Linked Life Data

8641475

Source:http://linkedlifedata.com/resource/pubmed/id/8641475

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1996-7-12
pubmed:abstractText
Upon trypsinolysis, the 18 C-terminal residues of Escherichia coli peptide deformylase were removed but the resulting form exhibited full activity. Moreover, a mutant fms gene encoding the first 145 out of the 168 residues of the enzyme was able to complement a fms(Ts) strain and exhibited full activity. Upon progressive truncation up to residue 139, both activity and stability decreased up to complete inactivation. Mutagenesis of residues of the 138-145 region highlights the importance of Leu-141 and Phe-142. N-Terminal deletions were also carried out. Beyond two residues off, the enzyme showed a dramatic instability. Finally, NMR and thermostability studies of the full-length enzyme and comparison to the 1-147 form strongly suggest that the dispensable residues are disordered in solution.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
385
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
91-5
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
The C-terminal domain of peptide deformylase is disordered and dispensable for activity.
pubmed:affiliation
Laboratoire de Biochimie, Unité de Recherche Associée No. 1970 du Centre National de la Recherche Scientifique, Ecole Polytechnique, Palaiseau, France.titi@botrytis.polytechnique.fr
pubmed:publicationType
Journal Article