Diversity of glycerol dehydrogenase in methylotrophic yeasts.
نویسندگان
چکیده
منابع مشابه
Purification and properties of methyl formate synthase, a mitochondrial alcohol dehydrogenase, participating in formaldehyde oxidation in methylotrophic yeasts.
Methyl formate synthase, which catalyzes methyl formate formation during the growth of methylotrophic yeasts, was purified to homogeneity from methanol-grown Candida boidinii and Pichia methanolica cells. Both purified enzymes were tetrameric, with identical subunits with molecular masses of 42 to 45 kDa, containing two atoms of zinc per subunit. The enzymes catalyze NAD(+)-linked dehydrogenati...
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Bioconversion of cellulosic material into bioethanol needs cellulase complex enzymesthat contain endoglucanase, exoglucanase and beta glucosidase. One of the most important organisms that produce cellulases is the filamentous fungi, Trichoderma reesei which able to secrete large amounts of different cellulases. These enzymes are probably the most widely used cellulases industrially, however, th...
متن کاملStructure of glycerol dehydrogenase from Serratia.
The 1.90 Å resolution X-ray crystal structure of glycerol dehydrogenase derived from contaminating bacteria present during routine Escherichia coli protein expression is presented. This off-target enzyme showed intrinsic affinity for Ni(2+)-Sepharose, migrated at the expected molecular mass for the target protein during gel filtration and was crystallized before it was realised that contaminati...
متن کاملProduction of D-mannitol and glycerol by yeasts.
D-Mannitol has not so far been known as a major product of sugar metabolism by yeasts. Three yeast strains, a newly isolated yeast from soy-sauce mash, Torulopsis versatilis, and T. anomala, were found to be good mannitol producers. Under optimal conditions, the isolate produced mannitol at good yield of 30% of the sugar consumed. Glucose, fructose, mannose, galactose, maltose, glycerol, and xy...
متن کاملAn NAD+-dependent alanine dehydrogenase from a methylotrophic bacterium.
A study was made of the NAD+-dependent alanine dehydrogenase (EC 1.4.1.1) elaborated by the methylotrophic bacterium Pseudomonas sp. strain MA when growing on succinate and NH4Cl. This enzyme was purified 400-fold and was found to be highly specific for NH3 and NAD+; however, hydroxypyruvate and bromopyruvate, but not alpha-oxoglutarate or glyoxylate, could replace pyruvate to a limited extent....
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1987
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.51.2401