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CPA5
CPA5 (carboxypeptidase A5) is a secreted member of the M14 family of carboxypeptidases, a group of enzymes that remove amino acids from the C-terminus of peptides and proteins. It belongs to the A/B subfamily and is synthesised with an N-terminal pro region that is cleaved to activate the enzyme. Browse Assay Genie's current range of CPA5 research reagents below, or read on for the biology behind the target.
CPA5 is a carboxypeptidase, an enzyme that acts on peptide substrates from the carboxyl end. Carboxypeptidases as a group have functions ranging from the digestion of food to the selective biosynthesis of neuroendocrine peptides. CPA5 is classed under EC 3.4.17.-, and UniProt assigns it to the peptidase M14 family. It is annotated as a secreted protein.
Members of the A/B subfamily of carboxypeptidases, including CPA5, contain a pro region of roughly 90 amino acids. This region assists in the folding of the active carboxypeptidase domain. Cleavage of the pro region activates the enzyme, so CPA5 is made as a precursor and becomes catalytically active only after processing. This is relevant when choosing which form of the CPA5 protein to study, or what an CPA5 antibody is expected to recognise.
The CPA5 gene is located on human chromosome 7 and is listed by HGNC within the M14 carboxypeptidases gene group. The mouse ortholog is Cpa5. Related A-type carboxypeptidases, including CPA1, CPA2, CPA3 and CPA4, belong to the same wider family, which makes them useful comparators when characterising specificity or expression. The source information available for CPA5 is limited, and its precise substrates and physiological roles are not described in the annotation used for this page.
CPA5 is an M14 family carboxypeptidase, making it a subject for studies of C-terminal peptide processing within this enzyme group.
The pro region of about 90 amino acids aids folding, and its cleavage activates the enzyme, providing a model for precursor processing.
Carboxypeptidases act in roles from food digestion to neuroendocrine peptide biosynthesis, a context for investigating where CPA5 fits.
Comparing CPA5 with CPA1, CPA2, CPA3 and CPA4 helps to define differences within the A/B carboxypeptidase subfamily.
CPA5 is a secreted carboxypeptidase of the peptidase M14 family. Carboxypeptidases cleave amino acids from peptide C-termini, with roles ranging from food digestion to neuroendocrine peptide biosynthesis. CPA5 is made with a pro region that aids folding and is cleaved to activate the enzyme.
As an A/B subfamily carboxypeptidase, CPA5 contains a pro region of approximately 90 amino acids. It assists the folding of the active carboxypeptidase domain, and its cleavage activates the enzyme. Researchers should therefore consider whether a reagent targets the precursor, the mature form or both.
The mouse ortholog is Cpa5. In humans, CPA5 sits in the M14 carboxypeptidase group alongside CPA1, CPA2, CPA3 and CPA4. Cross-species use depends on sequence conservation, so check the datasheet of any product for its validated reactivity.
Other A-type carboxypeptidases from the M14 family with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q8WXQ8; product specifications from Assay Genie datasheets.
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