Alcohol Dehydrogenase from Methylobacterium organophilum
نویسندگان
چکیده
منابع مشابه
Alcohol dehydrogenase from Methylobacterium organophilum.
The alcohol dehydrogenase from Methylobacterium organophilum, a facultative methane-oxidizing bacterium, has been purified to homogeneity as indicated by sodium dodecyl sulfate-gel electrophoresis. It has several properties in common with the alcohol dehydrogenases from other methylotrophic bacteria. The active enzyme is a dimeric protein, both subunits having molecular weights of about 62,000....
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The structure of methanol dehydrogenase (MDH) at 0.194 nm (1.94 A) has been used to provide a model structure for part of a membrane quinoprotein glucose dehydrogenase (GDH). The basic superbarrel structure is retained, along with the tryptophandocking motifs. The active-site regions are similar, but there are important differences, the most important being that GDH lacks the novel disulphide r...
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The 1.94 A structure of methanol dehydrogenase has been used to provide a model structure for part of a membrane quinohaemoprotein alcohol dehydrogenase. The basic superbarrel structure and the active-site region are retained, indicating essentially similar mechanisms of action, but there are considerable differences in the external loops, particularly those involved in formation of the shallow...
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Methylobacterium organophilum CZ-2 synthesized polyhydroxyalkanoates (PHAs) under nitrogen limitation with CH4 as carbon source and when either citrate or propionate was added as cosubstrates. The highest PHAs content (yPHA) in closed flasks was obtained in the CH4-citrate and CH4-propionate experiments attaining values of 0.82 and 0.68, respectively. M. organophilum CZ-2 cultivated in bioreact...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1978
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.36.1.105-114.1978