Information on EC 1.1.1.B38 - hydroxymethylglutaryl-CoA reductase [NAD(P)H]

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The expected taxonomic range for this enzyme is: Archaeoglobus fulgidus

EC NUMBER
COMMENTARY hide
1.1.1.B38
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
hydroxymethylglutaryl-CoA reductase [NAD(P)H]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
mevalonate + CoA + 2 NAD(P)+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NAD(P)H + 2 H+
show the reaction diagram
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-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mevalonate metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
mevalonate:NAD(P)+ oxidoreductase (CoA-acylating)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
mevalonate + CoA + 2 NAD+
3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
show the reaction diagram
optimal activity using NADP(H) occurs at pH from 1 to 3 units more acidic than that observed using NAD(H)
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-
r
mevalonate + CoA + 2 NADP+
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
show the reaction diagram
slight preference for NAD(H) versus NADP(H). Optimal activity using NADP(H) occurs at a pH from 1 to 3 units more acidic than that observed using NAD(H)
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-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
slight preference for NAD(H) versus NADP(H). Optimal activity using NADP(H) occurrs at a pH from 1 to 3 units more acidic than that observed using NAD(H). Each coenzyme acts as a competitive inhibitor of the other
NADH
slight preference for NAD(H) versus NADP(H). Optimal activity using NADP(H) occurrs at a pH from 1 to 3 units more acidic than that observed using NAD(H). Each coenzyme acts as a competitive inhibitor of the other
NADP+
slight preference for NAD(H) versus NADP(H). Optimal activity using NADP(H) occurrs at a pH from 1 to 3 units more acidic than that observed using NAD(H). Each coenzyme acts as a competitive inhibitor of the other
NADPH
slight preference for NAD(H) versus NADP(H). Optimal activity using NADP(H) occurrs at a pH from 1 to 3 units more acidic than that observed using NAD(H). Each coenzyme acts as a competitive inhibitor of the other
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mevinolin
competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.62
mevalonate
50°C, pH not specified in the publication
0.5
NAD+
pH 10.0, 50°C
0.16
NADH
pH 9.0, 50°C
1.7
NADP+
pH 7.0, 50°C
0.5
NADPH
pH 6.0, 50°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
NAD+
Archaeoglobus fulgidus
O28538
pH 10.0, 50°C
0.08
NADH
Archaeoglobus fulgidus
O28538
pH 9.0, 50°C
6.8
NADP+
Archaeoglobus fulgidus
O28538
pH 7.0, 50°C
2
NADPH
Archaeoglobus fulgidus
O28538
pH 6.0, 50°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
NAD+
Archaeoglobus fulgidus
O28538
pH 10.0, 50°C
7
2
NADH
Archaeoglobus fulgidus
O28538
pH 9.0, 50°C
8
0.25
NADP+
Archaeoglobus fulgidus
O28538
pH 7.0, 50°C
10
1
NADPH
Archaeoglobus fulgidus
O28538
pH 6.0, 50°C
5
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
Mevinolin
Archaeoglobus fulgidus
O28538
50°C, pH not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
reductive deacylation of 3-hydroxy-3-methylglutaryl-CoA to mevalonate with NADPH
6.8
oxidative acylation of mevalonate to 3-hydroxy-3-methylglutaryl-CoA with NADP+
9
reductive deacylation of 3-hydroxy-3-methylglutaryl-CoA to mevalonate with NADH
9.5 - 10
oxidative acylation of mevalonate to 3-hydroxy-3-methylglutaryl-CoA with NAD+
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65 - 95
65°C: about 45% of maximal activity, 95°C: about 65% of maximal activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli