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Methanol dehydrogenase structure
1996Methanol dehydrogenase (MEDH, EC 1.1.99.8) is a soluble quinoprotein located in the periplasmic space of many methylotrophic bacteria (Anthony, 1986). The enzyme catalyzes the oxidation of methanol to formaldehyde, utilizing the single carbon compound as the sole source of carbon and energy.
Z.-X. Xia +6 more
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Methanol Dehydrogenase, a PQQ-Containing Quinoprotein Dehydrogenase
2000Methanol dehydrogenase (MDH; EC 1.1.99.8) catalyses the oxidation of methanol to formaldehyde in the periplasm of methylotrophic bacteria during growth on methanol or methane. It was first described in Methylobacterium extorquens (Anthony and Zatman, 1964a,b) and has subsequently been shown to be the one feature that is common to almost all ...
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Purification and properties of methanol dehydrogenase from Methylophaga marina
Biochimie, 1987Purification of methanol dehydrogenase from Methylophaga marina, in order to avoid the instability observed in crude extracts, was achieved initially by a rapid procedure using mainly an aqueous two-phase partition system composed of polyethylene glycol 1000 (50%, v/v) and potassium phosphate (50%, w/v).
M, Janvier, F, Gasser
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Purification and properties of methanol dehydrogenase from Hyphomicrobium X
Biochimica et Biophysica Acta (BBA) - Enzymology, 1978(1) A method for the isolation of methanol dehydrogenase (alcohol:(acceptor) oxidoreductase, EC 1.1.99.8) from Hyphomicrobium X is decribed. The purified enzyme was resolved by polyacrylamide gel electrophoresis into one main and two minor active bands. Iron and manganese were the only detected metals in the enzyme preparation.
J A, Duine, J, Frank, J, Westerling
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On the mechanism of inhibition of methanol dehydrogenase by cyclopropane‐derived inhibitors
European Journal of Biochemistry, 1989Extraction of cyclopropanol‐inactivated methanol dehydrogenase (MDH) gave a mixture of two interconverting compounds. The same compounds could be prepared from 2,7,9‐tricarboxy‐1H‐pyrrolo[2,3‐f]quinoline‐4,5‐dione (PQQ) and cyclopropanol using a metal oxide (e.g. Ag2O) as a catalyst.
J, Frank +5 more
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Journal of Molecular Structure: THEOCHEM, 2009
Abstract Models representing the active sites of Ca2+- and Ba2+-containing methanol dehydrogenase (MDH) enzymes and their interaction with methanol are investigated using density functional theory methods and a continuum solvation model (PCM). Information on structure and energetics of such models in gas phase and implicit water solvent environments ...
N.B. Idupulapati, D.S. Mainardi
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Abstract Models representing the active sites of Ca2+- and Ba2+-containing methanol dehydrogenase (MDH) enzymes and their interaction with methanol are investigated using density functional theory methods and a continuum solvation model (PCM). Information on structure and energetics of such models in gas phase and implicit water solvent environments ...
N.B. Idupulapati, D.S. Mainardi
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X-ray structure of PQQ-dependent methanol dehydrogenase
1994The three-dimensional structure of the PQQ-dependent quinoprotein, methanol dehydrogenase from Methylobacterium extorquens AM1, has been determined at 3A resolution. The a2b2 tetrameric enzyme has a large a-chain of almost spherical form with a chain fold in which eight 4-stranded antiparallel b-sheets segments are arranged radially around a pseudo 8 ...
M, Ghosh +4 more
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Biosensor-Based Directed Evolution of Methanol Dehydrogenase from Lysinibacillus xylanilyticus
International Journal of Molecular Sciences, 2021Thien-Kim Le +2 more
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