KEGG ENZYME: 1.13.11.48

ENZYME: 1.13.11.48

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

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

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)

AGRA:

AGRA3207_003896

Reference

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)
DOI:10.1128/JB.181.18.5725-5733.1999

Sequence

[ag:CAA75080]