Mimics of Transaminase Enzymes

R. Breslow, A. W. Czarnik, M. Lauer, R. Leppkes, J. Winkler, S. Zimmerman

Research output: Contribution to journalArticlepeer-review

Abstract

Pyridoxamine has been attached to the primary side and to the secondary side of β-cyclodextrin; the resulting compounds convert α-keto acids to amino acids with substrate selectivity and some stereoselectivity. Pyridoxamine has also been attached to a synthetic macrocycle; the attached binding group showed substrate selectivity. Chains carrying catalytic basic groups have been attached to pyridoxamine; appropriate systems catalyze the prototropic rearrangement characteristic of transamination. A catalyzed HCl elimination involving chloropyruvic acid was also observed. A tetrahydroquinoline system related to pyridoxamine was synthesized to permit the stereochemically defined placement of a basic catalytic group. This converted keto acids to amino acids with good stereoselectivity for the formation of optically active products.

Original languageEnglish (US)
Pages (from-to)1969-1979
Number of pages11
JournalJournal of the American Chemical Society
Volume108
Issue number8
DOIs
StatePublished - Jan 1 1986

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Fingerprint Dive into the research topics of 'Mimics of Transaminase Enzymes'. Together they form a unique fingerprint.

Cite this