| EC |
1.14.13.229 |
| Accepted name: |
tert-butyl alcohol monooxygenase |
| Reaction: |
tert-butyl alcohol + NADPH + H+ + O2 = 2-methylpropane-1,2-diol + NADP+ + H2O |
| Other name(s): |
mdpJK (gene names); tert-butanol monooxygenase |
| Systematic name: |
tert-butyl alcohol,NADPH:oxygen oxidoreductase |
| Comments: |
The enzyme, characterized from the bacterium Aquincola tertiaricarbonis, is a Rieske nonheme mononuclear iron oxygenase. It can also act, with lower efficiency, on propan-2-ol, converting it to propane-1,2-diol. Depending on the substrate, the enzyme also catalyses EC 1.14.19.48, tert-amyl alcohol desaturase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Schafer, F., Breuer, U., Benndorf, D., von Bergen, M., Harms, H. and Muller, R.H. Growth of Aquincola tertiaricarbonis L108 on tert-butyl alcohol leads to the induction of a phthalate dioxygenase-related protein and its associated oxidoreductase subunit. Eng. Life Sci. 7 (2007) 512–519. |
| 2. |
Schuster, J., Schafer, F., Hubler, N., Brandt, A., Rosell, M., Hartig, C., Harms, H., Muller, R.H. and Rohwerder, T. Bacterial degradation of tert-amyl alcohol proceeds via hemiterpene 2-methyl-3-buten-2-ol by employing the tertiary alcohol desaturase function of the Rieske nonheme mononuclear iron oxygenase MdpJ. J. Bacteriol. 194 (2012) 972–981. [DOI] [PMID: 22194447] |
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| [EC 1.14.13.229 created 2016] |
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| EC |
1.14.19.48 |
| Accepted name: |
tert-amyl alcohol desaturase |
| Reaction: |
tert-amyl alcohol + NADPH + H+ + O2 = isoprenyl alcohol + NADP+ + 2 H2O |
| Glossary: |
isoprenyl alcohol = 3-methylbut-1-en-3-ol
tert-amyl alcohol = 2-methylbutan-2-ol |
| Other name(s): |
mdpJK (gene names) |
| Systematic name: |
tert-amyl alcohol,NADPH:oxygen oxidoreductase (1,2-dehydrogenating) |
| Comments: |
The enzyme, characterized from the bacterium Aquincola tertiaricarbonis, is a Rieske nonheme mononuclear iron oxygenase. It can also act, with lower efficiency, on butan-2-ol, converting it to but-1-en-3-ol. Depending on the substrate, the enzyme also catalyses EC 1.14.13.229, tert-butanol monooxygenase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Schafer, F., Schuster, J., Wurz, B., Hartig, C., Harms, H., Muller, R.H. and Rohwerder, T. Synthesis of short-chain diols and unsaturated alcohols from secondary alcohol substrates by the Rieske nonheme mononuclear iron oxygenase MdpJ. Appl. Environ. Microbiol. 78 (2012) 6280–6284. [DOI] [PMID: 22752178] |
| 2. |
Schuster, J., Schafer, F., Hubler, N., Brandt, A., Rosell, M., Hartig, C., Harms, H., Muller, R.H. and Rohwerder, T. Bacterial degradation of tert-amyl alcohol proceeds via hemiterpene 2-methyl-3-buten-2-ol by employing the tertiary alcohol desaturase function of the Rieske nonheme mononuclear iron oxygenase MdpJ. J. Bacteriol. 194 (2012) 972–981. [DOI] [PMID: 22194447] |
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| [EC 1.14.19.48 created 2016] |
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