Source:http://linkedlifedata.com/resource/pubmed/id/17573926
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2007-7-16
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pubmed:abstractText |
Recent data suggest that hexokinase KlHxk1 (Rag5) represents the only glucose-phosphorylating enzyme of Kluyveromyces lactis, which also is required for glucose signalling. Long-term growth studies of a K. lactis rag5 mutant, however, reveal slow growth on glucose, but no growth on fructose. Isolation of the permissive glucose-phosphorylating enzyme, mass spectrometric tryptic peptide analysis and determination of basic kinetic data identify a novel glucokinase (KlGlk1) encoded by ORF KLLA0C01,155g. In accordance with the growth characteristics of the rag5 mutant, KlGlk1 phosphorylates glucose, but fails to act on fructose as a sugar substrate. Multiple sequence alignment indicates the presence of at least one glucokinase gene in all sequenced yeast genomes.
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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
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pubmed:month |
Aug
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pubmed:issn |
1567-1356
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
683-92
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pubmed:meshHeading |
pubmed-meshheading:17573926-Amino Acid Sequence,
pubmed-meshheading:17573926-Fructose,
pubmed-meshheading:17573926-Fungal Proteins,
pubmed-meshheading:17573926-Gene Expression Regulation, Fungal,
pubmed-meshheading:17573926-Glucokinase,
pubmed-meshheading:17573926-Glucose,
pubmed-meshheading:17573926-Humans,
pubmed-meshheading:17573926-Kluyveromyces,
pubmed-meshheading:17573926-Molecular Sequence Data,
pubmed-meshheading:17573926-Phosphorylation,
pubmed-meshheading:17573926-Phylogeny,
pubmed-meshheading:17573926-Sequence Alignment,
pubmed-meshheading:17573926-Substrate Specificity
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pubmed:year |
2007
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pubmed:articleTitle |
Identification and characterization of a novel glucose-phosphorylating enzyme in Kluyveromyces lactis.
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pubmed:affiliation |
Technische Universität Dresden, Medizinische Fakultät Carl Gustav Carus, Institut für Physiologische Chemie, Dresden, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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