Active site organization of bacterial type I fatty acid synthetase.

Abstract:

:Four kinds of active sites of bacterial fatty acid synthetase were mapped on distinct regions within a subunit. Active sites were specifically labeled with radioactive substrates and active-site-directed inhibitors. Labeled enzymes were cleaved with proteases, and the fragments thus produced were identified with respect to specific labels by SDS-polyacrylamide gel electrophoresis and a fluorographic technique. The linear alignment of such fragments in the original subunit was established and when the results were combined with those of our previous work, five active sites were located in three regions as follows. Starting from the N-terminal of the subunit, we located acetyl, malonyl and palmitoyl transferases in the first region, the acyl carrier site in the second region (Morishima & Ikai (1985) Biochim. Biophys. Acta 832, 297-307), and beta-ketoacyl synthetase in the third region. The observed order of active sites of bacterial fatty acid synthetase can be correlated with that of the yeast enzyme, which has two kinds of subunits.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Morishima N,Ikai A

doi

10.1093/oxfordjournals.jbchem.a122191

subject

Has Abstract

pub_date

1987-12-01 00:00:00

pages

1451-7

issue

6

eissn

0021-924X

issn

1756-2651

journal_volume

102

pub_type

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