Some properties of a homocarnosine-carnosine synthetase isolated from rat brain
Laboratory studyOther animals
- Design
- Laboratory study
- What was measured
- Partial purification and kinetic properties of an enzyme from rat brain that synthesises carnosine and homocarnosine.
What the authors reported
The enzyme was purified roughly 30 to 40-fold and synthesised both carnosine and homocarnosine with a pH optimum of 7.4. Synthesis required ATP, magnesium and DPN, and an ATP-PPi exchange reaction pointed to an aminoacyl-AMP intermediate. About 6 ATP were hydrolysed per dipeptide formed, which the authors took to indicate a catalytic role for DPN.
Limits of this study
Early enzymology; the enzyme was later identified molecularly as ATPGD1. Full text not read. PubMed record carries no abstract, so findings could not be rechecked against PubMed.
Source
PubMed 4358880 · doi:10.1111/j.1471-4159.1973.tb06027.x
Entry checked against PubMed record (title and citation only, no abstract); findings from OpenAlex abstract on 2026-10-19. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.