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Information on EC 1.13.11.6 - 3-hydroxyanthranilate 3,4-dioxygenase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P47096

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IUBMB Comments
Requires Fe2+.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P47096
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
3-hydroxyanthranilate 3,4-dioxygenase, 3-hydroxyanthranilic acid oxygenase, 3-hao, 3-hydroxyanthranilate oxygenase, 3-had, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-hydroxyanthranilate oxygenase
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3-hydroxyanthranilic acid oxidase
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3-hydroxyanthranilic acid oxygenase
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3-hydroxyanthranilic oxygenase
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3HAO
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oxygenase, 3-hydroxyanthranilate 3,4-di-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing)
Requires Fe2+.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-50-9
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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
3-hydroxyanthranilate + O2
2-amino-3-carboxymuconate semialdehyde
show the reaction diagram
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reacts spontaneously to quinolinic acid
?
3-hydroxyanthranilate + O2
2-amino-3-carboxymuconate semialdehyde
show the reaction diagram
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in the kynurenine pathway
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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
3-hydroxyanthranilate + O2
2-amino-3-carboxymuconate semialdehyde
show the reaction diagram
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in the kynurenine pathway
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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non-heme enzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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non-heme ferrous enzyme
Ni2+
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two nickel binding sites per molecule. One of the bound nickel atoms occupies the proposed ferrous-coordinated active site
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0159 - 0.0192
3-hydroxyanthranilic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop-vapor diffusion method, 2.4 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Y3HAO protein is subcloned into the pET-28a expression vector from extracted Saccharomyces cerevisiae genomic DNA, and the Y3HAO protein is highly expressed as a soluble protein in Escherichia coli strain BL21(DE3) with a six-residueHis tag attached to its N-terminus
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kucharczyk, R.; Zagulski, M.; Rytka, J.; Herbert, C.J.
The yeast gene YJR025c encodes a 3-hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis
FEBS Lett.
424
127-130
1998
Escherichia coli, Saccharomyces cerevisiae (P47096), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Li, X.; Guo, M.; Fan, J.; Tang, W.; Wang, D.; Ge, H.; Rong, H.; Teng, M.; Niu, L.; Liu, Q.; Hao, Q.
Crystal structure of 3-hydroxyanthranilic acid 3,4-dioxygenase from Saccharomyces cerevisiae: a special subgroup of the type III extradiol dioxygenases
Protein Sci.
15
761-773
2006
Saccharomyces cerevisiae
Manually annotated by BRENDA team