Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Fimognari, G.M.; Rodwell, V.W.
    Substrate-competitive inhibition of bacterial mevalonate:nicotinamide-adenine dinucleotide oxidoreductase (acylating CoA) (1965), Biochemistry, 4, 2086-2090.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.88 3-Hydroxy-3-methylbutyrate
-
Mycobacterium sp.
1.1.1.88 3-Hydroxy-3-methylbutyrate
-
Pseudomonas mevalonii
1.1.1.88 3-hydroxy-3-methylcarboxylic acid competitive inhibitor Mycobacterium sp.
1.1.1.88 3-hydroxy-3-methylcarboxylic acid competitive inhibitor Pseudomonas mevalonii
1.1.1.88 3-hydroxy-3-methylglutarate
-
Mycobacterium sp.
1.1.1.88 3-hydroxy-3-methylglutarate
-
Pseudomonas mevalonii
1.1.1.88 3-hydroxybutyrate
-
Mycobacterium sp.
1.1.1.88 3-hydroxybutyrate
-
Pseudomonas mevalonii
1.1.1.88 deoxycholate competitive inhibitor Mycobacterium sp.
1.1.1.88 deoxycholate competitive inhibitor Pseudomonas mevalonii
1.1.1.88 additional information no inhibition citrate, succinate, glutarate, 3,3-dimethylacrylate, 2,2-dimethylpropionate, acetoacetate Mycobacterium sp.
1.1.1.88 additional information no inhibition citrate, succinate, glutarate, 3,3-dimethylacrylate, 2,2-dimethylpropionate, acetoacetate Pseudomonas mevalonii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.88 0.1
-
CoA oxidative acylation of mevalonate Mycobacterium sp.
1.1.1.88 0.1
-
CoA oxidative acylation of mevalonate Pseudomonas mevalonii
1.1.1.88 0.35
-
NAD+ oxidative acylation of mevalonate Pseudomonas mevalonii
1.1.1.88 0.35
-
DL-mevalonate oxidative acylation of mevalonate Pseudomonas mevalonii
1.1.1.88 0.49
-
DL-mevalonate oxidative acylation of mevalonate Mycobacterium sp.
1.1.1.88 0.6
-
NAD+ oxidative acylation of mevalonate Mycobacterium sp.

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.88 cytosol
-
Mycobacterium sp. 5829
-
1.1.1.88 cytosol
-
Pseudomonas mevalonii 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.88 Mg2+
-
Mycobacterium sp.

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.88 Mycobacterium sp.
-
S4
-
1.1.1.88 Mycobacterium sp. s4
-
S4
-
1.1.1.88 Pseudomonas mevalonii
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.88 0.163
-
mevalonate acylation Pseudomonas mevalonii
1.1.1.88 0.17
-
mevalonate acylation Mycobacterium sp.

Storage Stability

EC Number Storage Stability Organism
1.1.1.88 -20°C stable to repeated freezing and thawing Pseudomonas mevalonii
1.1.1.88 -20°C unstable to repeated freezing and thawing Mycobacterium sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.88 (R)-mevalonate + CoA + 2 NAD+
-
Mycobacterium sp. (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
-
?
1.1.1.88 (R)-mevalonate + CoA + 2 NAD+
-
Pseudomonas mevalonii (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
-
?
1.1.1.88 (R)-mevalonate + CoA + 2 NAD+
-
Mycobacterium sp. s4 (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
-
?
1.1.1.88 3-hydroxy-3-methylglutaryl-CoA + NADH + H+
-
Pseudomonas mevalonii mevalonate + CoA + NAD+
-
?
1.1.1.88 DL-mevalonate + CoA + NADP+
-
Mycobacterium sp. 3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
-
r
1.1.1.88 DL-mevalonate + CoA + NADP+
-
Mycobacterium sp. s4 3-hydroxy-3-methylglutaryl-CoA + NADPH + H+
-
r
1.1.1.88 additional information oxidative acylation of mevalonate: the carboxy-, 3-methyl-, and 3-hydroxy groups are essential for substrate binding to the enzyme Mycobacterium sp. ?
-
?
1.1.1.88 additional information oxidative acylation of mevalonate: the carboxy-, 3-methyl-, and 3-hydroxy groups are essential for substrate binding to the enzyme Pseudomonas mevalonii ?
-
?
1.1.1.88 additional information oxidative acylation of mevalonate: the carboxy-, 3-methyl-, and 3-hydroxy groups are essential for substrate binding to the enzyme Mycobacterium sp. s4 ?
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.88 7.1
-
assay conditions Mycobacterium sp.
1.1.1.88 7.1
-
assay conditions Pseudomonas mevalonii

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.88 NAD+
-
Mycobacterium sp.
1.1.1.88 NAD+
-
Pseudomonas mevalonii
1.1.1.88 NADH reverse reaction Pseudomonas mevalonii