Information on EC 1.14.14.13 - 4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] monooxygenase

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The expected taxonomic range for this enzyme is: Bacillus circulans

EC NUMBER
COMMENTARY hide
1.14.14.13
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RECOMMENDED NAME
GeneOntology No.
4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] + FMNH2 + O2 = 4-(gamma-L-glutamylamino)-(2S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] + FMN + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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butirosin biosynthesis
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Neomycin, kanamycin and gentamicin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein],FMN:oxygen oxidoreductase (2-hydroxylating)
Catalyses a step in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family. FMNH2 is used as a free cofactor. Forms a complex with a dedicated NAD(P)H:FMN oxidoreductase. The enzyme is not able to hydroxylate free substrates, activation by the acyl-carrier protein is mandatory. Octanoyl-S-[BtrI acyl-carrier protein] is also accepted.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
putative
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
involved in biosynthesis of the aminoglycoside antibiotic butirosin
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-(L-gamma-glutamylamino)butanoyl-[BtrI acyl-carrier protein] + FMNH2 + O2
4-(L-gamma-glutamylamino)-(2S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] + FMN + H2O
show the reaction diagram
presence of FMN and O2 are required
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?
butanoyl-[BtrI acyl-carrier protein] + FMNH2 + O2
(2S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] + FMN + H2O
show the reaction diagram
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?
octanoyl-[BtrI acyl-carrier protein] + FMNH2 + O2
(2S)-2-hydroxyoctanoyl-[BtrI acyl-carrier protein] + FMN + H2O
show the reaction diagram
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?
additional information
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no substrates: butanoate, butanoyl-CoA, L-glutamate, L-aspartate, gamma-aminobutanoate, and L-ornithine
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
no cofactor: FAD
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38700
x * 38700, calculated, x * 40000, SDS-PAGE of recombinant His-tagged protein
40000
x * 38700, calculated, x * 40000, SDS-PAGE of recombinant His-tagged protein
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 38700, calculated, x * 40000, SDS-PAGE of recombinant His-tagged protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli