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

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Neil R. Gilkes, Bernard Henrissat, Douglas G. Kilburn, Robert C. Miller, R. A. J. Warren·1991·Microbiological Reviews

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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Metadata

Authors
Gilkes, N. R., Henrissat, B., Kilburn, D. G., Miller, R. C., & Warren, R. A. J.
Venue
Microbiological Reviews
Publisher
American Society for Microbiology
Published
1991-01-01
Volume
55
Issue
2
Pages
303-315
ISSN
0146-0749 (ISSN-L)
OpenAlex
W1778903788
Cited by
961
References
0
FWCI
52.01
Type
journal article
Language
en
Open access
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Gilkes, N. R., Henrissat, B., Kilburn, D. G., Miller, R. C., & Warren, R. A. J. (1991). Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families. Microbiological Reviews. https://doi.org/10.1128/mmbr.55.2.303-315.1991

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