Mannitol Metabolism in Agaricus bisporus: Purification and Properties of Mannitol Dehydrogenase
نویسندگان
چکیده
منابع مشابه
Mannitol Dehydrogenase from Agaricus Campestris.
Enzymes capable of catalyzing n-mannitol formation from n-fructose or n-fructose 6-phosphate have been identified in various microorganisms. Substrate and coenzyme specificity have been established in only a few instances, but there appear to be enzymes, dependent upon nicotinamide adenine dinucleotide and upon nicotinamide adenine dinucleotide phosphate, which reduce fructose directly to manni...
متن کاملCrystallization and preliminary crystallographic analysis of mannitol dehydrogenase (MtDH) from the common mushroom Agaricus bisporus.
Mannitol dehydrogenase (MtDH) is a key enzyme controlling the reductive synthesis of mannitol from fructose in the common mushroom Agaricus bisporus. A better understanding of the control of mannitol metabolism can be obtained by studying the structure of this enzyme. Here, the purification and crystallization of recombinant MtDH are reported. Crystals generally belonged to the space group C2, ...
متن کاملPurification and characterization of mannitol dehydrogenase from Aspergillus parasiticus.
Mannitol dehydrogenase, NADP specific (EC 1.1.1.138), was purified from mycelium of Aspergillus parasiticus (1-11-105 Whl). The enzyme had a molecular weight of 1.4 X 10(5) and was composed of four subunits of apparently equal size. The substrate specificity was limited to D-mannitol, D-glucitol, D-arabinitol, 1-deoxy-D-mannitol, and 1-deoxy-D-glucitol. Zinc ion was a powerful inhibitor of the ...
متن کاملProduction , Purification and Properties of Extracellular Laccase of Agaricus bisporus
Extracellular laccase (EC 1 .14.18.1) of the cultivated mushroom Agaricus bisporus was produced constitutively in defined or complex media. No enzyme induction was found after treatment with cycloheximide or with other potential inducers such as toluidine or xylidine. The enzyme was purified to homogeneity by ammonium sulphate precipitation, ion-exchange chromatography, gel filtration and affin...
متن کاملPurification and characterisation of mannitol dehydrogenase from Lactobacillus sanfranciscensis.
Mannitol dehydrogenase (MDH) was purified and characterised from Lactobacillus sanfranciscensis. Two peptide fragments of MDH were N-terminally sequenced for the first time in the genus Lactobacillus. The purified enzyme had an apparent molecular mass of 44 kDa and catalysed both the reduction of fructose to mannitol and the oxidation of mannitol to fructose. The K(m) value for the reduction re...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Microbiology
سال: 1985
ISSN: 1350-0872,1465-2080
DOI: 10.1099/00221287-131-11-2885