| EC |
1.14.13.212 |
| Accepted name: |
1,3,7-trimethyluric acid 5-monooxygenase |
| Reaction: |
1,3,7-trimethylurate + NADH + H+ + O2 = 1,3,7-trimethyl-5-hydroxyisourate + NAD+ + H2O |
| Glossary: |
isourate = 1,3,5,7-tetrahydropurine-2,6,8-trione |
| Other name(s): |
tmuM (gene name) |
| Systematic name: |
1,3,7-trimethylurate,NADH:oxygen oxidoreductase (1,3,7-trimethyl-5-hydroxyisourate-forming) |
| Comments: |
The enzyme, characterized from the bacterium Pseudomonas sp. CBB1, is part of the bacterial C-8 oxidation-based caffeine degradation pathway. The product decomposes spontaneously to a racemic mixture of 3,6,8-trimethylallantoin. The enzyme shows no acitivity with urate. cf. EC 1.14.13.113, FAD-dependent urate hydroxylase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Mohanty, S.K., Yu, C.L., Das, S., Louie, T.M., Gakhar, L. and Subramanian, M. Delineation of the caffeine C-8 oxidation pathway in Pseudomonas sp. strain CBB1 via characterization of a new trimethyluric acid monooxygenase and genes involved in trimethyluric acid metabolism. J. Bacteriol. 194 (2012) 3872–3882. [DOI] [PMID: 22609920] |
| 2. |
Summers, R.M., Mohanty, S.K., Gopishetty, S. and Subramanian, M. Genetic characterization of caffeine degradation by bacteria and its potential applications. Microb. Biotechnol. 8 (2015) 369–378. [DOI] [PMID: 25678373] |
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| [EC 1.14.13.212 created 2016] |
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