HMGR is a key enzyme in the mevalonate pathway of isoprenoid biosynthesis, the sole route in haloarchaea for lipid and carotenoid production
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevaldyl-CoA + NADP+
-
first step reaction
-
-
?
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonolactone + CoA + 2 NADP+ + H2O
-
rate-limiting step of cholesterol biosynthesis
-
-
r
D-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
mevaldyl-CoA + NADPH + H+ + H2O
(R)-mevalonate + CoA + NADP+
-
second step reaction
-
-
?
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
F1DTB9
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
W6APW1
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
I7CKJ5
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
I7CKJ5
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Ochromonas malhamensis
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
Ochromonas malhamensis
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
Q1W675
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
enzyme is essential for sterol biosynthesis
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
involved in isopentenyl diphosphate biosynthesis, mevalonate pathway overview
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
-
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
-
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
ir
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
Q980N1
-
-
-
-
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
Q980N1
-
-
-
-
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
up- and down-regulation of HMGR activity in response to changes in the flux of the mevalonate pathway occur via post-translational control
-
-
?
3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
key enzyme of the mevalonic acid pathway catalysing the first committed step with NADPH as cofactor, overview
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
B2KX91
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
HMGR is the key regulatory enzyme of the mevalonate pathway and also the iridoid biosynthesis, it is highly regulated itself, HMGR may represent a regulator in maintenance of homeostasis between de novo produced and sequestered intermediates of iridoid metabolism, overview
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
-
-
-
-
?
additional information
?
-
F1DTB9
the enzyme is involved in the synthesis of the protostane triterpene Alisol B 23-acetate
-
-
-
additional information
?
-
-
phytosterol biosynthetic pathway, overview
-
-
-
additional information
?
-
A0N0D3
HMGR can accelerate the biosynthesis of carotenoids in the Escherichia coli transformant, it plays an influential role in isoprenoid biosynthesis
-
-
-
additional information
?
-
-
HMGR can accelerate the biosynthesis of carotenoids in the Escherichia coli transformant, it plays an influential role in isoprenoid biosynthesis
-
-
-
additional information
?
-
-
HMG-CoA reductase is regulated by salinity at the level of transcription
-
-
-
additional information
?
-
-
the expression of HMGR is regulated in response to non-optimal salinity in the halophilic archaeon
-
-
-
additional information
?
-
-
enzyme plays a central role in sterol biosynthesis, investigation of the physiological regulation, 3-hydroxy-3-methylglutaryl CoA reductase and C24-sterol methyltransferase type 1 work in concert to control carbon flux into end-product sterols
-
-
-
additional information
?
-
-
the reaction is a highly regulated process within the cholesterol biosynthetic pathway
-
-
-
additional information
?
-
-
ubiquitination and proteasomal degradation of microsomal, but not mitochondrial, HMGR isozymes depends on environmental salinity, overview
-
-
-
additional information
?
-
-
small heterodimer partner nuclear receptor directly regulates cholesterol biosynthesis through inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase
-
-
-
additional information
?
-
-
biphasic regulation of HMG-CoA reductase expression and activity during wound healing and its functional role in the control of keratinocyte angiogenic and proliferative responses, overview
-
-
-
additional information
?
-
-
biphasic regulation of HMG-CoA reductase expression and activity during wound healing and its functional role in the control of keratinocyte angiogenic and proliferative responses, overview
-
-
-
additional information
?
-
-
HMGR activity is not only diminished in iridoid producers but most likely prevalent within the Chrysomelina subtribe and also within the insecta
-
-
-
additional information
?
-
-
enzyme undergoes endoplasmic reticulum-associated degradation which is physiologically regulated by sterol pathway signals, determination of structural features leading to modification and degradation by the quality control system of the endoplasmic reticulum, overview
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
-
286557, 286559, 286560, 286561, 286565, 286567, 286568, 286569, 286572, 286573, 286574, 654375, 685520, 685531, 688473
NADPH
-
-
additional information
the enzyme prefers NAD(H) over NADP(H) as a cofactor, suggesting an oxidative physiological role for the enzyme
-
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
NaCl