rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
17
|
pubmed:dateCreated |
1988-7-13
|
pubmed:abstractText |
Escherichia coli grown in limited methionine and excess norleucine media accumulate cyanogen bromide-resistant species of proteins after the methionine supply is exhausted. Bacteria, transformed by recombinant plasmid pIPD37 carrying the adk gene and grown under limiting methionine and excess norleucine, synthesize 16-20% of adenylate kinase molecules having all 6 methionine residues replaced by norleucine. Species showing only partial replacement of methionine residues by norleucine are identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis after cyanogen bromide treatment of pure enzyme. Norleucine-substituted adenylate kinase shows structural and catalytic properties similar to the wild-type protein as indicated by circular dichroism spectroscopy and kinetic experiments but exhibits a much higher resistance to hydrogen peroxide inactivation under denaturing conditions.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0021-9258
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
263
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
8204-9
|
pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2836418-Adenosine Monophosphate,
pubmed-meshheading:2836418-Adenylate Kinase,
pubmed-meshheading:2836418-Amino Acids,
pubmed-meshheading:2836418-Aminocaproic Acids,
pubmed-meshheading:2836418-Circular Dichroism,
pubmed-meshheading:2836418-Cyanogen Bromide,
pubmed-meshheading:2836418-Escherichia coli,
pubmed-meshheading:2836418-Hydrogen Peroxide,
pubmed-meshheading:2836418-Kinetics,
pubmed-meshheading:2836418-Methionine,
pubmed-meshheading:2836418-Norleucine,
pubmed-meshheading:2836418-Phosphotransferases,
pubmed-meshheading:2836418-Structure-Activity Relationship
|
pubmed:year |
1988
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pubmed:articleTitle |
Conservative replacement of methionine by norleucine in Escherichia coli adenylate kinase.
|
pubmed:affiliation |
Unité de Chimie des Protéines, Institut Pasteur, Paris, France.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|