Stereochemistry of reactions of the inhibitor/substrates L- and D-beta-chloroalanine with beta-mercaptoethanol catalysed by L-aspartate aminotransferase and D-amino acid aminotransferase respectively.
Two members of the alpha-family of PLP-dependent enzymes, L-aspartate aminotransferase and D-amino acid aminotransferase, have been shown to catalyse beta-substitution of L- and D-beta-chloroalanine respectively with beta-mercaptoethanol, reactions typical of the beta-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 beta-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 beta-chloroalanine is the substrate.
Adams
Benjamin
B
Department of Chemistry, University of Sussex, Falmer, Brighton, UK BN1 9QJ.
Lowpetch
Kreingkrai
K
Thorndycroft
Faye
F
Whyte
Sheena M
SM
Young
Douglas W
DW
D001219:Aspartate Aminotransferases / Q000737:chemistry* / Q000378:metabolism; D008623:Mercaptoethanol / Q000737:chemistry*; D008956:Models, Chemical; D008968:Molecular Conformation; D015394:Molecular Structure; D015091:beta-Alanine / Q000031:analogs & derivatives* / Q000737:chemistry
D015091:beta-Alanine; C006977:3-chloroalanine; D008623:Mercaptoethanol; D001219:Aspartate Aminotransferases