Kinetic and inactivation studies of recombinant Drosophila choline acetyltransferase.

Abstract:

: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 microM, KmCoA = 25 microM, Kmcholine = 330 microM, 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.

journal_name

Brain Res Bull

journal_title

Brain research bulletin

authors

Carbini L,Rodriguez G,Hersh LB

doi

10.1016/0361-9230(90)90295-b

subject

Has Abstract

pub_date

1990-01-01 00:00:00

pages

119-24

issue

1

eissn

0361-9230

issn

1873-2747

pii

0361-9230(90)90295-B

journal_volume

24

pub_type

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