Kinetic and inactivation studies of recombinant Drosophila choline acetyltransferase

Luis Carbini, Gerry Rodriguez, Louis B. Hersh

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


A cDNA for Drosophila choline acetyltransferase (ChAT) was expressed in E. coli and the recombinant enzyme partially purified. Kinetic analysis yielded the following constants for the recombinant enzyme; KmAcCoA = 29 μM, KmCoA = 25 μM, Kmcholine = 330 μM and Kmacetylcholine = 2 mM. The recombinant Drosophila enzyme, like the enzyme from other species, exhibited an increase in activity as a function of increased salt concentration. Chemical modification studies using dithio-bis-nitro-2-carboxylate, butanedione, and diethylpyrocarbonate showed that the recombinant enzyme contains active site cysteine, arginine, and histidine residues. These studies demonstrate that the recombinant Drosophila ChAT possesses the same catalytic properties as the enzyme from a variety of other sources.

Original languageEnglish
Pages (from-to)119-124
Number of pages6
JournalBrain Research Bulletin
Issue number1
StatePublished - Jan 1990

Bibliographical note

Funding Information:
This research was supported in part by grants AG 05893 and AG 08013 from the National Institute on Aging.


  • Choline acetyltransferase (ChAT)
  • Drosophila
  • Kinetics
  • Recombinant enzyme

ASJC Scopus subject areas

  • General Neuroscience


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