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- W2021362013 abstract "The ggh-A gene, encoding a 1,4-β-d-glucan glucohydrolase/β-glucosidase, of Microbispora bispora (Mb) was subcloned and expressed from a 4.0-kb XhoI DNA fragment. The nucleotide sequence of this fragment was determined. Analysis of the sequence revealed one open reading frame (ORF) which encodes a 986-amino-acid (aa) protein with a calculated molecular weight of 107 510. The ggh-A ORF has features typical of an actinomycete gene including high GC content (70.5%) and corresponding biased codon usage. Comparison of the aa sequence of the Mb 1,4-β-d-glucan glucohydrolase (Mbggh-A) with other glycosidases reveals high overall homology to several β-glucosidases and a 1,4-β-d-glucan glucohydrolase belonging to the glycosyl hydrolase family 3. The aa sequence alignments of Mbggh-A and β-glucosidases show that the active site region potentially involves two Asp residues. The aa sequence homology studies revealed a potential two-domain structure for Mbggh-A and other β-glucosidases. Furthermore, Mbggh-A has localized homology to a cellulose-binding domain present in some xylanases. This report is significant, as, to date, 1,4-β-d-glucan glucohydrolases have rarely been reported, though they are assumed to have a critical role in cellulolysis." @default.
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- W2021362013 title "Cloning, sequencing and analysis of the ggh-A gene encoding a 1,4-β-d-glucan glucohydrolase from Microbispora bispora" @default.
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- W2021362013 doi "https://doi.org/10.1016/0378-1119(96)00076-5" @default.
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