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Literature summary for 1.14.14.1 extracted from

  • Oliver, C.F.; Modi, S.; Primrose, W.U.; Lian, L.Y.; Roberts, G.C.K.
    Engineering the substrate specificity of Bacillus megaterium cytochrome P-450 BM3: hydroxylation of alkyl trimethylammonium compounds (1997), Biochem. J., 327, 537-544.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Priestia megaterium

Protein Variants

Protein Variants Comment Organism
R47E the mutant enzyme retains significant hydroxylase activity towards saturated fatty acids and shows much increased activity towards C12-C16 alkyl trimethylammonium compounds Priestia megaterium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Km-values of wild-type and mutant enzyme for different fatty acids and alkyl trimethylammonium compounds Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme catalyses hydroxylation in the omega-1, omega-2 and omega-3 positions and/or epoxidation of medium- and long-chain fatty acids Priestia megaterium ?
-
?

Synonyms

Synonyms Comment Organism
CYP102
-
Priestia megaterium
cytochrome P-450 BM3 enzyme contains a P-450 heme domain and an NADPH-cytochrome P-450 reductase flavoprotein domain in a single polypeptide chain Priestia megaterium

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information Kcat-values of wild-type and mutant enzyme for different fatty acids and alkyl trimethylammonium compounds Priestia megaterium