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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1989-2-14
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pubmed:abstractText |
The amino acid sequence for the two subunits of the glutamate synthase of Escherichia coli K-12 was compared to the protein sequences compiled in the National Biomedical Research Foundation databank. Similarities were detected between the small glutamate synthase subunit and three members of the flavin-containing pyridine nucleotide-disulphide oxidoreductase superfamily, and also with three members of a lactate dehydrogenase family. Two segments in this glutamate synthase subunit showed similarity to regions previously proposed as part of dinucleotide-binding sites in some members of these two families. Similarity can be extended if the predicted secondary structure is considered. Based on these data, residues 148-260 and 289-409 in the small GOGAT subunit are proposed as dinucleotide-binding regions. Comparison of the amino acid sequence of the large glutamate synthase subunit with the glutamine phosphoribosylamine:pyrophosphate phosphoribosyltransferases of B. subtilis and E. coli revealed a significant similarity between the amino termini of these three enzymes. In these last two amidotransferases, the glutamine-binding site has been located in their amino-terminal region. The comparison with a second group of glutamine amidotransferases did not show any significant global similarity with the large glutamate synthase subunit. However, this polypeptide contains a small segment that shares similarity with a 13-amino acid segment proposed as part of the glutamine-binding site in this second group of amidotransferases.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-Hydroxybenzoate-3-Monooxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamine,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Transaminases
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pubmed:status |
MEDLINE
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pubmed:issn |
0931-9506
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9-16
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2643092-4-Hydroxybenzoate-3-Monooxygenase,
pubmed-meshheading:2643092-Amino Acid Sequence,
pubmed-meshheading:2643092-Binding Sites,
pubmed-meshheading:2643092-Escherichia coli,
pubmed-meshheading:2643092-Glutamate Synthase,
pubmed-meshheading:2643092-Glutamine,
pubmed-meshheading:2643092-Information Systems,
pubmed-meshheading:2643092-Mathematical Computing,
pubmed-meshheading:2643092-Molecular Sequence Data,
pubmed-meshheading:2643092-Oxidoreductases,
pubmed-meshheading:2643092-Protein Conformation,
pubmed-meshheading:2643092-Transaminases
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pubmed:year |
1989
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pubmed:articleTitle |
Amino acid sequence analysis of the glutamate synthase enzyme from Escherichia coli K-12.
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pubmed:affiliation |
Departamento de Biología Molecular, Centro de Investigación sobre Ingeniería Genética y Biotecnología, Universidad Nacional Autónoma de México.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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