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

Gehmayr Verena | Zendy; Mollay Christa | Zendy; Reith Lorenz | Zendy; Müller Norbert | Zendy; Jilek Alexander | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

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 ).

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research