Latexin (LXN)

ECI; TCI; MUM; Endogenous carboxypeptidase inhibitor; Tissue carboxypeptidase inhibitor

Latexin (LXN)
Latexin is a specific inhibitor of zinc-dependent metallocarboxypeptidases. The deduced 222-amino acid protein is an elongated molecule with N- and C-terminal domains that each consist of an alpha helix enveloped by a curved beta sheet. The 2 domains are separated by a connecting segment.Lxn was less potent against other mammalian carboxypeptidases, and it did not inhibit other metallopeptidases or serine proteases.
It also showed low specificity, inhibiting several metallocarboxypeptidases containing a characteristic alpha/beta hydrolase fold. The inhibition constant was within the nanomolar range for these substrates. LXN did not inhibit enzymes of other carboxypeptidase classes.

Organism species: Homo sapiens (Human)

Organism species: Mus musculus (Mouse)

Organism species: Rattus norvegicus (Rat)