| EC |
1.5.99.14 |
| Accepted name: |
6-hydroxypseudooxynicotine dehydrogenase |
| Reaction: |
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + acceptor + H2O = 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + reduced acceptor |
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For diagram of nicotine catabolism by arthrobacter, click here |
| Glossary: |
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 6-hydroxypseudooxynicotine
1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 2,6-dihydroxypseudooxynicotine |
| Systematic name: |
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one:acceptor 6-oxidoreductase (hydroxylating) |
| Comments: |
Contains a cytidylyl molybdenum cofactor [3]. The enzyme, which participates in the nicotine degradation pathway, has been characterized from the soil bacterium Arthrobacter nicotinovorans [1,2]. |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Freudenberg, W., Konig, K. and Andreesen, J. R. Nicotine dehydrogenase from Arthrobacter oxidans: A molybdenum-containing hydroxylase. FEMS Microbiology Letters 52 (1988) 13–18. |
| 2. |
Grether-Beck, S., Igloi, G.L., Pust, S., Schilz, E., Decker, K. and Brandsch, R. Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans. Mol. Microbiol. 13 (1994) 929–936. [DOI] [PMID: 7815950] |
| 3. |
Sachelaru, P., Schiltz, E. and Brandsch, R. A functional mobA gene for molybdopterin cytosine dinucleotide cofactor biosynthesis is required for activity and holoenzyme assembly of the heterotrimeric nicotine dehydrogenases of Arthrobacter nicotinovorans. Appl. Environ. Microbiol. 72 (2006) 5126–5131. [DOI] [PMID: 16820521] |
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| [EC 1.5.99.14 created 2012] |
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| EC |
3.7.1.19 |
| Accepted name: |
2,6-dihydroxypseudooxynicotine hydrolase |
| Reaction: |
1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O = 2,6-dihydroxypyridine + 4-methylaminobutanoate |
|
For diagram of nicotine catabolism by arthrobacter, click here |
| Glossary: |
1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 2,6-dihydroxypseudooxynicotine |
| Systematic name: |
1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one hydrolase |
| Comments: |
The enzyme, characterized from the soil bacterium Arthrobacter nicotinovorans, participates in nicotine degradation. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Gherna, R.L., Richardson, S.H. and Rittenberg, S.C. The bacterial oxidation of nicotine. VI. The metabolism of 2,6-dihydroxypseudooxynicotine. J. Biol. Chem. 240 (1965) 3669–3674. [PMID: 5835946] |
| 2. |
Sachelaru, P., Schiltz, E., Igloi, G.L. and Brandsch, R. An α/β-fold C—C bond hydrolase is involved in a central step of nicotine catabolism by Arthrobacter nicotinovorans. J. Bacteriol. 187 (2005) 8516–8519. [DOI] [PMID: 16321959] |
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| [EC 3.7.1.19 created 2012] |
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