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Literature summary for 1.1.1.88 extracted from

  • Jordan-Starck, T.C.; Rodwell, V.W.
    Role of cysteine residues in Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl-CoA reductase. Site-directed mutagenesis and characterization of the mutant enzymes (1989), J. Biol. Chem., 264, 17919-17923.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Pseudomonas mevalonii

Protein Variants

Protein Variants Comment Organism
C156/296 A fully active, resistant to N-ethylmaleimide Pseudomonas mevalonii
C156A fully active, resistant to N-ethylmaleimide Pseudomonas mevalonii
C296A fully active Pseudomonas mevalonii

Organism

Organism UniProt Comment Textmining
Pseudomonas mevalonii
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
54.2
-
cysteine-free mutant, mevalonate acylation Pseudomonas mevalonii
65.6
-
C156A-mutant, mevalonate acylation Pseudomonas mevalonii
70.5
-
wild-type enzyme, mevalonate acylation Pseudomonas mevalonii
77.7
-
C296A-mutant, mevalonate acylation Pseudomonas mevalonii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-mevalonate + CoA + 2 NAD+
-
Pseudomonas mevalonii (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+
-
?

Cofactor

Cofactor Comment Organism Structure
NAD+ four-electron pyridine oxidoreductase Pseudomonas mevalonii
NADH reverse reaction Pseudomonas mevalonii