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Literature summary extracted from

  • Lawrence, C.M.; Rodwell, V.W.; Stauffacher, C.V.
    Crystal structure of Pseudomonas mevalonii HMG-CoA reductase at 3.0 Angstrom resolution (1995), Science, 268, 1758-1762.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.88 3 A resolution, 3 dimers packed along three-fold crystallographic axis, hexamer Pseudomonas mevalonii

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.88 Pseudomonas mevalonii
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.88 (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+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.88 hexamer 3alpha2, XSA Pseudomonas mevalonii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.88 6
-
 oxidative acylation of mevalonate with NADP+ as cofactor Pseudomonas mevalonii
1.1.1.88 9
-
 oxidative acylation of mevalonate Pseudomonas mevalonii

Cofactor

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