Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Biochem J. 1988 Mar 15;250(3):789-96.

Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli.

Author information

  • 1Department of Biochemical Microbiology, Wellcome Research Laboratories, Beckenham, Kent, U.K.

Abstract

A multi-step procedure has been developed for the purification of [acyl-carrier-protein] acetyltransferase from Escherichia coli, which allows the production of small amounts of homogeneous enzyme. The subunit Mr was estimated to be 29,000 and the native Mr was estimated to be 61,000, suggesting a homodimeric structure. The catalytic properties of the enzyme are consistent with a Bi Bi Ping Pong mechanism and the existence of an acetyl-enzyme intermediate in the catalytic cycle. The enzyme was inhibited by N-ethylmaleimide and more slowly by iodoacetamide in reactions protected by the substrate, acetyl-CoA. However, the enzyme was apparently only weakly inhibited by the thiol-specific reagent methyl methanethiosulphonate. The nature of the acetyl-enzyme intermediate is discussed in relationship to that found in other similar enzymes from E. coli, yeast and vertebrates.

PMID:
3291856
[PubMed - indexed for MEDLINE]
PMCID:
PMC1148925
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Portland Press Icon for PubMed Central
    Loading ...
    Write to the Help Desk