Linked Life Data

3237715

Source:http://linkedlifedata.com/resource/pubmed/id/3237715

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1989-5-2
pubmed:abstractText
Proteinase K, the extracellular serine endopeptidase (E.C.3.4.21.14) from the fungus Tritirachium album limber, is homologous to the bacterial subtilisin proteases. The binding geometry of the synthetic inhibitor carbobenzoxy-Ala-Phechloromethyl ketone to the active site of proteinase K was first determined from a Fourier synthesis based on synchrotron X-ray diffraction data between 1.8 A and 5.0 A resolution. The protein inhibitor complex was refined by restrained least-squares minimization with the data between 10.0 and 1.8 A. The final R factor was 19.1%, and the model contained 2,018 protein atoms, 28 inhibitor atoms, 125 water molecules, and two Ca2+ ions. The peptide portion of the inhibitor is bound to the active center of proteinase K by means of a three-stranded antiparallel pleated sheet, with the side chain of the phenylalanine located in the P1 site. Model building studies, with lysine replacing phenylalanine in the inhibitor, explain the relatively unspecific catalytic activity of the enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0887-3585
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-64
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
X-ray and model-building studies on the specificity of the active site of proteinase K.
pubmed:affiliation
European Molecular Biology Laboratory, Hamburg, Federal Republic of Germany.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't