Purification and characterization of a novel imidazole dipeptide synthase from the muscle of the Japanese eel Anguilla japonica
Laboratory studyOther animals
- Design
- Laboratory study
- What was measured
- Purification, molecular mass, pH and temperature optima, kinetics, metal dependence and N-terminal sequence of an enzyme from eel white muscle that synthesises carnosine, anserine and balenine from their precursors.
What the authors reported
The enzyme was purified 1130-fold, had a native mass of about 275 kDa with 43 kDa subunits, optimal pH about 9.5 and temperature about 60 degrees C, Km values of 44 mM for beta-alanine and 89 mM for pi-methylhistidine, was activated by zinc and inhibited by EDTA, and also hydrolysed the dipeptides. Anserine-synthesising activity was highest even though eel muscle contains mostly carnosine; the N-terminus resembled a haptoglobin precursor.
Limits of this study
Fish enzyme; relevance to mammalian carnosine synthase not established. Abstract only.
Source
PubMed 17261377 · doi:10.1016/j.cbpb.2006.12.002
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.