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Heterologous expression AND characterization of mannitol-1-phasphate dehydrogenase from the basidiomycete Pholiotanameko KCI 등재
- 언어ENG
- URLhttps://db.koreascholar.com/Article/Detail/276324
pp.166-167
Basidiomycetes can degrade lignocellulosic biomass, and some basidiomycetes produce alcohol dehydrogenase, so it is feasible to produce alcohol from basidiomycetes. Agaricus blazei, Flammulina velutipes and Tricholoma matsutake have been used for mushroom fermentation to produce alcohol. To investigate whether Pholilta nameko can be used for mushroom fermentation, and find out the relationship between mannitol-1-phosphate dehydrogenase and alcohol dehydrogenase, we cloned mannitol-1-phosphate dehydrogenase gene from P. nameko, which is a zinc-containing long- chain alcohol dehydrogenase. Mpd, the gene encoding mannitol-1-phosphate dehydrogenase (MPD), has been sequenced and characterized from basiodiomycete P. nameko. The length of the coding region is 1360bp. The gene encodes a putative protein of 359 amino acids; predicted protein molecular weight is 38.6 kDa and an isoelectric point is PI = 7.34. The locations of exons and introns in the gene were deduced on the basis of interruptions in the amino acid sequence that were homologous to those in the MPD of Laccaria bicolor, the coding region was split into 6 exons and 5 introns. The protein deduced from the gene MPD showed more than 46% sequence identity to 20 fungal MPDs or alcohol dehydrogenases documented in the Gene bank protein database, based on BLASTP analysis, and was phylogenetically close to the MPDs of L. bicolor and Coprinopsis cinerea. This protein shared the same conserved domain with the alcohol dehydrogenase.
