Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1983-3-24
pubmed:abstractText
Circular-dichroism and fluorescence studies indicate that the 5-dimethylaminonaphthalene-1-sulphonyl and phenylmethanesulphonyl derivatives of subtilisin DY have three-dimensional structure closely similar to that of native enzyme. The single tryptophan residue is largely accessible to the aqueous solvent, and is not directly involved in the enzyme-substrate interactions, since its photochemical modification causes only a partial inhibition of the enzyme activity. It appears very likely that the location of the single tryptophan residue in the three-dimensional structure of subtilisin DY is similar to that of the single tryptophan residue in subtilisin Carlsberg. Fluorescence-quenching experiments further indicate that the 14 tyrosine residues are also largely accessible to the aqueous solvent, and probably interact with hydrated peptide carbonyl groups. The charge environment for tryptophan and tyrosine residues in subtilisin DY, as deduced by quenching experiments with ionic species, is also discussed. In general, subtilisin DY displays strong similarities to subtilisin Carlsberg, as suggested by a comparative analysis of the amino acid composition and fluorescence properties.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-13837240, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-14933256, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-235273, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-238582, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-25246, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-4310322, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-4366945, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-4583619, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-4755422, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-4967581, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-5055784, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-5056240, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-5119250, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-5484810, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-5763076, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-6065094, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-6818946, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-6990995, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-8113, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-843526, http://linkedlifedata.com/resource/pubmed/commentcorrection/6818945-986170
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
207
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
193-200
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Chemical, photochemical and spectroscopic characterization of an alkaline proteinase from Bacillus subtilis variant DY.
pubmed:publicationType
Journal Article, Comparative Study