Linked Life Data

9665853

Source:http://linkedlifedata.com/resource/pubmed/id/9665853

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-8-7
pubmed:abstractText
Previous work indicated that peptide deformylase behaves as a metalloenzyme since the Escherichia coli enzyme was shown to copurify with a zinc ion. The present study establishes that nickel:enzyme complexes can also be isolated provided that nickel salts were added in the buffers throughout the purification. Similar results were obtained with the deformylases from Thermus thermophilus and Bacillus stearothermophilus. As a result of nickel binding, the catalytic efficiencies of peptide deformylases increased by two to three orders of magnitude with respect to those of the forms previously characterized. Using the model substrate N-formyl-Met-Ala-Ser, kcat/Km values of 5.4, 1.2 and 25 10(4)M-1s-1 could be obtained for the E. coli, T. thermophilus and B. stearothermophilus enzymes, respectively. This value satisfyingly accounts for the deformylation turnover required in the cell. In vitro characterization of the E. coli enzyme shows that zinc can readily substitute for the bound nickel with the catalytic efficiency decreasing to 80 M-1s-1 in turn. Conversely, the activity of the zinc-containing protein can be significantly improved by addition of nickel to the enzymatic assay.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 1998 Academic Press.
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
515-23
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Control of peptide deformylase activity by metal cations.
pubmed:affiliation
Unité Mixte de Recherche, Ecole Polytechnique, Palaiseau cedex, F-91128, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't