| pubmed-article:7858965 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7858965 | lifeskim:mentions | umls-concept:C0025663 | lld:lifeskim |
| pubmed-article:7858965 | lifeskim:mentions | umls-concept:C0002594 | lld:lifeskim |
| pubmed-article:7858965 | lifeskim:mentions | umls-concept:C0009235 | lld:lifeskim |
| pubmed-article:7858965 | lifeskim:mentions | umls-concept:C0020275 | lld:lifeskim |
| pubmed-article:7858965 | lifeskim:mentions | umls-concept:C0680730 | lld:lifeskim |
| pubmed-article:7858965 | lifeskim:mentions | umls-concept:C1705822 | lld:lifeskim |
| pubmed-article:7858965 | lifeskim:mentions | umls-concept:C0348011 | lld:lifeskim |
| pubmed-article:7858965 | lifeskim:mentions | umls-concept:C1148554 | lld:lifeskim |
| pubmed-article:7858965 | lifeskim:mentions | umls-concept:C0205352 | lld:lifeskim |
| pubmed-article:7858965 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:7858965 | pubmed:dateCreated | 1995-3-20 | lld:pubmed |
| pubmed-article:7858965 | pubmed:abstractText | A simple method was established for determination of the stereospecificity of C-4' hydrogen transfer of the coenzymes (pyridoxal and pyridoxamine). The method is based on the findings that aspartate aminotransferase of pig heart and D-amino acid aminotransferase of Bacillus sp. YM-1 catalyze the abstraction of the pro-S and pro-R proton at C-4' of pyridoxamine, respectively. Pyridoxal is a poor coenzyme, but readily released from the enzyme. It reacts in 3H2O with a substrate amino acid and an apo-aminotransferase whose stereospecificity for C-4' hydrogen transfer is to be determined. The resultant pyridoxamine which is tritiated at C-4' is incubated with an apo form of aspartate aminotransferase or D-amino acid aminotransferase and a substrate, alpha-keto acid. The stereospecificity for the C-4' hydrogen transfer examined is determined by measurement of radioactivity retained in the pyridoxal formed. We showed by means of this method that C-4' hydrogen transfer of coenzyme occurs on the si face of the external Schiff base in the transamination reactions of two aspartate aminotransferases of Bacillus sp. YM-2 and Escherichia coli, and aromatic amino acid aminotransferase of E. coli. | lld:pubmed |
| pubmed-article:7858965 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7858965 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7858965 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7858965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7858965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7858965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7858965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7858965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7858965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7858965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7858965 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7858965 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:7858965 | pubmed:issn | 0968-0896 | lld:pubmed |
| pubmed-article:7858965 | pubmed:author | pubmed-author:SodaKK | lld:pubmed |
| pubmed-article:7858965 | pubmed:author | pubmed-author:NishimuraKK | lld:pubmed |
| pubmed-article:7858965 | pubmed:author | pubmed-author:YoshimuraTT | lld:pubmed |
| pubmed-article:7858965 | pubmed:author | pubmed-author:ItoJJ | lld:pubmed |
| pubmed-article:7858965 | pubmed:author | pubmed-author:EsakiNN | lld:pubmed |
| pubmed-article:7858965 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7858965 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:7858965 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7858965 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7858965 | pubmed:pagination | 605-7 | lld:pubmed |
| pubmed-article:7858965 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:7858965 | pubmed:meshHeading | pubmed-meshheading:7858965-... | lld:pubmed |
| pubmed-article:7858965 | pubmed:meshHeading | pubmed-meshheading:7858965-... | lld:pubmed |
| pubmed-article:7858965 | pubmed:meshHeading | pubmed-meshheading:7858965-... | lld:pubmed |
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| pubmed-article:7858965 | pubmed:meshHeading | pubmed-meshheading:7858965-... | lld:pubmed |
| pubmed-article:7858965 | pubmed:meshHeading | pubmed-meshheading:7858965-... | lld:pubmed |
| pubmed-article:7858965 | pubmed:meshHeading | pubmed-meshheading:7858965-... | lld:pubmed |
| pubmed-article:7858965 | pubmed:meshHeading | pubmed-meshheading:7858965-... | lld:pubmed |
| pubmed-article:7858965 | pubmed:meshHeading | pubmed-meshheading:7858965-... | lld:pubmed |
| pubmed-article:7858965 | pubmed:meshHeading | pubmed-meshheading:7858965-... | lld:pubmed |
| pubmed-article:7858965 | pubmed:meshHeading | pubmed-meshheading:7858965-... | lld:pubmed |
| pubmed-article:7858965 | pubmed:meshHeading | pubmed-meshheading:7858965-... | lld:pubmed |
| pubmed-article:7858965 | pubmed:meshHeading | pubmed-meshheading:7858965-... | lld:pubmed |
| pubmed-article:7858965 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7858965 | pubmed:articleTitle | A simple method for determination of stereospecificity of aminotransferases for C-4' hydrogen transfer of the coenzyme. | lld:pubmed |
| pubmed-article:7858965 | pubmed:affiliation | Department of Applied Chemistry and Biotechnology, Yamanashi University, Japan. | lld:pubmed |
| pubmed-article:7858965 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:945553 | entrezgene:pubmed | pubmed-article:7858965 | lld:entrezgene |
| entrez-gene:948563 | entrezgene:pubmed | pubmed-article:7858965 | lld:entrezgene |
