Characterization of the recombinant (R )- and (S )-hydroxypropyl-coenzyme M dehydrogenases: A case study to augment the teaching of enzyme kinetics and stereoselectivity
Author:
Affiliation:
1. Department of Chemistry and Biochemistry; California State University-Chico; Chico California 95929
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/bmb.21202/fullpdf
Reference14 articles.
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2. Purification to homogeneity and reconstitution of the individual components of the epoxide carboxylase multiprotein enzyme complex from Xanthobacter strain Py2;Allen;J. Biol. Chem.,1997
3. Two short-chain dehydrogenases confer stereoselectivity for enantiomers of epoxypropane in the multiprotein epoxide carboxylating systems of Xanthobacter strain Py2 and Nocardia corallina B276;Allen;Biochemistry,1999
4. A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation;Allen;Proc. Natl. Acad. Sci. U. S. A.,1999
5. Aliphatic epoxide carboxylation;Ensign;Annu. Rev. Biochem.,2003
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