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Literature summary for 1.1.1.88 extracted from

  • Rodwell, V.W.; Bensch, W.R.
    S-3-Hydroxy-3-methylglutaryl-CoA reductase from Pseudomonas (1981), Methods Enzymol., 71, 480-486.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
3-hydroxy-3-methylglutarate competitive inhibitor Pseudomonas mevalonii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.032
-
NADH reductive deacylation to mevalonate Pseudomonas mevalonii
0.039
-
CoA oxidative acylation of mevalonate Pseudomonas mevalonii
0.046
-
CoA mevaldate oxidation Pseudomonas mevalonii
0.05
-
DL-3-hydroxy-3-methylglutaryl-CoA reductive deacylation to mevalonate Pseudomonas mevalonii
0.06
-
NAD+ mevaldate oxidation Pseudomonas mevalonii
0.27
-
NAD+ oxidative acylation of mevalonate Pseudomonas mevalonii
0.3
-
mevalonate oxidative acylation of mevalonate Pseudomonas mevalonii
0.36
-
NADH mevaldate reduction to mevalonate Pseudomonas mevalonii
0.61
-
DL-mevaldate mevaldate oxidation Pseudomonas mevalonii
9
-
DL-mevaldate mevaldate reduction to mevalonate Pseudomonas mevalonii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
270000
-
SDS-PAGE Pseudomonas mevalonii

Organism

Organism UniProt Comment Textmining
Pseudomonas mevalonii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas mevalonii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-mevalonate + CoA + 2 NAD+ with mevalonate as sole source of carbon enzyme acts as a biodegradative enzyme Pseudomonas mevalonii (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
-
r
3-hydroxy-3-methylglutaryl-CoA + NADH + H+
-
Pseudomonas mevalonii mevalonate + CoA + NAD+
-
?
DL-mevaldate + CoA + NAD+
-
Pseudomonas mevalonii 4-hydroxy-3-methylglutaryl-CoA NADH + H+
-
r
DL-mevaldate + CoA + NAD+
-
Pseudomonas mevalonii 5-hydroxy-3-methylglutaryl-CoA NADH + H+
-
r
additional information oxidative acylation of mevalonate: the carboxy-, 3-methyl-, and 3-hydroxy groups are essential for substrate binding to the enzyme Pseudomonas mevalonii ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
Pseudomonas mevalonii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1
-
assay conditions Pseudomonas mevalonii
9.2 9.6 oxidative acylation of mevalonate Pseudomonas mevalonii

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Pseudomonas mevalonii
NADH reverse reaction Pseudomonas mevalonii