HMGCR dimer reduces bHMG-CoA to MVA

Stable Identifier
R-HSA-191352
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
(3S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H(+) => (R)-mevalonate + 2 NADP(+) + CoA
ReviewStatus
5/5
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Dimeric 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR dimer) (Istvan et al. 2000) catalyzes the four-electron reduction of beta-hydroxy-beta-methylglutaryl-CoA (bHMG-CoA) to mevalonate (MVA). MVA concentrations in the cell are tightly controlled through regulation of the activity of HMGCR dimer, which is one of the most highly regulated enzymes in metabolism (Goldstein & Brown 1990).
Literature References
PubMed ID Title Journal Year
10698924 Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis

Istvan, ES, Palnitkar, M, Buchanan, SK, Deisenhofer, J

EMBO J 2000
1967820 Regulation of the mevalonate pathway

Goldstein, JL, Brown, MS

Nature 1990
Participants
Participates
Catalyst Activity

hydroxymethylglutaryl-CoA reductase (NADPH) activity of HMGCR dimer [endoplasmic reticulum membrane]

Orthologous Events
Cross References
RHEA
Authored
Reviewed
Created
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