Linked Life Data

8098056

Source:http://linkedlifedata.com/resource/pubmed/id/8098056

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-6-10
pubmed:abstractText
Negatively charged glutamic acid residues at positions 132 and 133 in human Cu2Zn2SOD are located at the entrance to the active site cavity and affect electrostatic interactions with the negatively charged substrate. The mutants in which these residues have been neutralized separately and together by conversion to glutamine residues or changed to a positive group on position 133 have been characterized through a variety of biophysical techniques. The structure around the metal ions, as monitored by spectroscopic measurements, is the same in the mutants and native enzyme. The mutants have been characterized with respect to the affinity for the anion N3-. The mutants have larger affinity for azide than the WT, as a result of the removal of one or two negative charges or of the introduction of a positive group. The pattern of the azide affinity constants parallels that of the rate of O2- dismutation. The substitution of the negative Glu-133 with a positive group does not induce a larger increase in the affinity as well as in the catalytic rates with respect to its neutralization. These patterns cannot, therefore, be rationalized only in terms of electrostatic interactions. The behavior of the mutants towards the substrate (O2-) and substrate analogue (N3-) is discussed on the basis of theoretical predictions available in the literature.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0162-0134
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
89-100
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
An essential role for the conserved Glu-133 in the anion interaction with superoxide dismutase.
pubmed:affiliation
Department of Chemistry, University of Florence, Italy.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't