868077-83-2Relevant articles and documents
Stereochemistry of the reaction of the inhibitor β-chloroalanine with mercaptoethanol, a β-substitution reaction catalysed by an aminotransferase
Adams, Benjamin,Beresford, Kenneth J. M.,Whyte, Sheena M.,Young, Douglas W.
, p. 619 - 620 (2000)
L-Aspartate aminotransferase, a member of the α-family of PLP mediated enzymes, which normally catalyses transamination, has been used to catalyse the β-substitution reaction of stereospecifically labelled samples of the enzyme inhibitor β-chloro-L-alanin
Stereochemistry of reactions of the inhibitor/substrates L- And D-β-chloroalanine with β-mercaptoethanol catalysed by L-aspartate aminotransferase and D-amino acid aminotransferase respectively
Adams, Benjamin,Lowpetch, Kreingkrai,Thorndycroft, Faye,Whyte, Sheena M.,Young, Douglas W.
, p. 3357 - 3364 (2007/10/03)
Two members of the α-family of PLP-dependent enzymes, L-aspartate aminotransferase and D-amino acid aminotransferase, have been shown to catalyse β-substitution of L- and D-β-chloroalanine respectively with β-mercaptoethanol, reactions typical of the β-family of PLP-dependent enzymes. The reaction catalysed by L-aspartate aminotransferase has been shown to occur with retention of stereochemistry, a typical outcome for reactions catalysed by β-family enzymes. There are also indications that the reaction catalysed by D-amino acid aminotransferase may involve retention of stereochemistry. Both enzymes have been shown to catalyse exchange at C-3 when the appropriate enantiomer of β-chloroalanine is the substrate. The Royal Society of Chemistry 2005.
