New enzymes for biotransformations: microbial alkyl sulfatases displaying stereo- and enantioselectivity.
The majority of hydrolytic enzymes used in white biotechnology for the production of non-natural compounds--such as carboxyl ester hydrolases, lipases and proteases--show a certain preference for a given enantiomer. However, they are unable to alter the stereochemistry of the substrate during catalysis with respect to inversion or retention of configuration. The latter can be achieved by (alkyl) sulfatases, which can be employed for the enantio-convergent transformation of racemic sulfate esters into a single stereoisomeric secondary alcohol, with a theoretical yield of 100%. This is a major improvement over traditional kinetic resolution processes, which yield both enantiomers, each at 50%.
Gadler
Petra
P
Department of Chemistry, Organic & Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, A-8010 Graz, Austria.
Faber
Kurt
K
D001419:Bacteria / Q000201:enzymology; D001709:Biotechnology / Q000379:methods; D001711:Biotransformation; D006868:Hydrolysis; D007700:Kinetics; D011487:Protein Conformation; D019998:Racemases and Epimerases / Q000737:chemistry / Q000378:metabolism*; D013237:Stereoisomerism; D013379:Substrate Specificity; D013429:Sulfatases / Q000737:chemistry / Q000378:metabolism*
D013429:Sulfatases; C019244:alkylsulfatase; D019998:Racemases and Epimerases