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Literature summary for 1.14.14.1 extracted from

  • Lamb, D.C.; Lei, L.; Zhao, B.; Yuan, H.; Jackson, C.J.; Warrilow, A.G.; Skaug, T.; Dyson, P.J.; Dawson, E.S.; Kelly, S.L.; Hachey, D.L.; Waterman, M.R.
    Streptomyces coelicolor A3(2) CYP102 protein, a novel fatty acid hydroxylase encoded as a heme domain without an N-terminal redox partner (2010), Appl. Environ. Microbiol., 76, 1975-1980.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Streptomyces coelicolor

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor
-
-
-
Streptomyces coelicolor A3(2)
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography, gel filtration Streptomyces coelicolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
-
Streptomyces coelicolor 18-hydroxyarachidonic acid + 14,15-epoxyeicosa-5,8,11-trienoic acid + 11,12-epoxyeicosa-5,8,14-trienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O reaction products generated by isoform CYP102B1 ?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
-
Streptomyces coelicolor A3(2) 18-hydroxyarachidonic acid + 14,15-epoxyeicosa-5,8,11-trienoic acid + 11,12-epoxyeicosa-5,8,14-trienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O reaction products generated by isoform CYP102B1 ?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
-
Streptomyces coelicolor 18-hydroxyarachidonic acid + 14,15-epoxyeicosa-5,8,11-trienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O reaction products generated by isoform CYP102A1 ?
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
-
Streptomyces coelicolor A3(2) 18-hydroxyarachidonic acid + 14,15-epoxyeicosa-5,8,11-trienoic acid + [oxidized NADPH-hemoprotein reductase] + H2O reaction products generated by isoform CYP102A1 ?
additional information palmitate, stearate, and oleate show negligible binding to isoform CYP102B1, in contrast to CYP102A1 Streptomyces coelicolor ?
-
?
additional information palmitate, stearate, and oleate show negligible binding to isoform CYP102B1, in contrast to CYP102A1 Streptomyces coelicolor A3(2) ?
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
-
Streptomyces coelicolor ?
-
?
oleic acid + [reduced NADPH-hemoprotein reductase] + O2
-
Streptomyces coelicolor A3(2) ?
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
-
Streptomyces coelicolor ?
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
-
Streptomyces coelicolor A3(2) ?
-
?
stearic acid + [reduced NADPH-hemoprotein reductase] + O2
-
Streptomyces coelicolor ?
-
?

Synonyms

Synonyms Comment Organism
CYP102
-
Streptomyces coelicolor
CYP102A1 isoform, binds arachidonate more tightly than isoform CYP102B1 Streptomyces coelicolor
CYP102B1 isoform Streptomyces coelicolor
fatty acid hydroxylase
-
Streptomyces coelicolor

Cofactor

Cofactor Comment Organism Structure
heme
-
Streptomyces coelicolor
NADPH
-
Streptomyces coelicolor

General Information

General Information Comment Organism
physiological function isoform CYP102B1 is not required for normal cell growth and secondary metabolite productio Streptomyces coelicolor