Requires zinc. Acts on both enantiomers of chiral epoxyalkanes to form the corresponding (R)- and (S)-2-hydroxyalkyl-CoM adducts. The enzyme will function with some other thiols (e.g., 2-sulfanylethanol) as the nucleophile. Uses short-chain epoxyalkanes from C2 (epoxyethane) to C6 (1,2-epoxyhexane). This enzyme forms component I of a four-component enzyme system (comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
Requires zinc. Acts on both enantiomers of chiral epoxyalkanes to form the corresponding (R)- and (S)-2-hydroxyalkyl-CoM adducts. The enzyme will function with some other thiols (e.g., 2-sulfanylethanol) as the nucleophile. Uses short-chain epoxyalkanes from C2 (epoxyethane) to C6 (1,2-epoxyhexane). This enzyme forms component I of a four-component enzyme system (comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]) that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
this enzyme forms component I of a four-component enzyme system, comprising EC 4.2.99.19 2-hydroxypropyl-CoM lyase, component I, EC 1.8.1.5 2-oxopropyl-CoM reductase (carboxylating), component II, EC 1.1.1.268 2-(R)-hydroxypropyl-CoM dehydrogenase, component II and EC 1.1.1.269 2-(S)-hydroxypropyl-CoM dehydrogenase, component IV that is involved in epoxyalkane carboxylation
this enzyme forms component I of a four-component enzyme system, comprising EC 4.2.99.19 2-hydroxypropyl-CoM lyase, component I, EC 1.8.1.5 2-oxopropyl-CoM reductase (carboxylating), component II, EC 1.1.1.268 2-(R)-hydroxypropyl-CoM dehydrogenase, component II and EC 1.1.1.269 2-(S)-hydroxypropyl-CoM dehydrogenase, component IV that is involved in epoxyalkane carboxylation
Zn plays a key role in activating an organic thiol substrate for nucleophilic attack on an alkyl-donating substrate, removal of Zn results in loss of catalytic activity, the inactive and Zn-deficient form of enzyme is activated by addition of ZnCl2 or CoCl2. Thermodynamic characterization of the interaction of CoM with an enzyme-bound Zn center
40% of the initial enzyme activity remains after 24 h of carbon starvation, while alkene monooxygenase activity is lost after 7 h. This imbalance likely contributes to the extended lag period by delaying epoxide accumulation and subsequent alkene monooxygenase induction
this enzyme forms component I of a four-component enzyme system, comprising EC 4.2.99.19 2-hydroxypropyl-CoM lyase, component I, EC 1.8.1.5 2-oxopropyl-CoM reductase (carboxylating), component II, EC 1.1.1.268 2-(R)-hydroxypropyl-CoM dehydrogenase, component II and EC 1.1.1.269 2-(S)-hydroxypropyl-CoM dehydrogenase, component IV that is involved in epoxyalkane carboxylation
the phylotype Nocardioides (Actinobacteria) is responsible for carbon assimilation from vinyl chloride. This phylotype is observed in the heavy fractions from the 13C-vinyl chloride-amended cultures at both day 32 and day 45. Identifcation of degrading strains uses gene etnE, encoding for epoxyalkane coenzymeM-transferase, a critical enzyme in the pathway for vinyl chloride degradation
Heterologous expression of bacterial epoxyalkane:coenzyme M transferase and inducible coenzyme M biosynthesis in Xanthobacter strain Py2 and Rhodococcus rhodochrous B276