In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH.

Abstract:

:The Escherichia coli siderophore enterobactin is assembled from 2,3-dihydroxybenzoate (2,3-DHB) and l-serine by the nonribosomal peptide synthetases EntB and EntF. The processive thiol-template strategy used can be sabotaged by EntB misacylation. Through in vitro kinetic analysis, we demonstrate two potential routes to EntB misacylation and provide evidence for two mechanisms by which the hot dog-fold thioesterase EntH can potentially prevent or reverse EntB misacylation.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Chen D,Wu R,Bryan TL,Dunaway-Mariano D

doi

10.1021/bi802207t

subject

Has Abstract

pub_date

2009-01-27 00:00:00

pages

511-3

issue

3

eissn

0006-2960

issn

1520-4995

pii

10.1021/bi802207t

journal_volume

48

pub_type

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