Abstract
Nonribosomal enterobactin synthetase of Escherichia coli was found to prematurely release a large amount of linear precursors in an in vitro reconstitution. However, these side products are suppressed to negligible levels by polymeric cosolvents that create macromolecular crowding, a prominent feature of the intracellular environment. These findings show that macromolecular crowding is essential to normal functioning of the nonribosomal peptide synthetase and suggest that it may be crucial to btotechnological utilization of similar enzyme systems.
Original language | English (US) |
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Pages (from-to) | 649-652 |
Number of pages | 4 |
Journal | Organic Letters |
Volume | 10 |
Issue number | 4 |
DOIs | |
State | Published - Feb 21 2008 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Physical and Theoretical Chemistry
- Organic Chemistry