Purification and Characterization of Glycerol Dehydratase from Lactobacillus reuteri†
AUTOR(ES)
Talarico, Todd L.
RESUMO
A coenzyme B12-dependent glycerol dehydratase from Lactobacillus reuteri has been purified and characterized. The dehydratase has a molecular weight of approximately 200,000, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis yielded a single major band with a molecular weight of 52,000. Km values for substrates and coenzyme B12 were in the millimolar and the submicromolar range, respectively.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=184372Documentos Relacionados
- Utilization of Glycerol as a Hydrogen Acceptor by Lactobacillus reuteri: Purification of 1,3-Propanediol:NAD+ Oxidoreductase †
- Characterization of Reutericyclin Produced by Lactobacillus reuteri LTH2584
- Identification and Characterization of Coenzyme B12-Dependent Glycerol Dehydratase- and Diol Dehydratase-Encoding Genes from Metagenomic DNA Libraries Derived from Enrichment Cultures
- Purification and characterization of a dipeptidase from Lactobacillus sake.
- Chemical characterization of an antimicrobial substance produced by Lactobacillus reuteri.