Molecular identification of carnosine synthase as ATP-grasp domain-containing protein 1 (ATPGD1)
Laboratory studyOther animals
- Design
- Laboratory study
- What was measured
- Purification of carnosine synthase from chicken pectoral muscle, candidate identification and activity of recombinant mouse and human ATPGD1.
What the authors reported
Carnosine synthase was purified about 1500-fold from chicken muscle and database mining identified ATPGD1 as the candidate. Recombinant mouse and human ATPGD1 expressed in HEK293T cells synthesised carnosine and homocarnosine. The enzyme showed 15 to 25-fold higher catalytic efficiency for beta-alanine than for GABA.
Limits of this study
Enzyme identification study; no physiological outcomes. Full text not read.
Source
PubMed 20097752 · doi:10.1074/jbc.M109.095505
Entry checked against PubMed abstract (E-utilities) on 2026-10-19. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.