Abstract:
:The gene cbhA from the cellulolytic bacterium Cellulomonas fimi encodes a protein of 872 amino acids designated cellobiohydrolase A (CbhA). Mature CbhA contains 832 amino acid residues and has a predicted molecular mass of 85,349 Da. It is composed of five domains: an N-terminal catalytic domain, three repeated sequences of 95 amino acids, and a C-terminal cellulose-binding domain typical of other C. fimi glycanases. The structure and enzymatic activities of the CbhA catalytic domain are closely related to those of CBH II, an exocellobiohydrolase in the glycosyl hydrolase family B from the fungus Trichoderma reesei. CbhA is the first such enzyme to be characterized in bacteria. The data support the proposal that extended loops around the active site distinguish exohydrolases from endohydrolases in this enzyme family.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Meinke A,Gilkes NR,Kwan E,Kilburn DG,Warren RA,Miller RC Jrdoi
10.1111/j.1365-2958.1994.tb01030.xsubject
Has Abstractpub_date
1994-05-01 00:00:00pages
413-22issue
3eissn
0950-382Xissn
1365-2958journal_volume
12pub_type
杂志文章abstract::The DNA encoding the zinc metalloprotease of Legionella pneumophila Philadelphia 1 has been isolated and expressed in Escherichia coli. This protein, which is 38,000 Daltons in size, possesses immunological and biochemical properties identical to those previously described for the purified L. pneumophila protease. Per...
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