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

Adams, Benjamin, Lowpetch, Kreingkrai, Thornydycroft, Faye, Whyte, Sheena M and Young, Douglas W (2005) 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. Organic and Biomolecular Chemistry, 3 (18). pp. 3357-3364. ISSN 1477-0520

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Abstract

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

Item Type: Article
Additional Information: DWY directed the work and is corresponding author and all authors are from Sussex. First demonstration that enzymes of the alpha-PLP subgroup can be induced to behave with the overall stereochemistry of the beta-enzyme subgroup. The stereochemistry of the antibacterial drugs by their target enzymes is also defined.
Schools and Departments: School of Life Sciences > Chemistry
Depositing User: EPrints Services
Date Deposited: 06 Feb 2012 20:14
Last Modified: 27 Mar 2012 09:23
URI: http://sro.sussex.ac.uk/id/eprint/24871
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