Structural insights into Escherichia coli phosphopantothenoylcysteine synthetase by native ion mobility–mass spectrometry
Author:
Affiliation:
1. Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.
2. Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, U.K.
Abstract
Publisher
Portland Press Ltd.
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
https://portlandpress.com/biochemj/article-pdf/476/21/3125/859412/bcj-2019-0318.pdf
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3. Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified coenzyme A biosynthetic enzyme in bacteria;J. Biol. Chem.,2001
4. Molecular characterization of lantibiotic-synthesizing enzyme EpiD reveals a function for bacterial Dfp proteins in coenzyme A biosyntheis;J. Biol. Chem.,2000
5. Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed with a pentapeptide substrate;EMBO J.,2000
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