Mechanistic issues in asparagine synthetase catalysis

Adv Enzymol Relat Areas Mol Biol. 1998;72:145-98. doi: 10.1002/9780470123188.ch5.

Abstract

The enzymatic synthesis of asparagine is an ATP-dependent process that utilizes the nitrogen atom derived from either glutamine or ammonia. Despite a long history of kinetic and mechanistic investigation, there is no universally accepted catalytic mechanism for this seemingly straightforward carboxyl group activating enzyme, especially as regards those steps immediately preceding amide bond formation. This chapter considers four issues dealing with the mechanism: (a) the structural organization of the active site(s) partaking in glutamine utilization and aspartate activation; (b) the relationship of asparagine synthetase to other amidotransferases; (c) the way in which ATP is used to activate the beta-carboxyl group; and (d) the detailed mechanism by which nitrogen is transferred.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Ammonia / metabolism
  • Aspartate-Ammonia Ligase / antagonists & inhibitors
  • Aspartate-Ammonia Ligase / classification
  • Aspartate-Ammonia Ligase / metabolism*
  • Aspartic Acid / metabolism
  • Binding Sites
  • Eukaryotic Cells / enzymology
  • Glutamine / metabolism
  • Molecular Sequence Data
  • Prokaryotic Cells / enzymology
  • Sequence Homology, Amino Acid

Substances

  • Glutamine
  • Aspartic Acid
  • Ammonia
  • Adenosine Triphosphate
  • Aspartate-Ammonia Ligase