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Information on EC 1.14.15.13 - pulcherriminic acid synthase and Organism(s) Bacillus subtilis and UniProt Accession O34926

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IUBMB Comments
A heme-thiolate (P-450) enzyme from the bacterium Bacillus subtilis. The order of events during the overall reaction is unknown. Pulcherrimic acid spontaneously forms an iron chelate with Fe(3+) to form the red pigment pulcherrimin .
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This record set is specific for:
Bacillus subtilis
UNIPROT: O34926
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
cyp134a1, pulcherriminic acid synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclo-L-leucyl-L-leucyl dipeptide oxidase
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cyclo-L-leucyl-L-leucyl dipeptide oxidase
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CYP134A1
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PATHWAY SOURCE
PATHWAYS
-
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SYSTEMATIC NAME
IUBMB Comments
cyclo(L-leucyl-L-leucyl),reduced-ferredoxin:oxygen oxidoreductase (N-hydroxylating,aromatizing)
A heme-thiolate (P-450) enzyme from the bacterium Bacillus subtilis. The order of events during the overall reaction is unknown. Pulcherrimic acid spontaneously forms an iron chelate with Fe(3+) to form the red pigment pulcherrimin [2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-phenylimidazole + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
?
2,5-di-tert-butylhydroquinone + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
?
2,5-di-tert-butylquinone + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
?
2-phenylimidazole + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
?
4-phenylimidazole + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
?
cyclo(L-alanyl-L-alanyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
?
cyclo(L-leucyl-L-leucyl) + reduced ferredoxin + O2
pulcherriminic acid + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
?
cyclo(L-leucyl-L-phenylalanyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
?
cyclo(L-leucyl-L-prolyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
?
cyclo(L-leucyl-L-tryptophanyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
?
cyclo(L-methionyl-L-methionyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
?
cyclo(L-valyl-L-valyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cyclo(L-leucyl-L-leucyl) + reduced ferredoxin + O2
pulcherriminic acid + oxidized ferredoxin + H2O
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, Resource Q column chromatography, and Superose-12 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Biochemistry
49
7282-7296
2010
Bacillus subtilis (O34926), Bacillus subtilis
Manually annotated by BRENDA team