Carnosinases, their substrates and diseases
ReviewHumansOther animals
- Design
- Review
- Subjects
- not stated in abstract
- Dose used in the study
- not stated in abstract
- Duration
- not stated in abstract
- What was measured
- Review of the structure and function of carnosinase enzymes (human serum CN1 and tissue CN2, and related PepD, PepV and anserinase enzymes) and their substrates carnosine, homocarnosine and anserine.
What the authors reported
The authors describe carnosinases as Xaa-His dipeptidases found across all kingdoms of life. The two human forms, serum CN1 and tissue CN2, hydrolyse carnosine and homocarnosine under suitable conditions. They report that changes in serum CN1 activity have been linked to neurological disorders, chronic diseases and cancer, and that the use of carnosinase levels as a cerebrospinal fluid biomarker has been questioned.
Limits of this study
Narrative review focused on enzymology; no clinical outcome data.
Source
PubMed 24566305 · doi:10.3390/molecules19022299
Entry checked against full text (journal site, MDPI) on 2026-10-11. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.