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(R)-mevaldehyde + NADPH + H+
(R)-mevalonate + NADP+
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
-
-
-
-
r
(R,S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
(R,S)-mevaldehyde + acetate
?
-
-
-
-
?
(R,S)-mevaldehyde + NADPH
?
-
-
-
-
?
(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 + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
-
-
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevaldehyde + CoA + NADP+
-
first step reaction
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevaldyl-CoA + NADP+
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonolactone + CoA + 2 NADP+ + H2O
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevalonate + CoA + NADP+
-
-
-
-
?
acetyl-CoA
acetoacetyl-CoA + CoA
-
-
-
-
r
D-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
r
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
DL-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
-
-
-
-
?
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
mevaldehyde + NADPH + H+
(R)-mevalonate + NADP+
mevaldyl-CoA + H2O
mevaldehyde + NADP+
-
second step reaction
-
-
r
mevaldyl-CoA + NADPH + H+ + H2O
(R)-mevalonate + CoA + NADP+
-
second step reaction
-
-
?
additional information
?
-
(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 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)-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
-
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+
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
enzyme is essential for sterol biosynthesis
-
-
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+
-
involved in isopentenyl diphosphate biosynthesis, mevalonate pathway overview
-
-
r
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
overall reaction
-
-
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+
-
-
-
-
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+
-
-
-
-
?
(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+
the enzyme is implicated in latex metabolism
-
-
?
(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 + 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+
-
-
-
-
?
(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+
-
-
-
?
(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+
-
overall reaction
-
-
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+
-
the reduction of 3-hydroxy-3-methylglutaryl-CoA is preferred over oxidation of mevalonate
-
-
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+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevaldyl-CoA + NADP+
-
first step reaction
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevaldyl-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 + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
-
-
-
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+
-
-
-
-
?
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+
-
-
286557, 286559, 286560, 286561, 286565, 286567, 286568, 286569, 286572, 286573, 286574 -
-
?
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
(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
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+
-
-
-
-
?
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 + H+
(R)-mevalonate + NADP+
-
second step reaction
-
-
r
mevaldehyde + NADPH + H+
(R)-mevalonate + NADP+
-
-
-
-
?
mevaldehyde + NADPH + H+
(R)-mevalonate + NADP+
-
third step reaction
-
-
r
mevaldehyde + NADPH + H+
(R)-mevalonate + NADP+
-
-
-
-
?
additional information
?
-
the enzyme is involved in the synthesis of the protostane triterpene Alisol B 23-acetate
-
-
?
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
?
-
-
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
?
-
no substrate: NADH
-
-
?
additional information
?
-
-
no substrate: NADH
-
-
?
additional information
?
-
no substrate: NADH
-
-
?
additional information
?
-
-
no substrate: NADH
-
-
?
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
?
-
-
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
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additional information
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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?
additional information
?
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-
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
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?
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
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?
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
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?
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
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?
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
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(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
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(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
mevaldyl-CoA + NADP+
-
first step reaction
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?
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonolactone + CoA + 2 NADP+ + H2O
-
rate-limiting step of cholesterol biosynthesis
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-
r
3-hydroxy-3-methylglutaryl-CoA + NADPH
(R)-mevalonate + CoA + NADP+
3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
acetyl-CoA
acetoacetyl-CoA + CoA
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-
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r
D-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
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r
D-3-hydroxy-3-methylglutaryl-CoA + NADPH
mevalonate + CoA + NADP+
hydroxymethylglutaryl-CoA + NADPH + H+
mevalonate + NADP+ + CoA
mevaldyl-CoA + NADPH + H+ + H2O
(R)-mevalonate + CoA + NADP+
-
second step reaction
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additional information
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(R)-mevalonate + CoA + 2 NADP+
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
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-
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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)-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
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-
-
-
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+
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
enzyme is essential for sterol biosynthesis
-
-
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+
-
involved in isopentenyl diphosphate biosynthesis, mevalonate pathway overview
-
-
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+
-
-
-
-
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+
the enzyme is implicated in latex metabolism
-
-
?
(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+
-
-
-
-
?
(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+
-
-
-
-
?
(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+
-
-
-
?
(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+
-
-
-
-
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 + 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+
-
-
-
-
?
(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
(R)-mevalonate + CoA + 2 NADP+
-
-
-
-
?
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
-
-
-
-
r
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 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+
-
-
-
-
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+
-
-
286557, 286559, 286560, 286561, 286565, 286567, 286568, 286569, 286572, 286573, 286574 -
-
?
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+
-
-
-
-
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
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
-
-
-
?
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
?
-
the enzyme is involved in the synthesis of the protostane triterpene Alisol B 23-acetate
-
-
?
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
?
-
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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(3R,5R)-7-(1-ethyl-3-(4-fluorophenyl)-4-methyl-5-[(5-methyl-pyrazin-2-ylmethyl)-carbamoyl]-1H-pyrrol-2-yl)-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-4-methyl-5-phenylcarbamoyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
-
-
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-5-(4-methoxybenzylcarbamoyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-5-(4-methoxycarbonyl-benzylcarbamoyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[3-(4-fluoro-phenyl)-1-isopropyl-5-phenylcarbamoyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[3-(4-fluorophenyl)-1-isopropyl-4-phenyl-5-phenylcarbamoyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[3-(4-fluorophenyl)-5-[(3-methoxybenzyl)carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
(3R,5R)-7-[3-(4-fluorophenyl)-5-[[4-(methoxymethyl)benzyl]carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
(3R,5R)-7-[5-(4-carboxy-benzylcarbamoyl)-ethyl-3-(4-fluorophenyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid disodium salt
-
-
(3R,5R)-7-[5-benzylcarbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid
-
-
(3R,5R)-7-[5-carbamoyl-1-ethyl-3-(4-fluorophenyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
-
-
(3R,5R)-7-[5-carbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid sodium salt
-
-
(3R,5R)-7-[5-cyano-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
-
-
(3R,5R)-7-[5-[(3-carbamoylbenzyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
(3R,5R)-7-[5-[(4-cyanobenzyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
(3R,5R)-7-[5-[[4-(dimethylcarbamoyl)benzyl]carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
(5S)-5-hydroxy-4-{2-[(1S,2R,4aR)-1,2,4a,5-tetramethyl-1,2,3,4,4a,7,8,8a-octahydronaphthalen-1-yl]ethyl}furan-2(5H)-one
-
22.65% inhibition of HMG-CoA reductase at 0.001 mM concentration and maximum inhibition of 78.03% at 0.1 mM, the HMG-CoA reductase inhibitor, a clerodane diterpene from ethanolic extract of Polyalthia longifolia var. pendula, is a potential lipid lowering agent, molecular docking analysis, overview
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoic acid
-
competitive inhibitor, shows slight inhibitory activity
(R)-3-hydroxy-3-methylglutaryl-CoA
-
competitive inhibitor
(S)-4-carboxy-3-hydroxy-3-methylbutyryl-CoA
-
competitive inhibitor
(S)-4-carboxy-3-hydroxybutyryl-CoA
-
competitive inhibitor
3,3-dimethylglutaryl-CoA
-
competitive inhibitor
3-hydroxy-3-methylglutaryl-CoA
-
0.05 mM
3-hydroxyglutaryl-CoA
-
competitive inhibitor
3-methylglutaryl-CoA
-
competitive inhibitor
4-[[([5-[(3R,5R)-6-carboxy-3,5-dihydroxyhexyl]-4-(4-fluorophenyl)-1-(1-methylethyl)-3-phenyl-1H-pyrrol-2-yl]carbonyl)amino]methyl]benzoic acid
-
-
7-[3,4-bis(4-fluorophenyl)-1-(1-methylethyl)-5-(phenylcarbamoyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3,4-bis(4-fluorophenyl)-5-[(3-hydroxyphenyl)carbamoyl]-1-(1-methylethyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3,4-bis(4-fluorophenyl)-5-[(3-methoxyphenyl)carbamoyl]-1-(1-methylethyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-(phenylcarbamoyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-(propylcarbamoyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-[(4-sulfamoylphenyl)carbamoyl]-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-[(pyridin-2-ylmethyl)carbamoyl]-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-5-[[(4-methyl-1,3-thiazol-2-yl)methyl]carbamoyl]-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-5-[[(5-methyl-1H-imidazol-2-yl)methyl]carbamoyl]-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-5-[[(5-methyl-1H-pyrazol-3-yl)methyl]carbamoyl]-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-5-(methylcarbamoyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-5-[(4-hydroxyphenyl)carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[3-(4-fluorophenyl)-5-[(4-methoxybenzyl)carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-(benzylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-(cyclopropylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-(dimethylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-(ethylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-carbamoyl-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-ethylcarbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
-
-
7-[5-[(4-carbamoylphenyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-[(4-carboxyphenyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-[[(1,5-dimethyl-1H-pyrazol-3-yl)methyl]carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-[[3-(dimethylcarbamoyl)phenyl]carbamoyl]-3,4-bis(4-fluorophenyl)-1-(1-methylethyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
7-[5-[[4-(dimethylcarbamoyl)phenyl]carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
-
-
8-hydroxygeraniol
-
competitive inhibition mechanism, binds at the catalytic site, docking experiments, overview
adenosine-2'-monophospho-5'-diphosphoribose
-
competitive inhibitor for NADPH binding site
alpha-asarone
-
9.4% inhibition at 0.1 mM
brutieridin
i.e. hesperetin 7-(2''-alpha-rhamnosyl-6''-(3''''-hydroxy-3''''-methylglutaryl)-beta-D-glucoside), a flavonoid conjugate from bergamot fruit extract, structural analogue of statins, computational study, overview
ceramide
-
treatment with exogenous ceramides, or increasing the endogenous ceramide levels inhibits HMGCR by 6080%
CoA disulfide
-
no inactivation in presence of NADPH 1 mM, or HMG-CoA 0.5 mM
daidzein
-
isoflavone, isolated and purified from korean soybean paste, structural analysis
digitonine
-
2% digitonin, 80% inhibition
EDTA
-
inhibits the subsequent reactions of the mevalonate pathway in Hevea latex
eicosapentaenoic acid
-
inhibits translation of the enzyme about 50% at 0.15 mM, downregulation, slightly increases downregulation of protein synthesis by cycloheximide
F(4-fluoro)VAE
-
HMG-CoA competitive inhibitor
FVAE
-
HMG-CoA competitive inhibitor
genistein
-
isoflavone, isolated and purified from korean soybean paste, structural analysis
GFPDGG
-
designed on the basis of the rigid peptide backbone, increases the inhibitory potency more than 300 times compared to the first isolated LPYP from soybean, overview
GFPEGG
-
HMG-CoA competitive inhibitor
GLPDGG
-
NADPH and HMG-CoA competitive inhibitor
GLPEGG
-
NADPH and HMG-CoA competitive inhibitor
glycitein
-
isoflavone, isolated and purified from korean soybean paste, structural analysis
IAVE
-
HMG-CoA competitive inhibitor
IAVP
-
NADPH competitive inhibitor
IAVPGEVA
-
isolated from soybean by pepsin
Ile-Ala-Val-Pro-Gly-Glu-Val-Ala
-
-
IVAE
-
HMG-CoA competitive inhibitor
melitidin
i.e. naringenin 7-(2''-alpha-rhamnosyl-6''-(3''''-hydroxy-3''''-methylglutaryl)-beta-D-glucoside), a flavonoid conjugate from bergamot fruit extract, structural analogue of statins, computational study, overview
methyl (2-methoxy-5-nitro-4-propylphenoxy)acetate
-
96.8% inhibition at 0.1 mM
methyl (4-ethyl-2-nitrophenoxy)acetate
-
84.9% inhibition at 0.1 mM
Mevinolin
-
competitive with 3-hydroxy-3-methylglutaryl-CoA
myriocin
-
concomitant reduction of both HMGR activity and the sterol content by depletion of the sphingolipid pathway. At 0.01 mM myriocin decrease to ca. 55% of the HMGR activity in control plants. Myriocin-induced down-regulation of HMGR activity is exerted at the post-translational level, like the regulatory response of HMGR to enhancement or depletion of the flux through the sterol pathway
p-chloromercuribenzoate
-
1 mM, complete inhibition
resveratrol
inhibits the cell growth as well as the activity of recombinant enzyme. Resveratrol shows antitrypanosomal activity with an IC50 value of 0.00013 mM and moderate antipromastigote activity against Leishmania major with IC50 value: 0.153 mM
SFGYVAE peptide
-
most active inhibitory peptide; shows high ability to inhibit HMGR by competitive inhibition with respect to (S)-3-hydroxy-3-methylglutaryl-CoA
small heterodimer partner nuclear receptor
-
directly regulates cholesterol biosynthesis through inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase
-
SMase C
-
treatment of fibroblasts with SMase C results in a 90% inhibition of HMGCR
-
SMase D
-
treatment of fibroblasts with SMase D inhibits by 29%
-
sodium (E,3R,5S)-7-(2-(2-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
-
has almost no effect on the activity
sodium (E,3R,5S)-7-(2-(3-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
-
-
sodium (E,3R,5S)-7-(2-(4-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
-
shows the most potent inhibitory activity among compounds comparable with that of clinically useful mevastatin
sodium (E,3R,5S)-7-(2-phenyl-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxyhept-6-enoate
-
has almost no effect on the activity
sodium (E,3R,5S)-7-(4-(3-(2-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
-
-
sodium (E,3R,5S)-7-(4-(3-(3-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
-
-
sodium (E,3R,5S)-7-(4-(3-phenylpentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
-
-
squalestatin
-
mutant plants, not wild-type plants, become sterile
YAVE
-
HMG-CoA competitive inhibitor
YVAE
-
HMG-CoA competitive inhibitor
atorvastatin
-
-
atorvastatin
-
has a differentiating effect on wild-type and mutant forms of the human protein
atorvastatin
inhibits the cell growth as well as the activity of recombinant enzyme, 315.5 nM are enough to cause 50% recombinant LdHMGR enzyme inhibition, 93.2% inhibition at 0.001 mM
cerivastatin
-
-
cerivastatin
-
biphasic inhibition mechanism, slow, tight-binding type of inhibitor
CoASH
-
-
Compactin
-
competitive inhibitor for HMG-CoA binding site
cycloheximide
-
downregulation of protein synthesis, synergistic with eicosapentanoic acid and myristic acid
fluvastatin
-
-
fluvastatin
-
has a differentiating effect on wild-type and mutant forms of the human protein
fluvastatin
-
competitive inhibitor
fluvastatin
-
competitive
GFPTGG
-
HMG-CoA competitive inhibitor; NADPH and HMG-CoA competitive inhibitor
GFPTGG
-
competitive, effects on enzyme Michaelis-Menten kinetics, overview
GLPTGG
-
NADPH and HMG-CoA competitive inhibitor
Hydroxymethylglutarate
-
2 mM, slightly inhibitory
Hydroxymethylglutarate
-
-
lovastatin
-
-
lovastatin
-
no effect of lovastatin on the growth curve of Hortaea werneckii in salt-free media, whereas remarkably reduced growth in the otherwise physiologically optimal medium containing 17% NaCl, an effect even more pronounced in hypersaline medium containing 25% NaCl. Inhibition of HMGR in vivo by lovastatin impairs the halotolerant character
lovastatin
-
the representative of the statin class of drugs that in their active hydrolysed form are specific inhibitors of the enzyme
lovastatin
-
slightly inhibitory statin for class II enzyme, binding structure at the active site involves the residues Lys267, Asn271, Glu83, Arg261, and 2 water molecules, substrate mimicking binding mode
lovastatin
-
competitive inhibitor for HMG-CoA binding site
lovastatin
competitive inhibitor for HMG-CoA binding site
lovastatin
-
competitive inhibitor for HMG-CoA binding site and noncompetitive inhibitor for NADPH binding site
mevastatin
-
MgATP2-
-
4 mM
p-hydroxymercuribenzoate
-
0.01 mM inhibited 97% of reduction
p-hydroxymercuribenzoate
-
3.7 mM, complete inhibition
pravastatin
-
-
pravastatin
inhibitory in the presence of increasing concentrations of NADPH, but increasing concentrations of HMG-CoA block the HMG-CoA reductase-inhibiting activity
rosuvastatin
-
thermodynamics of binding and inhibition mechanism, Glu559 is involved, reversible, 2-step complex formation, competitive with respect to 3-hydroxy-3-methylglutaryl-CoA, non-competitive to NADPH
simvastatin
-
-
simvastatin
-
does not allow differentiation between the wild-type and mutant forms of the human protein
simvastatin
inhibits the cell growth as well as the activity of recombinant enzyme, 63% inhibition at 0.1 mM
simvastatin
-
enzyme inhibition causes 40% reduction of wound healing, inhibition of HMGR activity during acute wound healing interferes with keratinocyte VEGF production and proliferation at the wound site, overview
additional information
-
whether plants are grown with mevalonate from the beginning or only during the last 9 days, HMGR activity is drastically reduced to 25% of the activity in plants grown in the absence of mevalonate. Plants grown without mevalonate during the last 9 days show a severe, though less pronounced, reduction in HMGR activity, which decreases to 60% of the activity in control plants. Significant reduction of HMGR activity does not correlate with changes in both the expression of HMG1 and HMG2 genes and the amount of HMGR protein
-
additional information
no inhibition by farnesoate and farnesoic acid
-
additional information
no inhibition by farnesoate and farnesoic acid
-
additional information
-
no inhibition by farnesoate and farnesoic acid
-
additional information
-
27-hydroxycholesterol strongly supresses the expression of HMGR, the in vivo inhibition of sterol 27-hydroxylase CYP27A1, e.g. by the drugs rapamycin and cyclosporine A, reduces the inhibition and thus increases HMGR activity, overview
-
additional information
screening of eight-membered medium ring lactams and related tricyclic compounds, either seven-membered lactams, thiolactams or amines, for inhibitory potency, overview. The compounds are inhibitory also in the presence of increasing concentrations of NADPH, and are not affected by increasing concentrations of HMG-CoA. Medium ring lactams and existing statins may have different mechanisms of enzyme interaction and inhibition, molecular docking studies and comparisons using the HMG-CoA reductase statin-binding receptor model, overview. The ligands may occupy a narrow channel housing the pyridinium moiety on NADP+
-
additional information
-
screening of eight-membered medium ring lactams and related tricyclic compounds, either seven-membered lactams, thiolactams or amines, for inhibitory potency, overview. The compounds are inhibitory also in the presence of increasing concentrations of NADPH, and are not affected by increasing concentrations of HMG-CoA. Medium ring lactams and existing statins may have different mechanisms of enzyme interaction and inhibition, molecular docking studies and comparisons using the HMG-CoA reductase statin-binding receptor model, overview. The ligands may occupy a narrow channel housing the pyridinium moiety on NADP+
-
additional information
-
methanolic extracts of Quercus infectoria galls, Rosa damascena flowers, and Myrtus communis leaves inhibit the enzyme activity noncompetitively to 84%, 70%, and 62%, respectively. Extracts of diverse other plants are also inhibitory for the enzyme, detailed overview
-
additional information
statins are potent enzyme inhibitors that bind to the active site where also the natural substrate binds, used widely in the treatment of hypercholesterolemia
-
additional information
-
design of highly potent and competitive inhibitory peptides for 3-hydroxy-3-methylglutaryl CoA reductase, no inhibition with SFGYVAG peptide
-
additional information
-
the activity of microsomal isoyzme Hmg2 is highest under hypo-saline and extremely hyper-saline conditions, and down-regulated under optimal growth conditions
-
additional information
exogenous supplementation of ergosterol in case of atorvastatin and resveratrol treated cells causes complete reversal of growth inhibition whereas simvastatin is ergosterol refractory
-
additional information
-
exogenous supplementation of ergosterol in case of atorvastatin and resveratrol treated cells causes complete reversal of growth inhibition whereas simvastatin is ergosterol refractory
-
additional information
-
inhibition potency of inhibitors in hepatocytes, myocytes and on purified enzyme, overview
-
additional information
-
no inhibition by geraniol or by its glucoside and thioglucoside
-
additional information
-
discovery, synthesis, and optimization of substituted pyrrole-based hepatoselective ligands as potent inhibitors of HMG-CoA reductase for reducing low density lipoprotein cholesterol (LDL-c) in the treatment of hypercholesterolemia
-
additional information
-
design, synthesis and evaluation of structure-based peptide inhibitors, computational methods, overview
-
additional information
-
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)phenyl)-3,5-dihydroxyhept-6-enoic acid shows no apparent HMGR inhibitory activity even at 100 mM
-
additional information
-
the hybrid is resistant to race 0 of Phytophtora infestans
-
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0.00000035
(3R,5R)-7-(1-ethyl-3-(4-fluorophenyl)-4-methyl-5-[(5-methyl-pyrazin-2-ylmethyl)-carbamoyl]-1H-pyrrol-2-yl)-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000029
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-4-methyl-5-phenylcarbamoyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000024
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-5-(4-methoxybenzylcarbamoyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000028
(3R,5R)-7-[1-ethyl-3-(4-fluorophenyl)-5-(4-methoxycarbonyl-benzylcarbamoyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000017
(3R,5R)-7-[3-(4-fluoro-phenyl)-1-isopropyl-5-phenylcarbamoyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000043
(3R,5R)-7-[3-(4-fluorophenyl)-1-isopropyl-4-phenyl-5-phenylcarbamoyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.0000018
(3R,5R)-7-[3-(4-fluorophenyl)-5-[(3-methoxybenzyl)carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000007
(3R,5R)-7-[3-(4-fluorophenyl)-5-[[4-(methoxymethyl)benzyl]carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.00000011
(3R,5R)-7-[5-(4-carboxy-benzylcarbamoyl)-ethyl-3-(4-fluorophenyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid disodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.00000015
(3R,5R)-7-[5-benzylcarbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid
Rattus norvegicus
-
37°C, hepatocytes
0.000032
(3R,5R)-7-[5-carbamoyl-1-ethyl-3-(4-fluorophenyl)-4-methyl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoic acid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.0000049
(3R,5R)-7-[5-carbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoicacid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.0000021
(3R,5R)-7-[5-cyano-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.0000012
(3R,5R)-7-[5-[(3-carbamoylbenzyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000002
(3R,5R)-7-[5-[(4-cyanobenzyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000012
(3R,5R)-7-[5-[[4-(dimethylcarbamoyl)benzyl]carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
2.2 - 26
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoic acid
0.0000022
4-[[([5-[(3R,5R)-6-carboxy-3,5-dihydroxyhexyl]-4-(4-fluorophenyl)-1-(1-methylethyl)-3-phenyl-1H-pyrrol-2-yl]carbonyl)amino]methyl]benzoic acid
Mus musculus
-
inhibition of purified enzyme
0.0000018
7-[3,4-bis(4-fluorophenyl)-1-(1-methylethyl)-5-(phenylcarbamoyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000007
7-[3,4-bis(4-fluorophenyl)-5-[(3-hydroxyphenyl)carbamoyl]-1-(1-methylethyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000066
7-[3,4-bis(4-fluorophenyl)-5-[(3-methoxyphenyl)carbamoyl]-1-(1-methylethyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000124
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-(phenylcarbamoyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.000015
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-(propylcarbamoyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000029
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-[(4-sulfamoylphenyl)carbamoyl]-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000008
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-5-[(pyridin-2-ylmethyl)carbamoyl]-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000015
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-5-[[(4-methyl-1,3-thiazol-2-yl)methyl]carbamoyl]-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000034
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-5-[[(5-methyl-1H-imidazol-2-yl)methyl]carbamoyl]-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000026
7-[3-(4-fluorophenyl)-1-(1-methylethyl)-5-[[(5-methyl-1H-pyrazol-3-yl)methyl]carbamoyl]-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000088
7-[3-(4-fluorophenyl)-5-(methylcarbamoyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000004
7-[3-(4-fluorophenyl)-5-[(4-hydroxyphenyl)carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000008
7-[3-(4-fluorophenyl)-5-[(4-methoxybenzyl)carbamoyl]-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000008
7-[5-(benzylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000038
7-[5-(cyclopropylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.00002
7-[5-(dimethylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.000012
7-[5-(ethylcarbamoyl)-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.000003
7-[5-carbamoyl-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000051
7-[5-ethylcarbamoyl-3-(4-fluoro-phenyl)-1-isopropyl-4-pyridin-2-yl-1H-pyrrol-2-yl]-3,5-dihydroxy-heptanoicacid sodium salt
Rattus norvegicus
-
37°C, hepatocytes
0.0000003
7-[5-[(4-carbamoylphenyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000003
7-[5-[(4-carboxyphenyl)carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000006
7-[5-[[(1,5-dimethyl-1H-pyrazol-3-yl)methyl]carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000003
7-[5-[[3-(dimethylcarbamoyl)phenyl]carbamoyl]-3,4-bis(4-fluorophenyl)-1-(1-methylethyl)-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
0.0000014
7-[5-[[4-(dimethylcarbamoyl)phenyl]carbamoyl]-3-(4-fluorophenyl)-1-(1-methylethyl)-4-phenyl-1H-pyrrol-2-yl]-3,5-dihydroxyheptanoate
Mus musculus
-
inhibition of purified enzyme
1.2
8-hydroxygeraniol
Phaedon cochleariae
-
pH 6.8, 30°C, recombinant catalytic domain
0.00049
AFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.0194
atorvastatin
Leishmania donovani
pH 7.2, 37°C
0.0000017
cerivastatin
Rattus norvegicus
-
37°C, hepatocytes
0.00016
DFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.00024
EFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.0038
F(4-fluoro)VAE
Rattus norvegicus
-
-
0.00032
FFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.0025
FFYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.0085
FG-(4-fluoro)FVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.0004
FGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.00022 - 0.003
fluvastatin
0.0014
FPYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.0438
FVAE
Rattus norvegicus
-
-
0.00027
GFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.0015
GFPDGG
Rattus norvegicus
-
-
0.0017
GFPEGG
Rattus norvegicus
-
-
0.0169
GFPTGG
Rattus norvegicus
-
-
0.0223
GLPDGG
Rattus norvegicus
-
-
0.0272
GLPEGG
Rattus norvegicus
-
-
0.0194
GLPTGG
Rattus norvegicus
-
-
0.0752
IAVE
Rattus norvegicus
-
-
0.097
IAVP
Rattus norvegicus
-
-
0.152
IAVPGEVA
Rattus norvegicus
-
-
0.152
IAVPTGVA
Homo sapiens
-
pH and temperature not specified in the publication
0.00035
IFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.075
Ile-Ala-Val-Glu
Homo sapiens
-
pH and temperature not specified in the publication
0.201
Ile-Ala-Val-Pro-Gly-Glu-Val-Ala
Homo sapiens
-
pH and temperature not specified in the publication
0.052
Ile-Val-Ala-Glu
Homo sapiens
-
pH and temperature not specified in the publication
0.0441
IVAE
Rattus norvegicus
-
-
0.484
Leu-Pro-Tyr-Pro
Homo sapiens
-
pH and temperature not specified in the publication
0.00037
LFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.484
LPYP
Rattus norvegicus
-
-
0.04265
methyl (2-methoxy-5-nitro-4-propylphenoxy)acetate
[Candida] glabrata
-
at pH 8.0 and 37°C
0.02877
methyl (4-ethyl-2-nitrophenoxy)acetate
[Candida] glabrata
-
at pH 8.0 and 37°C
0.04
mevastatin
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
0.00043
PFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.00000023 - 0.0000031
rosuvastatin
0.000033
SFGYVAE peptide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000013 - 0.0732
simvastatin
0.82
sodium (E,3R,5S)-7-(2-(2-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
1.2
sodium (E,3R,5S)-7-(2-(3-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
0.15
sodium (E,3R,5S)-7-(2-(4-fluorophenyl)-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxy-hept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
0.85
sodium (E,3R,5S)-7-(2-phenyl-4-(3-phenylpentan-3-yl)phenyl)-3,5-dihydroxyhept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
7.4
sodium (E,3R,5S)-7-(4-(3-(2-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
92
sodium (E,3R,5S)-7-(4-(3-(3-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (3.7 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
1.8
sodium (E,3R,5S)-7-(4-(3-phenylpentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoate
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
0.00026
TFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.044
Tyr-Ala-Val-Glu
Homo sapiens
-
pH and temperature not specified in the publication
0.041
Tyr-Val-Ala-Glu
Homo sapiens
-
pH and temperature not specified in the publication
0.00045
VFGYVAE
Homo sapiens
-
pH and temperature not specified in the publication
0.0526
YAVE
Rattus norvegicus
-
-
0.0418
YVAE
Rattus norvegicus
-
-
2.2
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoic acid
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
26
(E,3R,5S)-7-(4-(3-(4-fluorophenyl)pentan-3-yl)-2-isopropylphenyl)-3,5-dihydroxyhept-6-enoic acid
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (3.7 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
0.00022
fluvastatin
Phaedon cochleariae
-
pH 6.8, 30°C
0.003
fluvastatin
Rattus norvegicus
-
DL-[3-14C]3-hydroxy-3-methylglutaryl-CoA (0.37 MBq) and 10 mg protein of microsomal fraction incubated at 37°C for 30 min
0.00000023
rosuvastatin
Rattus norvegicus
-
37°C, hepatocytes
0.0000031
rosuvastatin
Mus musculus
-
inhibition of purified enzyme
0.0000013
simvastatin
Rattus norvegicus
-
37°C, hepatocytes
0.000049
simvastatin
Mus musculus
-
inhibition of purified enzyme
0.0732
simvastatin
Leishmania donovani
pH 7.2, 37°C
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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
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
malfunction
-
inhibition of enzyme expression promotes the accumulation of anthocyanins and fruit coloration
malfunction
the enzyme is important in the biosynthesis of terpenoids such as patchouli alcohol
metabolism
-
part of cholesterol synthesis pathway
metabolism
HMG-CoA reductase is the rate-limiting enzyme of cholesterol biosynthesis
metabolism
-
HMGR catalyzes the first committed step in mevalonic acid pathway for biosynthesis of isoprenoids
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
-
3-hydroxy-3-methylglutaryl Co-A reductase is a rate-limiting enzyme in the eukaryotic mevalonate pathway
metabolism
-
3-hydroxy-3-methylglutaryl CoA reductase catalyzes the first committed step in the mevalonic acid (MVA) pathway for the biosynthesis of isoprenoids
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
-
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
the enzyme is implicated in latex metabolism
metabolism
-
the enzyme is involved in mevalonate biosynthesis
metabolism
enzyme overexpression significantly increases abscisic acid, gibberellic acid, carotene, and lycopene content, indicating that the enzyme participates in the regulation of terpenoid compound synthesis
metabolism
rate-limiting enzyme in mammalian phosphatidylethanolamine biosynthesis
metabolism
rate-limiting enzyme in mammalian phosphatidylethanolamine biosynthesis
metabolism
-
3-hydroxy-3-methylglutaryl Co-A reductase is a rate-limiting enzyme in the eukaryotic mevalonate pathway
-
metabolism
-
rate limiting enzyme of the ergosterol biosynthetic pathway
-
physiological function
within cells, the concentration of mevalonate and therefore that of its metabolic products is tightly controlled through the activity of HMGR, an enzyme that catalyzes the four-electron reduction of 3-hydroxy-3-methylglutaryl-CoA to mevalonate
physiological function
-
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
rate-limiting enzyme for cholesterol synthesis, regulated via a negative feedback mechanism through sterols and non-sterol metabolites derived from 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
-
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
-
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. Protein phosphatase 2A (PP2A) is both a transcriptional and a posttranslational regulator of HMGR in Arabidopsis thaliana
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
physiological function
-
brassinosteroids inhibit enzyme activity and cooperate with the enzyme to regulate the formation of color, aroma, and other quality characteristics in fruits
physiological function
-
overexpression of isoform HMGR5 enhances tolerance to oxidative stress by maintaining photosynthesis and scavenging reactive oxygen species in transgenic Arabidopsis thaliana
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
-
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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lipoprotein
identification of nineteen N-myristoylation sites and three characteristic sites
proteolytic modification
-
proteolysis releases a soluble, active fragment of 52-56 kDa
glycoprotein
-
-
glycoprotein
-
the enzyme sequence contains a glycosylation site
glycoprotein
identification of five N-glycosylation sites
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
isoform HMGR1S is inactivated through phosphorylation at Ser577 by the AKIN10-GRIK1 kinase cascade system in vitro
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
activity is regulated by phosphorylation and dephosphorylation
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
activity is regulated by phosphorylation and dephosphorylation
phosphoprotein
the enzyme is phosphorylated at Ser872 by AMP-activated protein kinase and reversibly dephosphorylated by phosphatase 2A
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
regulation of the plant enzyme by phosphorylation/dephosphorylation
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
Ochromonas malhamensis
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
the enzyme sequence contains a phosphorylation site
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
activity is regulated by phosphorylation and dephosphorylation
phosphoprotein
-
activity is regulated by phosphorylation and dephosphorylation
-
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
regulation of the plant enzyme by phosphorylation/dephosphorylation
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
regulation of the plant enzyme by phosphorylation/dephosphorylation
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
identification of a cAMP-and cGMP-dependent protein kinase phosphorylation site, thirteen Protein kinase C phosphorylation sites, and eleven Casein kinase II phosphorylation sites
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
phosphoprotein
-
phosphorylation at a conserved site of the catalytic domain of enzyme HMGR
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
the isozyme is not regulated by phosphorylation
additional information
the isozyme is not regulated by phosphorylation
additional information
-
the isozyme is not regulated by phosphorylation
additional information
the isozyme is probably not regulated by phosphorylation
additional information
the isozyme is probably not regulated by phosphorylation
additional information
-
the isozyme is probably not regulated by phosphorylation
additional information
-
genistein, eicosapentaenoic acid and docosahexaenoic acid down-regulate reductase activity, primarily through posttranscriptional effects
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
ubiquitination and proteasomal degradation of microsomal, but not mitochondrial, HMGR isozymes depends on environmental salinity, overview
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
Ochromonas malhamensis
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
additional information
-
protein degradation, inhibition, or activation by calcium, and phosphorylation at a conserved site of the catalytic domain are mechanisms by which plant enzyme HMGR is posttranslationally modulated
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