carboxypeptidaasit

Carboxypeptidaasit is not a term that appears in standard biochemical references as of now. It may be a misspelling or a localized name for carboxypeptidases, a class of exopeptidases that cleave amino acids from the C-terminus of peptides. If encountered in literature, it is advisable to verify the spelling and cross-check against recognized enzyme nomenclature such as carboxypeptidase A, B, C, and related family members.

Carboxypeptidases function by hydrolyzing the peptide bond at the C-terminus, releasing a single amino acid. The best-known mammalian carboxypeptidases are zinc-dependent metallocarboxypeptidases, which use a catalytic zinc ion to activate a water molecule for nucleophilic attack on the substrate. Active sites typically include histidine and glutamate residues that coordinate zinc and facilitate proton transfer.

Substrate specificity varies across family members. For example, classical pancreatic carboxypeptidase A and B prefer hydrophobic and basic C-terminal residues, respectively, while other members display zinc-dependent broad or narrow specificities. Some carboxypeptidases function in digestion (secreted into the digestive tract), whereas others act intracellularly in peptide maturation or hormone processing.

In naming practice, carboxypeptidases are designated with letters (A, B, C, etc.) or by organism and function, with new variants identified through gene and protein sequence analyses. If carboxypeptidaasit refers to a newly described enzyme, its characterization would include substrate range, kinetic parameters, metal dependence, cofactor requirements, tissue distribution, and physiological function.