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Literature summary extracted from

  • Cryle, M.J.; Bell, S.G.; Schlichting, I.
    Structural and biochemical characterization of the cytochrome P450 CypX (CYP134A1) from Bacillus subtilis: a cyclo-L-leucyl-L-leucyl dipeptide oxidase (2010), Biochemistry, 49, 7282-7296.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.15.13 expressed in Escherichia coli BL21(DE3) cells Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.15.13 mutant enzyme A356T, hanging drop vapor diffusion method, using 0.1 M Bis-Tris (pH 6.5), 0.1 M MgCl2, 12% (w/v) polyethylene glycol 3350 Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.13 A356T mutant enzyme A356T crystallizes under several PEG-3350 conditions, with an optimum pH around 6 and a relatively low PEG concentration (12-15% (w/v)). The wild-type protein does not crystallize under these conditions, while the protein of the A356T mutant crystallizes readily and forms large, thin plates Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.15.13 cyclo(L-leucyl-L-leucyl) + reduced ferredoxin + O2 Bacillus subtilis
-
 pulcherriminic acid + oxidized ferredoxin + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.13 Bacillus subtilis O34926
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.15.13 Ni-NTA column chromatography, Resource Q column chromatography, and Superose-12 gel filtration Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.13 1-phenylimidazole + reduced ferredoxin + O2
-
 Bacillus subtilis ? + oxidized ferredoxin + H2O
-
 ?
1.14.15.13 2,5-di-tert-butylhydroquinone + reduced ferredoxin + O2
-
 Bacillus subtilis ? + oxidized ferredoxin + H2O
-
 ?
1.14.15.13 2,5-di-tert-butylquinone + reduced ferredoxin + O2
-
 Bacillus subtilis ? + oxidized ferredoxin + H2O
-
 ?
1.14.15.13 2-phenylimidazole + reduced ferredoxin + O2
-
 Bacillus subtilis ? + oxidized ferredoxin + H2O
-
 ?
1.14.15.13 4-phenylimidazole + reduced ferredoxin + O2
-
 Bacillus subtilis ? + oxidized ferredoxin + H2O
-
 ?
1.14.15.13 cyclo(L-alanyl-L-alanyl) + reduced ferredoxin + O2
-
 Bacillus subtilis ? + oxidized ferredoxin + H2O
-
 ?
1.14.15.13 cyclo(L-leucyl-L-leucyl) + reduced ferredoxin + O2
-
 Bacillus subtilis pulcherriminic acid + oxidized ferredoxin + H2O
-
 ?
1.14.15.13 cyclo(L-leucyl-L-phenylalanyl) + reduced ferredoxin + O2
-
 Bacillus subtilis ? + oxidized ferredoxin + H2O
-
 ?
1.14.15.13 cyclo(L-leucyl-L-prolyl) + reduced ferredoxin + O2
-
 Bacillus subtilis ? + oxidized ferredoxin + H2O
-
 ?
1.14.15.13 cyclo(L-leucyl-L-tryptophanyl) + reduced ferredoxin + O2
-
 Bacillus subtilis ? + oxidized ferredoxin + H2O
-
 ?
1.14.15.13 cyclo(L-methionyl-L-methionyl) + reduced ferredoxin + O2
-
 Bacillus subtilis ? + oxidized ferredoxin + H2O
-
 ?
1.14.15.13 cyclo(L-valyl-L-valyl) + reduced ferredoxin + O2
-
 Bacillus subtilis ? + oxidized ferredoxin + H2O
-
 ?
1.14.15.13 additional information the enzyme does not use dimethylpyrazine and tetramethylpyrazine as substrates Bacillus subtilis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.15.13 cyclo-L-leucyl-L-leucyl dipeptide oxidase
-
 Bacillus subtilis
1.14.15.13 CYP134A1
-
 Bacillus subtilis
1.14.15.13 CypX
-
 Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.13 heme
-
 Bacillus subtilis