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Information on EC 1.1.1.34 - hydroxymethylglutaryl-CoA reductase (NADPH) and Organism(s) Cricetulus griseus and UniProt Accession P00347

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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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Cricetulus griseus
UNIPROT: P00347
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Word Map
The taxonomic range for the selected organisms is: Cricetulus griseus
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
HMG-CoA reductase
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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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-
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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HMDH_CRIGR
887
5
97081
Swiss-Prot
Secretory Pathway (Reliability: 4)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A333P
mutation disrupts Insig binding and abolishes sterol-accelerated degradation. The pivotal event for sterol-induced degradation of the choletsreol biosynthetic enzyme HMG-CoA reductase is binding of its membrane domain to Insig proteins in the endoplasmic reticulum. Insig are carriers for gp78, an E3 ubiquitin ligase that marks reductase for proteasomal degradation
G87R
mutation disrupts Insig binding and abolishes sterol-accelerated degradation. The pivotal event for sterol-induced degradation of the choletsreol biosynthetic enzyme HMG-CoA reductase is binding of its membrane domain to Insig proteins in the endoplasmic reticulum. Insig are carriers for gp78, an E3 ubiquitin ligase that marks reductase for proteasomal degradation
S60N
mutation disrupts Insig binding and abolishes sterol-accelerated degradation. The pivotal event for sterol-induced degradation of the choletsreol biosynthetic enzyme HMG-CoA reductase is binding of its membrane domain to Insig proteins in the endoplasmic reticulum. Insig are carriers for gp78, an E3 ubiquitin ligase that marks reductase for proteasomal degradation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, P.C.; Nguyen, A.D.; Debose-Boyd, R.A.
Mutations within membrane domain of HMG CoA reductase confer resistance to sterol-accelerated degradation
J. Lipid Res.
48
318-327
2006
Cricetulus griseus (P00347), Cricetulus griseus
Manually annotated by BRENDA team