Elsevier

Tetrahedron Letters

Volume 42, Issue 15, 9 April 2001, Pages 2775-2777
Tetrahedron Letters

Selective racemization in preference to transamination catalyzed by pyridoxal enzyme analogs

https://doi.org/10.1016/S0040-4039(01)00329-XGet rights and content

Abstract

The racemase activity of pyridoxal enzyme models is selectively increased in preference to transaminase activity by the attachment of rigid basic groups.

The racemase activity of pyridoxal enzyme models is selectively increased in preference to transaminase activity by the attachment of rigid basic groups.

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Acknowledgements

This work has been supported by the NIH and the NSF.

References (10)

  • E. Fasella et al.

    Bioorg. Med. Chem.

    (1999)
  • J. Olivard et al.

    J. Biol. Chem.

    (1952)
  • A.E. Martell

    Acc. Chem. Res.

    (1989)
  • R. Breslow

    Acc. Chem. Res.

    (1995)
  • J. Chmielewski et al.

    Heterocycles

    (1987)
There are more references available in the full text version of this article.

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