Linked Life Data

9821960

Source:http://linkedlifedata.com/resource/pubmed/id/9821960

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1998-12-2
pubmed:abstractText
The amino acid residue Asn141 of the restriction endonuclease EcoRI was proposed to make three hydrogen bonds to both adenine residues within the recognition sequence -GAATTC-. We have mutated Asn141 to alanine, aspartate, serine, and tyrosine. Only the serine mutant is active under normal buffer conditions although 1000-fold less than wild-type EcoRI. The alanine and aspartate mutants can be activated by Mn2+. At acidic pH the latter mutant becomes even more active than the wild-type enzyme in the presence of Mn2+. We conclude that Asn141 is essential for DNA recognition and that serine can partly substitute it.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
438
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
66-70
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Asn141 is essential for DNA recognition by EcoRI restriction endonuclease.
pubmed:affiliation
Institut für Pathologie, GSG-Forschungszentrum für Umwelt und Gesundheit GmbH, Oberschleissheim, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't