pubmed-article:8407879 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8407879 | lifeskim:mentions | umls-concept:C0079870 | lld:lifeskim |
pubmed-article:8407879 | lifeskim:mentions | umls-concept:C0318211 | lld:lifeskim |
pubmed-article:8407879 | lifeskim:mentions | umls-concept:C0441635 | lld:lifeskim |
pubmed-article:8407879 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
pubmed-article:8407879 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
pubmed-article:8407879 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:8407879 | lifeskim:mentions | umls-concept:C0070637 | lld:lifeskim |
pubmed-article:8407879 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:8407879 | pubmed:dateCreated | 1993-11-12 | lld:pubmed |
pubmed-article:8407879 | pubmed:abstractText | Phenylalanine dehydrogenase from Thermoactinomyces intermedius and leucine dehydrogenase from Bacillus stearothermophilus show a 59% sequence similarity in their substrate-binding domains, although their substrate specificities are different. We prepared a phenylalanine dehydrogenase mutant enzyme whose inherent hexapeptide segment (124F-V-H-A-A-129R) in the substrate-binding domain was replaced by the corresponding part of leucine dehydrogenase (M-D-I-I-Y-Q) in order to investigate the mechanism of substrate recognition by phenylalanine dehydrogenase. The catalytic efficiencies (kcat/Km) of the mutant enzyme with aliphatic amino acids and aliphatic keto acids as substrates were 0.5 to 2% of those of the wild-type enzyme. In contrast, the efficiencies for L-phenylalanine and phenylpyruvate decreased to 0.008 and 0.035% of those of the wild-type enzyme, respectively. These results suggest that the hexapeptide segment plays an important role in the substrate recognition by phenylalanine dehydrogenase. | lld:pubmed |
pubmed-article:8407879 | pubmed:language | eng | lld:pubmed |
pubmed-article:8407879 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8407879 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8407879 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8407879 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8407879 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8407879 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8407879 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8407879 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8407879 | pubmed:month | Jul | lld:pubmed |
pubmed-article:8407879 | pubmed:issn | 0021-924X | lld:pubmed |
pubmed-article:8407879 | pubmed:author | pubmed-author:SodaKK | lld:pubmed |
pubmed-article:8407879 | pubmed:author | pubmed-author:YoshimuraTT | lld:pubmed |
pubmed-article:8407879 | pubmed:author | pubmed-author:KataokaKK | lld:pubmed |
pubmed-article:8407879 | pubmed:author | pubmed-author:TakadaHH | lld:pubmed |
pubmed-article:8407879 | pubmed:author | pubmed-author:OhshimaTT | lld:pubmed |
pubmed-article:8407879 | pubmed:author | pubmed-author:EsakiNN | lld:pubmed |
pubmed-article:8407879 | pubmed:author | pubmed-author:FuruyoshiSS | lld:pubmed |
pubmed-article:8407879 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8407879 | pubmed:volume | 114 | lld:pubmed |
pubmed-article:8407879 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8407879 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8407879 | pubmed:pagination | 69-75 | lld:pubmed |
pubmed-article:8407879 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:meshHeading | pubmed-meshheading:8407879-... | lld:pubmed |
pubmed-article:8407879 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8407879 | pubmed:articleTitle | Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine dehydrogenase from Thermoactinomyces intermedius. | lld:pubmed |
pubmed-article:8407879 | pubmed:affiliation | Laboratory of Microbial Biochemistry, Kyoto University. | lld:pubmed |
pubmed-article:8407879 | pubmed:publicationType | Journal Article | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8407879 | lld:pubmed |