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Literature summary for 1.11.2.4 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)

Cloned (Comment) Organism
expressed in Escherichia coli Priestia megaterium

Protein Variants

Protein Variants Comment Organism
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Priestia megaterium
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Priestia megaterium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
12-4-nitrophenoxycarboxylic acid + H2O2
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Priestia megaterium 4-nitrophenolate + ?
-
?
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

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