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.
degradation of tert-amyl alcohol leads to formation of beta and gamma isomers of isoamylene. Both tert-alkyl alcohol degradation and alkene production are strictly oxygen dependent, the relative contribution of the dehydration reaction to total alcohol conversion increased with decreasing oxygen concentrations
degradation of tert-amyl alcohol leads to formation of beta and gamma isomers of isoamylene. Both tert-alkyl alcohol degradation and alkene production are strictly oxygen dependent, the relative contribution of the dehydration reaction to total alcohol conversion increased with decreasing oxygen concentrations
degradation of tert-amyl alcohol leads to formation of beta and gamma isomers of isoamylene. Both tert-alkyl alcohol degradation and alkene production are strictly oxygen dependent, the relative contribution of the dehydration reaction to total alcohol conversion increased with decreasing oxygen concentrations
MdpJ knockout mutants are not able to grow on the tertiary alcohols tert-butanol and tert-amyl alcohol, whereas 2-methylpropan-1,2-diol, the putative product of tert-butanol hydroxylation by MdpJ catalysis can still be used as the sole source of energy and carbon. The postulated 2-methylpropan-1,2-diol intermediate 2-hydroxyisobutanoate is metabolized by wild-type and mutant strains at the same rates. tert-amyl alcohol and hemiterpene degradation are linked with the catabolic route of leucine
degradation of tert-amyl alcohol leads to formation of beta and gamma isomers of isoamylene. Both tert-alkyl alcohol degradation and alkene production are strictly oxygen dependent, the relative contribution of the dehydration reaction to total alcohol conversion increased with decreasing oxygen concentrations; MdpJ knockout mutants are not able to grow on the tertiary alcohols tert-butanol and tert-amyl alcohol, whereas 2-methylpropan-1,2-diol, the putative product of tert-butanol hydroxylation by MdpJ catalysis can still be used as the sole source of energy and carbon. The postulated 2-methylpropan-1,2-diol intermediate 2-hydroxyisobutanoate is metabolized by wild-type and mutant strains at the same rates. tert-amyl alcohol and hemiterpene degradation are linked with the catabolic route of leucine
MdpJ is not hydroxylating tert-amyl alcohol to diols but functions as a desaturase, resulting in the formation of the hemiterpene 3-methyl-1-buten-3-ol. The latter is further processed via the hemiterpenes prenol, prenal, and 3-methylcrotonic acid
MdpJ is not hydroxylating tert-amyl alcohol to diols but functions as a desaturase, resulting in the formation of the hemiterpene 3-methyl-1-buten-3-ol. The latter is further processed via the hemiterpenes prenol, prenal, and 3-methylcrotonic acid
Schuster, J.; Schaefer, F.; Huebler, N.; Brandt, A.; Rosell, M.; Haertig, C.; Harms, H.; Mueller, R.H.; 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