Figure 2

Transglutaminase inhibition: possible therapeutic mechanisms to protect cells from death in neurological disorders

Vittorio Gentile*, Elenamaria Fioretti, Nicola Gaetano Gatta and Rosaria Romano

Published: 25 July, 2017 | Volume 1 - Issue 1 | Pages: 026-038

ibm-aid1004-g002

Figure 2:

Schematic representation of a two-step transglutaminase reaction. Step 1: In the presence of Ca2+, the active-site cysteine residue reacts with the γ-carboxamide group of an incoming glutaminyl residue of a protein/peptide substrate to yield a thioacyl-enzyme intermediate and ammonia. Step 2: The thioacyl-enzyme intermediate reacts with a nucleophilic primary amine substrate, resulting in the covalent attachment of the amine-containing donor to the substrate glutaminyl acceptor and regeneration of the cysteinyl residue at the active site. If the primary amine is donated by the ε-amino group of a lysyl residue in a protein/polypeptide, a Nε-(γ-L-glutamyl)-L-lysine (GGEL) isopeptide bond is formed.

Read Full Article HTML DOI: 10.29328/journal.hjbm.1001004 Cite this Article Read Full Article PDF

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