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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1995-3-20
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alanine Transaminase,
http://linkedlifedata.com/resource/pubmed/chemical/Apoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartate Aminotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/D-Alanine Transaminase,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridoxal,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridoxamine,
http://linkedlifedata.com/resource/pubmed/chemical/Transaminases
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0968-0896
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
605-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7858965-Alanine Transaminase,
pubmed-meshheading:7858965-Animals,
pubmed-meshheading:7858965-Apoenzymes,
pubmed-meshheading:7858965-Aspartate Aminotransferases,
pubmed-meshheading:7858965-Bacillus,
pubmed-meshheading:7858965-D-Alanine Transaminase,
pubmed-meshheading:7858965-Escherichia coli,
pubmed-meshheading:7858965-Myocardium,
pubmed-meshheading:7858965-Pyridoxal,
pubmed-meshheading:7858965-Pyridoxamine,
pubmed-meshheading:7858965-Stereoisomerism,
pubmed-meshheading:7858965-Substrate Specificity,
pubmed-meshheading:7858965-Swine,
pubmed-meshheading:7858965-Transaminases
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pubmed:year |
1994
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pubmed:articleTitle |
A simple method for determination of stereospecificity of aminotransferases for C-4' hydrogen transfer of the coenzyme.
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pubmed:affiliation |
Department of Applied Chemistry and Biotechnology, Yamanashi University, Japan.
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pubmed:publicationType |
Journal Article
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