Stereochemistry of the reaction of the inhibitor beta-chloroalanine with mercaptoethanol, a beta-substitution reaction catalysed by an aminotransferase
B. Adams et al., Stereochemistry of the reaction of the inhibitor beta-chloroalanine with mercaptoethanol, a beta-substitution reaction catalysed by an aminotransferase, CHEM COMMUN, (7), 2000, pp. 619-620
L-Aspartate aminotransferase, a member of the alpha-family of PLP mediated
enzymes, which normally catalyses transamination, has been used to catalyse
the beta-substitution reaction of stereospecifically labelled samples of t
he enzyme inhibitor beta-chloro-L-alanine with 2-mercaptoethanol; the stere
ochemistry of the products was assigned by independent synthesis, showing t
hat the abnormal substitution reaction proceeds with overall retention of s
tereochemistry, the usual stereochemical consequence of reactions catalysed
by enzymes of the beta-family of PLP mediated enzymes which have low homol
ogy with enzymes of the alpha-family.