| Literature DB >> 2176451 |
J Koizumi1, M Zhang, T Imanaka, S Aiba.
Abstract
Thermostabilities of kanamycin nucleotidyltransferase and of its mutants that became thermostable, in the free state, because of single-amino-acid replacements were studied after immobilization of the enzymes on cyanogen bromide-activated Sephadex G-200 particles. Lys in place of Gln at position 102 decreased the thermostability of the immobilized enzyme, whereas replacement with other amino acids enhanced it.Entities:
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Year: 1990 PMID: 2176451 PMCID: PMC185035 DOI: 10.1128/aem.56.11.3612-3614.1990
Source DB: PubMed Journal: Appl Environ Microbiol ISSN: 0099-2240 Impact factor: 4.792