Linked Life Data

7971953

Source:http://linkedlifedata.com/resource/pubmed/id/7971953

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1994-12-29
pubmed:abstractText
Carboxypeptidase Y is a serine carboxypeptidase isolated from Saccharomyces cerevisiae with a preference for C-terminal hydrophobic amino acid residues. In order to alter the inherent substrate specificity of CPD-Y into one for basic amino acid residues in P'1, we have introduced Asp and/or Glu residues at a number of selected positions within the S'1 binding site. The effects of these substitutions on the substrate specificity, pH dependence and protein stability have been evaluated. The results presented here demonstrate that it is possible to obtain significant changes in the substrate preference by introducing charged amino acids into the framework provided by an enzyme with a quite different specificity. The introduced acidic amino acid residues provide a marked pH dependence of the (kcat/Km)FA-A-R-OH/(kcat/Km)FA-A-L-OH ratio. The change in stability upon introduction of Asp/Glu residues can be correlated to the difference in the mean buried surface area between the substituted and the substituting amino acid. Thus, the effects of acidic amino acid residues on the protein stability depend upon whether the introduced amino acid protrudes from the solvent accessible surface as defined by the surrounding residues in the wild type enzyme or is submerged below.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0269-2139
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
911-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7971953-Amino Acid Sequence, pubmed-meshheading:7971953-Aspartic Acid, pubmed-meshheading:7971953-Base Sequence, pubmed-meshheading:7971953-Binding Sites, pubmed-meshheading:7971953-Carboxypeptidases, pubmed-meshheading:7971953-Cathepsin A, pubmed-meshheading:7971953-Fungal Proteins, pubmed-meshheading:7971953-Glutamic Acid, pubmed-meshheading:7971953-Hydrogen-Ion Concentration, pubmed-meshheading:7971953-Models, Molecular, pubmed-meshheading:7971953-Molecular Sequence Data, pubmed-meshheading:7971953-Mutagenesis, Site-Directed, pubmed-meshheading:7971953-Protein Conformation, pubmed-meshheading:7971953-Protein Denaturation, pubmed-meshheading:7971953-Saccharomyces cerevisiae, pubmed-meshheading:7971953-Saccharomyces cerevisiae Proteins, pubmed-meshheading:7971953-Structure-Activity Relationship, pubmed-meshheading:7971953-Substrate Specificity
pubmed:year
1994
pubmed:articleTitle
Effects of introduced aspartic and glutamic acid residues on the P'1 substrate specificity, pH dependence and stability of carboxypeptidase Y.
pubmed:affiliation
Carlsberg Laboratory, Department of Chemistry, Copenhagen, Denmark.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't