Literature DB >> 2121281

Determination of hydride transfer stereospecificity of NADH-dependent alcohol-aldehyde/ketone oxidoreductase from Sulfolobus solfataricus.

A Trincone1, L Lama, R Rella, S D'Auria, C A Raia, B Nicolaus.   

Abstract

This paper describes the determination of stereospecificity of hydride transfer reaction of an alcohol dehydrogenase isolated from the archaebacterium Sulfolobus solfataricus. The 1H-NMR and EI-MS data indicate that the enzyme transfers the pro-R hydrogen from coenzyme to substrate and is therefore an A-specific dehydrogenase.

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Year:  1990        PMID: 2121281     DOI: 10.1016/0167-4838(90)90127-2

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  1 in total

1.  DSD--an integrated, web-accessible database of Dehydrogenase Enzyme Stereospecificities.

Authors:  Christopher P Toseland; Helen M McSparron; Darren R Flower
Journal:  BMC Bioinformatics       Date:  2005-11-30       Impact factor: 3.169

  1 in total

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