Tight Binding of Transition-State Analogues to a Peptidyl-Aminoacyl-L/D-Isomerase from Frog Skin

Changing hands: In the biosynthesis of bombinin H, an isomerase catalyses the inversion of chirality of an amino acid in peptide linkage through a deprotonation/protonation mechanism. We have synthesized two substrate analogues (1) that are potent inhibitors of the enzyme reaction. Our results stron...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2011-09, Vol.12 (13), p.1996-2000
Main Authors: Gehmayr, Verena, Mollay, Christa, Reith, Lorenz, Müller, Norbert, Jilek, Alexander
Format: Article
Language:English
Subjects:
Amino Acid Isomerases - chemistry
Amino Acid Isomerases - metabolism
Amino Acids - chemistry
Amino Acids - metabolism
Animals
Anura
chirality
Communication
D-amino acids
enzyme catalysis
inhibitors
Kinetics
Molecular Structure
Peptides - chemistry
Peptides - metabolism
post-translational modifications
Protein Binding
Protein Processing, Post-Translational
Skin - enzymology
Skin - metabolism
Stereoisomerism
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Summary:Changing hands: In the biosynthesis of bombinin H, an isomerase catalyses the inversion of chirality of an amino acid in peptide linkage through a deprotonation/protonation mechanism. We have synthesized two substrate analogues (1) that are potent inhibitors of the enzyme reaction. Our results strongly support a planar transition state, such as an enolate anion intermediate (2).
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.201100203