Linked Life Data

5263013

Source:http://linkedlifedata.com/resource/pubmed/id/5263013

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1970-3-14
pubmed:abstractText
Several features of carboxypeptidase A (CPA) which were previously established by the X-ray diffraction structure studies have now been confirmed by the chemical sequence analysis. These results include the number (307) of amino acid residues in CPA(alpha), the identities of the residues (Arg 145, Glu 270, and Tyr 248) shown by the X-ray study to be involved in substrate binding and catalysis, and the existence of a disulfide bond. The Zn ligands, shown by the X-ray study to be residues 69, 72, and 196 and identified as His, Glx, and either Glx or Lys, are proved by the chemical sequence to be His, Glu, and His, respectively. No change is required in our previous mechanistic deductions, which are here extended to include a specific mechanism of activation of the substrate by a net charge on the metal ion, which suffers a change in local dielectric constant when it is covered by a substrate.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
28-35
pubmed:dateRevised
2010-9-13
pubmed:meshHeading
pubmed:year
1969
pubmed:articleTitle
The structure of carboxypeptidase A. IX. The x-ray diffraction results in the light of the chemical sequence.
pubmed:publicationType
Journal Article