Cellobiohydrolase A (CbhA) from the cellulolytic bacterium Cellulomonas fimi is a beta-1,4-exocellobiohydrolase analogous to Trichoderma reesei CBH II.

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 Microbiol

journal_title

Molecular microbiology

authors

Meinke A,Gilkes NR,Kwan E,Kilburn DG,Warren RA,Miller RC Jr

doi

10.1111/j.1365-2958.1994.tb01030.x

subject

Has Abstract

pub_date

1994-05-01 00:00:00

pages

413-22

issue

3

eissn

0950-382X

issn

1365-2958

journal_volume

12

pub_type

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