The β-mannanase from 'Caldocellum saccharolyticum' is part of a multidomain enzyme

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dc.contributor.author Gibbs, MD en
dc.contributor.author Saul, DJ en
dc.contributor.author Luthi, E en
dc.contributor.author Bergquist, Peter en
dc.date.accessioned 2011-07-24T21:36:51Z en
dc.date.issued 1992 en
dc.identifier.citation Appl Environ Microbiol 58(12):3864-3867 Dec 1992 en
dc.identifier.issn 0099-2240 en
dc.identifier.uri http://hdl.handle.net/2292/7017 en
dc.description.abstract The complete sequence of a β-mannanase gene from an anaerobic extreme thermophile was determined, and it shows that the expressed protein consists of two catalytic domains and two binding domains separated by spacer regions rich in proline and threonine residues. The amino-terminal catalytic domain has β-mannanase activity, and the carboxy-terminal domain acts as an endoglucanase. Neither domain shows homology with any other cellulase or hemicellulase sequence at the nucleic acid or protein level. en
dc.language EN en
dc.relation.ispartofseries Applied and Environmental Microbiology en
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/0099-2240/ en
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm en
dc.subject ESCHERICHIA-COLI en
dc.subject BACILLUS-SUBTILIS en
dc.subject GENE en
dc.subject SEQUENCE en
dc.subject EXPRESSION en
dc.subject CELLULASE en
dc.title The β-mannanase from 'Caldocellum saccharolyticum' is part of a multidomain enzyme en
dc.type Journal Article en
pubs.issue 12 en
pubs.begin-page 3864 en
pubs.volume 58 en
dc.rights.holder Copyright: 1992 American Society for Microbiology en
dc.identifier.pmid 1476429 en
pubs.end-page 3867 en
dc.rights.accessrights http://purl.org/eprint/accessRights/RestrictedAccess en
pubs.subtype Article en
pubs.elements-id 184866 en
pubs.record-created-at-source-date 2013-06-05 en
pubs.dimensions-id 1476429 en


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