KEGG   ENZYME: 1.13.11.48Help
Entry
EC 1.13.11.48               Enzyme                                 

Name
3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase;
(1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase
Class
Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of two atoms of oxygen
BRITE hierarchy
Sysname
3-hydroxy-2-methyl-1H-quinolin-4-one 2,4-dioxygenase (CO-forming)
Reaction(IUBMB)
3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate + CO [RN:R05720]
Reaction(KEGG)
R05720;
(other) R05155
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Substrate
3-hydroxy-2-methyl-1H-quinolin-4-one [CPD:C11504];
O2 [CPD:C00007]
Product
N-acetylanthranilate [CPD:C06332];
CO [CPD:C00237]
Comment
Does not contain a metal centre or organic cofactor. Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide. The enzyme from Arthrobacter sp. can also act on 3-hydroxy-4-oxoquinoline, forming N-formylanthranilate and CO (cf. EC 1.13.11.47, 3-hydroxy-4-oxoquinoline 2,4-dioxygenase), but more slowly.
History
EC 1.13.11.48 created 2001
Orthology
K21821  3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase
Genes
ARR: ARUE_113p00080(meqE)
Taxonomy
Reference
1
  Authors
Bauer, I., De Beyer, A., Tsisuaka, B., Fetzner, S. and Lingens, F.
  Title
A novel type of oxygenolytic ring cleavage: 2,4-Oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline.
  Journal
FEMS Microbiol Lett 117:299-304 (1994)
Reference
2  [PMID:8856057]
  Authors
Bauer I, Max N, Fetzner S, Lingens F.
  Title
2,4-dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1.
  Journal
Eur J Biochem 240:576-83 (1996)
DOI:10.1111/j.1432-1033.1996.0576h.x
Reference
3  [PMID:10482514]
  Authors
Fischer F, Kunne S, Fetzner S.
  Title
Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases.
  Journal
J Bacteriol 181:5725-33 (1999)
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.13.11.48
IUBMB Enzyme Nomenclature: 1.13.11.48
ExPASy - ENZYME nomenclature database: 1.13.11.48
UM-BBD (Biocatalysis/Biodegradation Database): 1.13.11.48
BRENDA, the Enzyme Database: 1.13.11.48
CAS: 160995-63-1

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