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Information on EC 1.14.13.223 - 3-hydroxy-4-methylanthranilyl-[aryl-carrier protein] 5-monooxygenase and Organism(s) Streptosporangium sibiricum and UniProt Accession C0LTM1

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IUBMB Comments
A flavoprotein (FAD). The enzyme, characterized from the bacterium Streptosporangium sibiricum, is involved in the biosynthesis of the antitumor antibiotic sibiromycin. The enzyme is not active with free 3-hydroxy-4-methylanthranilate.
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This record set is specific for:
Streptosporangium sibiricum
UNIPROT: C0LTM1
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The taxonomic range for the selected organisms is: Streptosporangium sibiricum
The expected taxonomic range for this enzyme is: Streptosporangium sibiricum
Synonyms
sibG, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sibG
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
3-hydroxy-4-methylanthranilyl-[aryl-carrier protein],NADH:oxygen oxidoreductase (5-hydroxylating)
A flavoprotein (FAD). The enzyme, characterized from the bacterium Streptosporangium sibiricum, is involved in the biosynthesis of the antitumor antibiotic sibiromycin. The enzyme is not active with free 3-hydroxy-4-methylanthranilate.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxy-4-methylanthranilyl-[aryl-carrier protein] + NADH + H+ + O2
3,5-dihydroxy-4-methylanthranilyl-[aryl-carrier protein] + NAD+ + H2O
show the reaction diagram
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SibG hydroxylates the C5 position of peptidyl-carrier protein-bound 3-hydroxy-4-methylanthranilic acid
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.743
3-hydroxy-4-methylanthranilyl-[aryl-carrier protein]
pH 7.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.48
3-hydroxy-4-methylanthranilyl-[aryl-carrier protein]
pH 7.0, 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
biosynthesis of the antitumor antibiotic sibiromycin. Starting from 3-hydroxykynurenine, the SAM-dependent methyltransferase SibL converts the substrate to its 4-methyl derivative, followed by hydrolysis through the action of the PLP-dependent kynureninase SibQ, leading to 3-hydroxy-4-methylanthranilic acid formation. Subsequently the nonribosomal peptide synthetase SibE activates 3-hydroxy-4-methylanthranilic acid and tethers it to its thiolation domain, where it is hydroxylated at the C5 position by the FAD/NADH-dependent hydroxylase SibG yielding the fully substituted anthranilate moiety found in sibiromycin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SIBG_STRSJ
351
0
38088
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 39900, SDS-PAGE, recombinant His-tagged protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Giessen, T.W.; Kraas, F.I.; Marahiel, M.A.
A four-enzyme pathway for 3,5-dihydroxy-4-methylanthranilic acid formation and incorporation into the antitumor antibiotic sibiromycin
Biochemistry
50
5680-5692
2011
Streptosporangium sibiricum (C0LTM1)
Manually annotated by BRENDA team