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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1996-10-24
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pubmed:abstractText |
Glucosamine 6-phosphate deaminase from Escherichia coli is an allosteric hexameric enzyme which catalyzes the reversible conversion of D-glucosamine 6-phosphate into D-fructose 6-phosphate and ammonium ion and is activated by N-acetyl-D-glucosamine 6-phosphate. Mechanistically, it belongs to the group of aldoseketose isomerases, but its reaction also accomplishes a simultaneous amination/deamination. The determination of the structure of this protein provides fundamental knowledge for understanding its mode of action and the nature of allosteric conformational changes that regulate its function.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Aldose-Ketose Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrate Epimerases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Fructosephosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose-6-Phosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosephosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Sorbitol,
http://linkedlifedata.com/resource/pubmed/chemical/Sugar Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/fructose-6-phosphate,
http://linkedlifedata.com/resource/pubmed/chemical/glucosamine 6-phosphate,
http://linkedlifedata.com/resource/pubmed/chemical/glucosamine-6-phosphate isomerase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1323-32
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:8747459-Aldose-Ketose Isomerases,
pubmed-meshheading:8747459-Allosteric Regulation,
pubmed-meshheading:8747459-Bacterial Proteins,
pubmed-meshheading:8747459-Binding Sites,
pubmed-meshheading:8747459-Carbohydrate Epimerases,
pubmed-meshheading:8747459-Catalysis,
pubmed-meshheading:8747459-Crystallography, X-Ray,
pubmed-meshheading:8747459-Enzyme Inhibitors,
pubmed-meshheading:8747459-Escherichia coli,
pubmed-meshheading:8747459-Fructosephosphates,
pubmed-meshheading:8747459-Glucosamine,
pubmed-meshheading:8747459-Glucose-6-Phosphate,
pubmed-meshheading:8747459-Glucosephosphates,
pubmed-meshheading:8747459-Macromolecular Substances,
pubmed-meshheading:8747459-Models, Molecular,
pubmed-meshheading:8747459-NAD,
pubmed-meshheading:8747459-Phosphates,
pubmed-meshheading:8747459-Protein Conformation,
pubmed-meshheading:8747459-Sorbitol,
pubmed-meshheading:8747459-Sugar Phosphates
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pubmed:year |
1995
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pubmed:articleTitle |
Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution.
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pubmed:affiliation |
Instituto de Fisica de São Carlos, Universidade de São Paulo, Brazil.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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