Crystallographic studies on the binding of selectively deuterated LLD- and LLL-substrate epimers by isopenicillin N synthase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
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1. Isopenicillin N Synthase: Crystallographic Studies;ChemBioChem;2021-03-25
2. The crystal structure of an isopenicillin N synthase complex with an ethereal substrate analogue reveals water in the oxygen binding site;FEBS Letters;2013-07-13
3. The Interaction of Isopenicillin N Synthase with Homologated Substrate Analogues δ-(L-α-Aminoadipoyl)-L-homocysteinyl-D-Xaa Characterised by Protein Crystallography;ChemBioChem;2013-03-06
4. The crystal structure of isopenicillin N synthase with a dipeptide substrate analogue;Archives of Biochemistry and Biophysics;2013-02
5. Motifs in the C-terminal region of the Penicillium chrysogenum ACV synthetase are essential for valine epimerization and processivity of tripeptide formation;Biochimie;2012-02
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