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Literature summary for 1.14.15.1 extracted from

  • Sono, M.; Perera, R.; Jin, S.; Makris, T.M.; Sligar, S.G.; Bryson, T.A.; Dawson, J.H.
    The influence of substrate on the spectral properties of oxyferrous wild-type and T252A cytochrome P450-CAM (2005), Arch. Biochem. Biophys., 436, 40-49.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
T252A about 5% of wild-type activity, similar spectra for oxyferrous mutant and wild-type except for Soret band position blue shifts. Epoxidation substrate 5-methylenylcamphor has a anomalous binding mode for the mutant Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida P00183
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(1R)-5,5-difluorocamphor + putidaredoxin + O2
-
Pseudomonas putida ? + oxidized putidaredoxin + H2O
-
?
(1R)-5-exo-methoxycamphor + putidaredoxin + O2
-
Pseudomonas putida ? + oxidized putidaredoxin + H2O
-
?
(1R)-5-methylenylcamphor + putidaredoxin + O2
-
Pseudomonas putida ? + oxidized putidaredoxin + H2O
-
?
(1R)-camphor + putidaredoxin + O2
-
Pseudomonas putida ? + oxidized putidaredoxin + H2O
-
?
(1R)-norcamphor + putidaredoxin + O2
-
Pseudomonas putida ? + oxidized putidaredoxin + H2O
-
?
(1S)-camphor + putidaredoxin + O2
-
Pseudomonas putida ? + oxidized putidaredoxin + H2O
-
?
adamantanone + putidaredoxin + O2
-
Pseudomonas putida ? + oxidized putidaredoxin + H2O
-
?