Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Salazar, O.; Cirino, P.C.; Arnold, F.H.
    Thermostabilization of a cytochrome P450 peroxygenase (2003), ChemBioChem, 4, 891-893.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.2.4 expressed in Escherichia coli Priestia megaterium

Protein Variants

EC Number Protein Variants Comment Organism
1.11.2.4 F878A P450 BM-3 heme domain containing the single amino acid substitution F87A is significantly more active than wild type heme domain in reactions driven by H2O2 Priestia megaterium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.11.2.4 additional information Priestia megaterium P450 BM-3 peroxygenase 21B3 is a laboratory-evolved variant of the P450 BM-3 heme domain which functions as an H2O2-driven hydroxylase (peroxygenase) and does not require NADPH, O2 , or the reductase ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.11.2.4 Priestia megaterium
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.2.4
-
Priestia megaterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.2.4 12-4-nitrophenoxycarboxylic acid + H2O2
-
Priestia megaterium 4-nitrophenolate + ?
-
?
1.11.2.4 additional information P450 BM-3 peroxygenase 21B3 is a laboratory-evolved variant of the P450 BM-3 heme domain which functions as an H2O2-driven hydroxylase (peroxygenase) and does not require NADPH, O2 , or the reductase Priestia megaterium ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.11.2.4 P450 BM-3 peroxygenase 21B3
-
Priestia megaterium