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Literature summary extracted from

  • Kim, D.Y.; Stauffacher, C.V.; Rodwell, V.W.
    Dual coenzyme specificity of Archaeoglobus fulgidus HMG-CoA reductase (2000), Protein Sci., 9, 1226-1234.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.B38 expression in Escherichia coli Archaeoglobus fulgidus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.B38 Mevinolin competitive Archaeoglobus fulgidus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.B38 0.16
-
NADH pH 9.0, 50°C Archaeoglobus fulgidus
1.1.1.B38 0.5
-
NADPH pH 6.0, 50°C Archaeoglobus fulgidus
1.1.1.B38 0.5
-
NAD+ pH 10.0, 50°C Archaeoglobus fulgidus
1.1.1.B38 0.62
-
mevalonate 50°C, pH not specified in the publication Archaeoglobus fulgidus
1.1.1.B38 1.7
-
NADP+ pH 7.0, 50°C Archaeoglobus fulgidus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.B38 Archaeoglobus fulgidus O28538
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.B38
-
Archaeoglobus fulgidus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.B38 mevalonate + CoA + 2 NAD+ optimal activity using NADP(H) occurs at pH from 1 to 3 units more acidic than that observed using NAD(H) Archaeoglobus fulgidus 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
-
r
1.1.1.B38 mevalonate + CoA + 2 NADP+ 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) Archaeoglobus fulgidus 3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+
-
r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.B38 AF1736
-
Archaeoglobus fulgidus
1.1.1.B38 HMG-CoA reductase
-
Archaeoglobus fulgidus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.B38 85
-
-
Archaeoglobus fulgidus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.B38 65 95 65°C: about 45% of maximal activity, 95°C: about 65% of maximal activity Archaeoglobus fulgidus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.B38 0.08
-
NADH pH 9.0, 50°C Archaeoglobus fulgidus
1.1.1.B38 0.1
-
NAD+ pH 10.0, 50°C Archaeoglobus fulgidus
1.1.1.B38 2
-
NADPH pH 6.0, 50°C Archaeoglobus fulgidus
1.1.1.B38 6.8
-
NADP+ pH 7.0, 50°C Archaeoglobus fulgidus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.B38 6
-
reductive deacylation of 3-hydroxy-3-methylglutaryl-CoA to mevalonate with NADPH Archaeoglobus fulgidus
1.1.1.B38 6.8
-
oxidative acylation of mevalonate to 3-hydroxy-3-methylglutaryl-CoA with NADP+ Archaeoglobus fulgidus
1.1.1.B38 9
-
reductive deacylation of 3-hydroxy-3-methylglutaryl-CoA to mevalonate with NADH Archaeoglobus fulgidus
1.1.1.B38 9.5 10 oxidative acylation of mevalonate to 3-hydroxy-3-methylglutaryl-CoA with NAD+ Archaeoglobus fulgidus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.B38 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 Archaeoglobus fulgidus
1.1.1.B38 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 Archaeoglobus fulgidus
1.1.1.B38 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 Archaeoglobus fulgidus
1.1.1.B38 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 Archaeoglobus fulgidus

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.1.1.B38 0.18
-
50°C, pH not specified in the publication Archaeoglobus fulgidus Mevinolin

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.B38 0.25
-
NADP+ pH 7.0, 50°C Archaeoglobus fulgidus
1.1.1.B38 1
-
NADPH pH 6.0, 50°C Archaeoglobus fulgidus
1.1.1.B38 2
-
NADH pH 9.0, 50°C Archaeoglobus fulgidus
1.1.1.B38 5
-
NAD+ pH 10.0, 50°C Archaeoglobus fulgidus