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1.1.1.B38
sirtuins
deacetylases
deacetylation
histone
nad+-dependent
tubulin
agk2
sirt1-7
sirt2-specific
sirts
sirtinol
sirt2-mediated
dinucleotide-dependent
Synonyms
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3-hydroxy-3-methylglutaryl coenzyme A reductase
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class II HMG-CoA reductase
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mevalonate + CoA + 2 NAD(P)+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NAD(P)H + 2 H+
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mevalonate:NAD(P)+ oxidoreductase (CoA-acylating)
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3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
mevalonate + CoA + 2 NAD+
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Substrates: -
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3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
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Substrates: -
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mevalonate + CoA + 2 NAD+
3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
Substrates: optimal activity using NADP(H) occurs at pH from 1 to 3 units more acidic than that observed using NAD(H)
r
mevalonate + CoA + 2 NADP+
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
Substrates: 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)
r
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3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
mevalonate + CoA + 2 NAD+
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Substrates: -
?
3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
mevalonate + CoA + 2 NADP+
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Substrates: -
?
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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
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
NADH
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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
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
NADPH
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kinetically preferred cofactor
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0.62
mevalonate
50°C, pH not specified in the publication
0.153
NADH
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at pH 7.4 and 37°C
0.0289
NADPH
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at pH 7.4 and 37°C
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0.08
NADH
pH 9.0, 50°C
0.131
NADH
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at pH 7.4 and 37°C
2
NADPH
pH 6.0, 50°C
6.85
NADPH
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at pH 7.4 and 37°C
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0.86
NADH
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at pH 7.4 and 37°C
1
NADPH
pH 6.0, 50°C
240
NADPH
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at pH 7.4 and 37°C
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0.18
Mevinolin
Archaeoglobus fulgidus
50°C, pH not specified in the publication
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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+
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65 - 95
65°C: about 45% of maximal activity, 95°C: about 65% of maximal activity
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SwissProt
brenda
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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metabolism
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key enzyme in the mevalonate pathway
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HMDH_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
436
0
47146
Swiss-Prot
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homodimer
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x-ray crystallography
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enzyme bound to 3-hydroxy-3-methylglutaryl-CoA, hanging drop vapor diffusion method, using 100 mM Tris pH 8.5, 100-250 mM lithium sulfate, and 15-25% (w/v) PEG 4000. Enzyme bound to NADPH, hanging drop vapor diffusion method, using 100 mM Tris pH 8.5, 100-250 mM lithium sulfate, and 30-40% (w/v) PEG 4000
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Ni-NTA column chromatography and Superdex 200 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
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Kim, D.Y.; Stauffacher, C.V.; Rodwell, V.W.
Dual coenzyme specificity of Archaeoglobus fulgidus HMG-CoA reductase
Protein Sci.
9
1226-1234
2000
Archaeoglobus fulgidus (O28538), Archaeoglobus fulgidus
brenda
Miller, B.R.; Kung, Y.
Structural features and domain movements controlling substrate binding and cofactor specificity in class II HMG-CoA reductase
Biochemistry
57
654-662
2018
Streptococcus pneumoniae
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