Information on EC 1.14.15.13 - pulcherriminic acid synthase

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

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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].
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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
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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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-
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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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-
-
?
4-phenylimidazole + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
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-
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?
cyclo(L-alanyl-L-alanyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
show the reaction diagram
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-
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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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-
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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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-
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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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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56300
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x * 56300, calculated from amino acid sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, Resource Q column chromatography, and Superose-12 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.15.13)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)