Information on EC 1.14.15.13 - pulcherriminic acid synthase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.14.15.13
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RECOMMENDED NAME
GeneOntology No.
pulcherriminic acid synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cyclo(L-leucyl-L-leucyl) + 6 reduced ferredoxin + 3 O2 = pulcherriminic acid + 6 oxidized ferredoxin + 4 H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pulcherrimin biosynthesis
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 56775
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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
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?
2,5-di-tert-butylhydroquinone + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
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?
2,5-di-tert-butylquinone + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
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?
2-phenylimidazole + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
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-
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?
4-phenylimidazole + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
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?
cyclo(L-alanyl-L-alanyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
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?
cyclo(L-leucyl-L-leucyl) + reduced ferredoxin + O2
pulcherriminic acid + oxidized ferredoxin + H2O
show the reaction diagram
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?
cyclo(L-leucyl-L-phenylalanyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
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?
cyclo(L-leucyl-L-prolyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
-
-
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?
cyclo(L-leucyl-L-tryptophanyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
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?
cyclo(L-methionyl-L-methionyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
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?
cyclo(L-valyl-L-valyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
O34926
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
ENGINEERING
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