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rdf:type |
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|
lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1998-7-6
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pubmed:abstractText |
Escherichia coli biotin carboxylase was affinity labeled with adenosine diphosphopyridoxal to identify its ATP binding site. Lysyl endopeptidase digestion of the modified protein, followed by high performance liquid chromatography separation and amino acid sequencing allowed to identify lysine-238 to be the site of modification. Site-directed mutagenesis of this residue into alanine, arginine or glutamine resulted in mutants with much decreased activity. Lysine-238 seems to interact with the gamma-phosphate group of ATP but is not involved in catalysis.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-5793
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:day |
15
|
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pubmed:volume |
427
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
377-80
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9637261-Adenosine Diphosphate,
pubmed-meshheading:9637261-Adenosine Triphosphate,
pubmed-meshheading:9637261-Affinity Labels,
pubmed-meshheading:9637261-Binding Sites,
pubmed-meshheading:9637261-Carbon-Nitrogen Ligases,
pubmed-meshheading:9637261-Escherichia coli,
pubmed-meshheading:9637261-Lysine,
pubmed-meshheading:9637261-Mutagenesis, Site-Directed,
pubmed-meshheading:9637261-Pyridoxal Phosphate,
pubmed-meshheading:9637261-Structure-Activity Relationship
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pubmed:year |
1998
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|
pubmed:articleTitle |
Identification of lysine-238 of Escherichia coli biotin carboxylase as an ATP-binding residue.
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pubmed:affiliation |
Department of Biochemical Engineering and Science, Kyushu Institute of Technology, Iizuka, Japan. kazuta@bse.kyutech.ac.jp
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pubmed:publicationType |
Journal Article,
Comparative Study
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