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dc.contributor.authorScawen, M. D.
dc.contributor.authorBarstow, D. A.
dc.contributor.authorNicholls, D. J.
dc.contributor.authorAtkinson, T.
dc.contributor.authorClarke, A. R.
dc.contributor.authorWigley, D. B.
dc.contributor.authorHart, K. W.
dc.contributor.authorChia, W. N.
dc.contributor.authorHolbrook, J. J.
dc.date.accessioned2023-11-03T10:02:46Z
dc.date.available2023-11-03T10:02:46Z
dc.date.issued1989
dc.date.submitted2023-11-03
dc.identifier.citationAdvances in protein design, 103 - 115en_US
dc.identifier.isbn3527280243
dc.identifier.isbn0895739534
dc.identifier.issn0930-4320
dc.identifier.urihttp://hdl.handle.net/10033/623526
dc.description.abstractMany changes have been made by protein engineering in lactate dehydrogenase from B.stearothermophilus. The role of groups involved in susbtrate and coenzyme binding, catalysis and effector molecule binding has been deduced and variants with improved thermal stability developed. The native substrate catalysis patern of lactate dehydrogenase has been modified by many orders of magnitude, to convert this protein into essentially a highly active malate dehydrogenase. Work is Currently on-going to modify this further and to convert malate dehydrogenase, Similarly by protein engineering, into a functional lactate dehydrogenase.en_US
dc.language.isoenen_US
dc.publisherGBF Gesellschaft für Biotechnologische Forschung mbH, Braunschweigen_US
dc.relation.ispartofseriesGBF monographs ; Volume 12en_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleLACTATE DEHYDROGENASE : EFFECT OF AMINO ACID CHANGES ON PROPERTIESen_US
dc.typeBook chapteren_US
dc.typeconference paperen_US
dc.contributor.departmentDivision of Biotechnology, PHLS' Centre for Applied Microbiology and Research Porton Down, Salisbury, SP4 0JG; Department of Biochemistry University of Bristolen_US
dc.identifier.journalAdvances in protein design, 1988en_US
refterms.dateFOA2023-11-03T10:02:46Z


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Attribution-NonCommercial-ShareAlike 4.0 International
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