EC Number   |
General Information |
Reference |
|---|
   1.1.1.244 | evolution |
Mdh2 is a group III Adh |
-, 741715 |
| 1.1.1.244 | evolution |
strain MGA3 contains three isozymes that belong to the type III Fe-NAD+-dependent alcohol dehydrogenases, but show a distinct substrate specificity and major differences with respect to transcriptional regulation of the paralogous genes |
-, 726329 |
| 1.1.1.244 | evolution |
strain PB1 contains three isozymes that belong to the type III Fe-NAD+-dependent alcohol dehydrogenases, but show a distinct substrate specificity and major differences with respect to transcriptional regulation of the paralogous genes |
-, 726329 |
| 1.1.1.244 | evolution |
the enzyme belongs to the type III alcohol dehydrogenase (Adh) family |
-, 742514 |
| 1.1.1.244 | evolution |
the formaldehyde reduction activity of the enzyme is successfully improved by directed evolution and screening, which might potentially be useful for the conversion of CO2 to methanol |
-, 763722 |
| 1.1.1.244 | metabolism |
assimilation of methanol into central metabolism, overview |
743225 |
| 1.1.1.244 | metabolism |
methanol dehydrogenase, is a crucial enzyme for utilizing methane and methanol as carbon and energy sources in methylotrophy and synthetic methylotrophy |
763157 |
| 1.1.1.244 | metabolism |
methanol oxidation catalyzed by methanol dehydrogenase is one of the key steps in methanol utilization in bacterial methylotrophy |
-, 763060 |
| 1.1.1.244 | metabolism |
the enzyme catalyzes a key step for ethanol production in bacterial methylotrophy and a key step for both toxic formaldehyde elimination |
-, 763722 |
| 1.1.1.244 | more |
in nature, methanol dehydrogenase (Mdh), which converts methanol to formaldehyde, highly favors the reverse reaction, efficient coupling with the irreversible sequestration of formaldehyde by 3-hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloseisomerase (Phi) serves as the key driving force to pull the pathway equilibrium toward central metabolism. An emerging strategy to promote efficient substrate channeling is to spatially organize pathway enzymes in an engineered assembly to provide kinetic driving forces that promote carbon flux in a desirable direction. A scaffoldless, self-assembly strategy is applied to organize Mdh, Hps, and Phi into an engineered supramolecular enzyme complex using an SH3-ligand interaction pair, which enhances methanol conversion to fructose-6-phosphate. An NADH sink is created using Escherichia coli lactate dehydrogenase as an NADH scavenger, thereby preventing reversible formaldehyde reduction, to increase methanol consumption. Combination of the two strategies improves in vitro fructose 6-phosphate production by 97fold compared with unassembled enzymes. The beneficial effect of supramolecular enzyme assembly is also realized in vivo as the engineered enzyme assembly improves whole-cell methanol consumption rate by ninefold. This approach ultimately allows direct coupling of enhanced fructose 6-phosphate synthesis with other metabolic engineering strategies for the production of many desired metabolites from methanol |
-, 743689 |
