Structure/function relationships in methylotrophic yeasts
نویسندگان
چکیده
منابع مشابه
Comparison of biochemical properties of recombinant endoglucanase II of Trichoderma reesei in methylotrophic yeasts, Pichia pastoris and Hansenula polymorpha
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 کاملcomparison of biochemical properties of recombinant endoglucanase ii of trichoderma reesei in methylotrophic yeasts, pichia pastoris and hansenula polymorpha
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 کاملPurification 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...
متن کاملAlcohol oxidase and dihydroxyacetone synthase, the abundant peroxisomal proteins of methylotrophic yeasts, assemble in different cellular compartments.
Alcohol oxidase (AO) and dihydroxyacetone synthase (DHAS) constitute the bulk of matrix proteins in methylotrophic yeasts, model organisms for the study of peroxisomal assembly. Both are homooligomers; AO is a flavin-containing octamer, whereas DHAS is a thiamine pyrophosphate-containing dimer. Experiments in recent years have demonstrated that assembly of peroxisomal oligomers can occur before...
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: FEMS Microbiology Letters
سال: 1990
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.1990.tb04912.x