Title : Enzymes involved in the glycidaldehyde (2,3-epoxy-propanal) oxidation step in the kinetic resolution of racemic glycidol (2,3-epoxy-1-propanol) by Acetobacter pasteurianus.

Pub. Date : 2001 Feb 1

PMID : 11166817






3 Functional Relationships(s)
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1 In addition, a preparation exhibiting dye-linked aldehyde dehydrogenase activity for acetaldehyde, most probably originating from molybdohemoprotein aldehyde dehydrogenase (ALDH), which has been described for other Acetic acid bacteria, oxidised glycidaldehyde as well with a preference for the (R)-enantiomer, the selectivity quantified by an enantiomeric ratio (E) value of 7. Acetic Acid D719_p1008 Acetobacter pasteurianus
2 In addition, a preparation exhibiting dye-linked aldehyde dehydrogenase activity for acetaldehyde, most probably originating from molybdohemoprotein aldehyde dehydrogenase (ALDH), which has been described for other Acetic acid bacteria, oxidised glycidaldehyde as well with a preference for the (R)-enantiomer, the selectivity quantified by an enantiomeric ratio (E) value of 7. Acetic Acid D719_p1008 Acetobacter pasteurianus
3 In addition, a preparation exhibiting dye-linked aldehyde dehydrogenase activity for acetaldehyde, most probably originating from molybdohemoprotein aldehyde dehydrogenase (ALDH), which has been described for other Acetic acid bacteria, oxidised glycidaldehyde as well with a preference for the (R)-enantiomer, the selectivity quantified by an enantiomeric ratio (E) value of 7. Acetic Acid D719_p1008 Acetobacter pasteurianus