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http://purl.uniprot.org/citations/1783373http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1783373http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1783373http://www.w3.org/2000/01/rdf-schema#comment"We have amplified and sequenced the complete coding region of bovine hexokinase isoenzyme 1 (HK1) from brain RNA with PCR primers selected for sequence conservation. The sequence information was analyzed to evaluate the evolutionary and structure-function relationships among the mammalian and yeast HK isoenzymes. Structure to function analysis identified an unduplicated, invariant N-terminal domain involved in HK1 outer mitochondrial membrane targeting, as well as putative carbohydrate and nucleotide-binding sites in the regulatory and catalytic halves of HK1 essential to enzyme function. The ATP-binding site in the catalytic half of the HK1 protein resembles nucleotide-binding regions from protein kinases, with the single amino acid replacement (lysine to glutamate) in the ATP-binding site of the amino half explaining the loss of HK1 catalytic function in the regulatory domain. Sequence comparisons suggest that the 50-kDa mammalian and yeast glucokinases arose separately in evolution. In addition to providing valuable phylogenetic and structure-function insights, this work provides an efficient strategy for rapid cloning and sequencing of the coding regions for other HKs and related proteins."xsd:string
http://purl.uniprot.org/citations/1783373http://purl.org/dc/terms/identifier"doi:10.1016/0888-7543(91)90027-c"xsd:string
http://purl.uniprot.org/citations/1783373http://purl.org/dc/terms/identifier"doi:10.1016/0888-7543(91)90027-c"xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/author"Wheeler D.A."xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/author"Wheeler D.A."xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/author"Adams V."xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/author"Adams V."xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/author"Griffin L.D."xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/author"Griffin L.D."xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/author"Gelb B.D."xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/author"Gelb B.D."xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/author"Davison D."xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/author"Davison D."xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/author"McCabe E.R."xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/author"McCabe E.R."xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/name"Genomics"xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/name"Genomics"xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/pages"1014-1024"xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/pages"1014-1024"xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/title"Mammalian hexokinase 1: evolutionary conservation and structure to function analysis."xsd:string
http://purl.uniprot.org/citations/1783373http://purl.uniprot.org/core/title"Mammalian hexokinase 1: evolutionary conservation and structure to function analysis."xsd:string