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Stereochemistry of the reaction of the inhibitor ß-chloroalanine with mercaptoethanol, a ß-substitution reaction catalysed by an aminotransferase

journal contribution
posted on 2023-06-07, 23:47 authored by Benjamin Adams, Kenneth J M Beresford, Sheena M Whyte, Douglas W Young
L-Aspartate aminotransferase, a member of the a-family of PLP mediated enzymes, which normally catalyses transamination, has been used to catalyse the ß-substitution reaction of stereospecifically labelled samples of the enzyme inhibitor ß-chloro-L-alanine with 2-mercaptoethanol; the stereochemistry of the products was assigned by independent synthesis, showing that the abnormal substitution reaction proceeds with overall retention of stereochemistry, the usual stereochemical consequence of reactions catalysed by enzymes of the ß-family of PLP mediated enzymes which have low homology with enzymes of the a-family

History

Publication status

  • Published

Journal

Chemical Communications

Volume

7

Page range

619 - 620

ISBN

1359-7345

Department affiliated with

  • Chemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

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