The dynamic nature of transglutaminases
Description
Transglutaminases incorporate a variety of primary amines into specific glutamine residues of target proteins in a transamidation reaction: the incorporation of lysine residues result in protein crosslinks, while the incorporation of small amines result in protein-amine conjugates. Transglutaminases play important but poorly understood roles in many diseases, and greater knowledge of their catalytic activity will provide valuable insight. This study provides evidence for a new transglutaminase mechanism-of-action: dynamic protein crosslinking via continuous interchange between incorporated lysines and incorporated amines. This finding contributes to a greater understanding of transglutaminase biology and potentially opens new avenues for disrupting disease processes.
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| ID Code: | 116350 |
|---|---|
| Item Type: | QUT Thesis (Masters by Research) |
| Supervisor: | Richard, Derek, Stephenson, Sally-Anne, Walsh, Terry, & Croll, Tristan |
| Keywords: | Transglutaminase, transamidation, amine incorporation, isopeptide crosslinks, monoamination, polyamination |
| DOI: | 10.5204/thesis.eprints.116350 |
| Divisions: | Past > QUT Faculties & Divisions > Faculty of Health Current > Schools > School of Biomedical Sciences |
| Institution: | Queensland University of Technology |
| Deposited On: | 22 May 2018 04:36 |
| Last Modified: | 22 May 2018 04:36 |
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