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Literature summary for 1.14.15.35 extracted from

  • Nagano, S.; Cupp-Vickery, J.R.; Poulos, T.L.
    Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T: investigation of the proton transfer system in P450eryF (2005), J. Biol. Chem., 280, 22102-22107.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion crystallization, crystal structures of the ferrous dioxygen complex of wild-type enzyme and its mutants, A245S and A245T Saccharopolyspora erythraea

Protein Variants

Protein Variants Comment Organism
A245S activity is decreased by 84%, the active site structure including water is essentially unchanged with the exception that the OH group of Ser245 points toward the I-helix cleft to make new H-bonds with water 63 and the carbonyl group of the Ala241 Saccharopolyspora erythraea
A245T more than 99% loss of activity Saccharopolyspora erythraea

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6-deoxyerythronolide B + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Saccharopolyspora erythraea the enzyme is involved in the biosynthesis of the antibiotic erythromycin erythronolide B + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
6-deoxyerythronolide B + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Saccharopolyspora erythraea NRRL 2338 the enzyme is involved in the biosynthesis of the antibiotic erythromycin erythronolide B + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?

Organism

Organism UniProt Comment Textmining
Saccharopolyspora erythraea Q00441
-
-
Saccharopolyspora erythraea NRRL 2338 Q00441
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharopolyspora erythraea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6-deoxyerythronolide B + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 the enzyme is involved in the biosynthesis of the antibiotic erythromycin Saccharopolyspora erythraea erythronolide B + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
6-deoxyerythronolide B + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 direct involvement of the substrate in O2 activation Saccharopolyspora erythraea erythronolide B + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
6-deoxyerythronolide B + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 the enzyme is involved in the biosynthesis of the antibiotic erythromycin Saccharopolyspora erythraea NRRL 2338 erythronolide B + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
6-deoxyerythronolide B + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 direct involvement of the substrate in O2 activation Saccharopolyspora erythraea NRRL 2338 erythronolide B + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?

Synonyms

Synonyms Comment Organism
CYP107A1
-
Saccharopolyspora erythraea
DEB hydroxylase
-
Saccharopolyspora erythraea
eryF
-
Saccharopolyspora erythraea
P450eryF
-
Saccharopolyspora erythraea

Cofactor

Cofactor Comment Organism Structure
heme a heme-thiolate protein (P-450) Saccharopolyspora erythraea

General Information

General Information Comment Organism
physiological function the enzyme is involved in the biosynthesis of the antibiotic erythromycin Saccharopolyspora erythraea