Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-8-6
pubmed:abstractText
In order to clarify the structural role of subsite B of hen egg-white lysozyme in hydrolytic activity towards a carbohydrate substrate, we analysed the structures of Trp-62-->Gly and Asp-101-->Gly mutant hen lysozymes, which have no side chain at positions 62 or 101, complexed with a substrate analogue, (N-acetyl-d-glucosamine)3 [(GlcNAc)3], using X-ray crystallography. The overall protein structures in the mutant lysozyme complexes were almost identical to those in the wild type. In the crystals of all the mutant complexes, the (GlcNAc)3 molecule, which is an inhibitor of wild-type lysozyme, had no inhibitory effect, but was hydrolysed as a substrate. One of the products, (GlcNAc)2, the reducing end of which is an alpha-anomer, was bound in an unproductive binding mode, protruding from the active-site cleft, and was able to act as an inhibitor. Hydrolysis of the synthetic substrate by the mutants occurred in a beta-anomer-retaining manner, and so the alpha-anomer product was converted from the beta-anomer product. Thus the interactions of Asp-101 and Trp-62 in subsite B are not essential for the catalytic mechanism, but co-operatively enhance the affinity of the substrate in the productive binding mode, other than the inhibitor in the unproductive mode.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-15299801, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-1537843, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-1569548, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-1593630, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-1856865, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-2461836, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-3058393, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-3841182, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-4979456, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-6387440, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-7265240, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-7583653, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-7707375, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-7990138, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-8125914, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-8266098, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-8289309, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-8444153, http://linkedlifedata.com/resource/pubmed/commentcorrection/9639564-8885835
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
333 ( Pt 1)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
71-6
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Structural and functional effect of Trp-62-->Gly and Asp-101-->Gly substitutions on substrate-binding modes of mutant hen egg-white lysozymes.
pubmed:affiliation
Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University, Aoba-ku, Sendai 980-77, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't