| EC |
1.13.11.48 |
| Accepted name: |
3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase |
| Reaction: |
3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate + CO |
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For diagram of reaction, click here |
| Other name(s): |
(1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase |
| Systematic name: |
3-hydroxy-2-methyl-1H-quinolin-4-one 2,4-dioxygenase (CO-forming) |
| Comments: |
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. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 160995-63-1 |
| References: |
| 1. |
Bauer, I., De Beyer, A., Tsisuaka, B., Fetzner, S. and Lingens, F. A novel type of oxygenolytic ring cleavage: 2,4-Oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline. FEMS Microbiol. Lett. 117 (1994) 299–304. |
| 2. |
Bauer, I., Max, N., Fetzner, S. and Lingens, F. 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. Eur. J. Biochem. 240 (1996) 576–583. [DOI] [PMID: 8856057] |
| 3. |
Fischer, F., Kunne, S. and Fetzner, S. Bacterial 2,4-dioxygenases: new members of the hydrolase-fold superfamily of enzymes functionally related to serine hydrolases. J. Bacteriol. 181 (1999) 5725–5733. [PMID: 10482514] |
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| [EC 1.13.11.48 created 2001] |
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