Substrate specificity and stereospecificity of nicotinamide adenine dinucleotide-linked alcohol dehydrogenases from methanol-grown yeasts.
AUTOR(ES)
Hou, C T
RESUMO
Nicotine adenine dinucleotide-linked primary alcohol dehydrogenase and a newly discovered secondary alcohol dehydrogenase coexist in most strains of methanol-grown yeasts. Alcohol dehydrogenases from methanol-grown yeasts oxidize (--)-2-butanol preferentially over its (+) enantiomorph. This is substantially different from alcohol dehydrogenases from bakers' yeast and horse liver.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=243783Documentos Relacionados
- FLAVINE ADENINE DINUCLEOTIDE-LINKED MALIC DEHYDROGENASE FROM ACETOBACTER XYLINUM
- The Effect of Exogenous Nicotinamide Adenine Dinucleotide on the Oxidation of Nicotinamide Adenine Dinucleotide-linked Substrates by Isolated Plant Mitochondria 1
- Ribulose bisphosphate carboxylase from methanol-grown Paracoccus denitrificans.
- Ferrous-activated Nicotinamide Adenine Dinucleotide-linked Dehydrogenase from a Mutant of Escherichia coli Capable of Growth on 1,2-Propanediol
- Occurrence of squalene in methanol-grown bacteria.
