Linked Life Data

8444153

Source:http://linkedlifedata.com/resource/pubmed/id/8444153

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-4-2
pubmed:abstractText
The subsite structures in the active site of hen egg-white lysozyme were altered by site-directed mutagenesis. Replacement of Trp62, which is involved in apolar interaction with a sugar ring, and Asp101, which is hydrogen bonded to the same sugar ring in subsite B, led to a shift of the oligosaccharide-binding mode in the active-site cleft. Consequently, the double-mutant lysozyme (Trp62His, Asp101Gly) exhibited a drastic change of substrate-binding without any significant loss of enzymic activity. Conversion of Asn37, which is postulated to be involved in interaction with a sugar ring in subsite F, had a reverse effect on substrate binding. Nuclear magnetic resonance analysis of mutant lysozymes, in which Trp62 was replaced with Phe or His, suggested that these replacements not only altered the structure of the amino acid chain at position 62 of the lysozyme, but also induced local structural changes around the residue at position 62.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
212
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
151-6
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Effects of subsite alterations on substrate-binding mode in the active site of hen egg-white lysozyme.
pubmed:affiliation
Department of Industrial Chemistry, Faculty of Engineering, University of Tokyo, Bunkyo-ku, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't