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Tight Binding of Transition‐State Analogues to a Peptidyl‐Aminoacyl‐ L / D ‐Isomerase from Frog Skin
Author(s) -
Gehmayr Verena,
Mollay Christa,
Reith Lorenz,
Müller Norbert,
Jilek Alexander
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201100203
Subject(s) - peptide , dermorphin , stereochemistry , chemistry , amino acid , isomerase , residue (chemistry) , biochemistry , peptide sequence , nonribosomal peptide , transition state analog , active site , enzyme , biosynthesis , opioid peptide , receptor , gene , opioid
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 ).