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Research Article
1 June 1991

Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families

Abstract

Several types of domain occur in beta-1, 4-glycanases. The best characterized of these are the catalytic domains and the cellulose-binding domains. The domains may be joined by linker sequences rich in proline or hydroxyamino acids or both. Some of the enzymes contain repeated sequences up to 150 amino acids in length. The enzymes can be grouped into families on the basis of sequence similarities between the catalytic domains. There are sequence similarities between the cellulose-binding domains, of which two types have been identified, and also between some domains of unknown function. The beta-1, 4-glycanases appear to have arisen by the shuffling of a relatively small number of progenitor sequences.

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Published In

cover image Microbiological Reviews
Microbiological Reviews
Volume 55Number 2June 1991
Pages: 303 - 315
PubMed: 1886523

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Published online: 1 June 1991

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Authors

N R Gilkes
Department of Microbiology, University of British Columbia, Vancouver, Canada.
B Henrissat
Department of Microbiology, University of British Columbia, Vancouver, Canada.
D G Kilburn
Department of Microbiology, University of British Columbia, Vancouver, Canada.
R C Miller, Jr
Department of Microbiology, University of British Columbia, Vancouver, Canada.
R A Warren
Department of Microbiology, University of British Columbia, Vancouver, Canada.

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