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Information on EC 1.1.1.34 - hydroxymethylglutaryl-CoA reductase (NADPH) and Organism(s) Saccharolobus solfataricus and UniProt Accession Q980N1

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EC Tree
IUBMB Comments
The enzyme is inactivated by EC 2.7.11.31 {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} and reactivated by EC 3.1.3.47 {[hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase}.
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This record set is specific for:
Saccharolobus solfataricus
UNIPROT: Q980N1
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Word Map
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
Synonyms
hmg-coa reductase, hmgcr, 3-hydroxy-3-methylglutaryl coenzyme a reductase, hmgr, hmg coa reductase, 3-hydroxy-3-methylglutaryl-coa reductase, 3-hydroxy-3-methylglutaryl-coenzyme a reductase, hmgcoa reductase, 3-hydroxy-3-methylglutaryl coa reductase, hmg-coar, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-hydroxy-3-methylglutaryl-CoA reductase
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3-hydroxy-3-methylglutaryl-CoA reductase (NADPH)
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beta-hydroxy-beta-methylglutaryl coenzyme A reductase
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beta-hydroxy-beta-methylglutaryl-Co A reductase
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HMG-CoA reductase
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HMG2.2
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HMG3.3
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HMGCoA reductase-mevalonate:NADP-oxidoreductase (acetylating CoA)
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HMGR
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HMGR1
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HMGR2
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hydroxymethylglutaryl CoA reductase (NADPH)
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hydroxymethylglutaryl-coenzyme A reductase (reduced nicotinamide adenine dinucleotide phosphate)
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mevalonate:NADP+ oxidoreductase (acetylating CoA)
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NADPH-hydroxymethylglutaryl-CoA reductase
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S-3-hydroxy-3-methylglutaryl-CoA reductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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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}.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-35-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
show the reaction diagram
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
show the reaction diagram
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r
(R)-mevalonate + CoA + NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
show the reaction diagram
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r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
show the reaction diagram
mevaldehyde + NADPH + H+
(R)-mevalonate + NADP+
show the reaction diagram
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additional information
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
show the reaction diagram
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?
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
show the reaction diagram
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lovastatin
competitive inhibitor for HMG-CoA binding site
Mevinolin
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competitive with 3-hydroxy-3-methylglutaryl-CoA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
3-hydroxy-3-methylglutaryl-CoA
0.023
NADPH
0.0015 - 0.0017
(R)-mevalonate
0.045 - 0.076
3-hydroxy-3-methylglutaryl-CoA
0.00011 - 0.00015
CoASH
0.045 - 0.076
HMG-CoA
0.0043 - 0.0063
mevaldehyde
0.0009 - 0.0013
NADP+
0.055 - 0.083
NADPH
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000005
Mevinolin
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pH 5.5, 50°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17.5
50°C, pH 5.5, recombinant enzyme
3.9
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50°C, mutant L403R/G404R/A406S
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
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oxidative acylation of (R,S)-mevaldehyde or mevalonate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L403R/G404R/A406S
synthesis
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due to use of rare codon, expression of enzyme in Escherichia coli is poor. Coexpression of the S. solfataricus hmgA gene with the argU gene that encodes tRNAAGA,AGG resulted in an over 10-fold increase in enzyme yield
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
coexpression of the Sulfolobus solfataricus hmgA gene in Escherichia coli with the argU gene that encodes tRNAAGA,AGG results in an over 10fold increase in enzyme yield
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expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bochar, D.A.; Brown, J.R.; Doolittle, W.F.; Klenk, H.P.; Lam, W.; Schenk, M.E.; Stauffacher, C.V.; Rodwell, V.W.
3-Hydroxy-3-methylglutaryl coenzyme A reductase of Sulfolobus solfataricus: DNA sequence, phylogeny, expression in Escherichia coli of the hmgA gene, and purification and kinetic properties of the gene product
J. Bacteriol.
179
3632-3638
1997
Saccharolobus solfataricus (Q980N1), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q980N1), Saccharolobus solfataricus P2
Manually annotated by BRENDA team
Kim, D.Y.; Bochar, D.A.; Stauffacher, C.V.; Rodwell, V.W.
Expression and characterization of the HMG-CoA reductase of the thermophilic archaeon Sulfolobus solfataricus
Protein Expr. Purif.
17
435-442
1999
Saccharolobus solfataricus
Manually annotated by BRENDA team
Kim, D.Y.; Bochar, D.A.; Stauffacher, C.V.; Rodwell, V.W.
Engineering of Sulfolobus solfataricus HMG-CoA reductase to a form whose activity is regulated by phosphorylation and dephosphorylation
Biochemistry
39
2269-2275
2000
Saccharolobus solfataricus
Manually annotated by BRENDA team