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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

journal contribution
posted on 2023-06-08, 05:33 authored by Benjamin Adams, Kreingkrai Lowpetch, Faye Thornydycroft, Sheena M Whyte, Douglas W Young
Two members of the a-family of PLP-dependent enzymes, L-aspartate aminotransferase and D-amino acid aminotransferase, have been shown to catalyse ß-substitution of L- and D-ß-chloroalanine respectively with ß-mercaptoethanol, reactions typical of the ß-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 ß-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 ß-chloroalanine is the substrate

History

Publication status

  • Published

Journal

Organic and Biomolecular Chemistry

ISSN

1477-0520

Issue

18

Volume

3

Page range

3357-3364

Pages

8.0

Department affiliated with

  • Chemistry Publications

Notes

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.

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

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