Linked Life Data

8386544

Source:http://linkedlifedata.com/resource/pubmed/id/8386544

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1993-5-25
pubmed:abstractText
The preparation and biophysical characterization of a mutant of superoxide dismutase in which the native Thr 137 has been substituted with a positive Arg residue are reported. Thr 137 forms, together with Arg 143, a bottleneck at the entrance to the active-site Cu ion. The geometry of the Cu ligands shows only minor changes after the above substitution. However, the enzymatic activity of the Arg 137 mutant is smaller than that of the wild type at physiological ionic strength and approaches that of wild type in the limit of zero ionic strength. The binding constant of the anion N3-, which had previously been shown to be a good probe of the O2- substrate, is increased about 20-fold in the mutant with respect to the value found in the wild type. These results are discussed on the bases of the whole charge of the cavity and the possible change in the conformation of the active-site channel.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4384-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Investigation of a new Cu,Zn superoxide dismutase mutant: the Thr-->Arg 137 derivative.
pubmed:affiliation
Department of Chemistry, University of Florence, Italy.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.