CNDP2
CNDP2 (carnosine dipeptidase 2) is a cytosolic metallodipeptidase with broad substrate specificity, also known as cytosolic non-specific dipeptidase, tissue carnosinase, peptidase A, CN2 and CPGL. It hydrolyses amide bonds in dipeptides and pseudopeptides. Browse Assay Genie's current range of CNDP2 research reagents below, or read on for the biology behind the target.
CNDP2 is a cytosolic metallodipeptidase that catalyses the hydrolysis of amide bonds in dipeptides and pseudopeptides, with broad substrate specificity. Its substrates include L-cysteinylglycine, an intermediate metabolite of the gamma-glutamyl cycle of glutathione metabolism, and it can also hydrolyse threonyl-containing dipeptides. Under physiological conditions of amino acid and lactate excess, the enzyme can run a reverse proteolysis reaction, generating N-[(S)-lactoyl]-L-phenylalanine and possibly other N-lactoyl-amino acids, which it can also hydrolyse in vitro. N-[(S)-lactoyl]-L-phenylalanine is an exercise-induced metabolite that influences food intake and systemic energy balance. CNDP2 has also been reported to play a role in the regulation of cell cycle arrest and apoptosis.
The CNDP2 gene encodes a protein that belongs to the peptidase M20A family and sits within the HGNC group of M20 metallopeptidases. The protein localises to the cytosol. Mouse and rat both have an ortholog named Cndp2, which allows the enzyme to be studied in common rodent models.
The name reflects a history of reassessment. The enzyme is known as tissue carnosinase and was previously called peptidase A, and the HGNC name refers to the CNDP dipeptidase 2 (metallopeptidase M20 family). NCBI Gene notes that it is a nonspecific dipeptidase rather than a selective carnosinase. UniProt likewise states that carnosine is probably not a physiological substrate and that L-homocarnosine is not a substrate. This distinguishes it from the related CNDP1 gene product, and researchers working on CNDP2 antibody, CNDP2 ELISA kit or CNDP2 protein experiments should keep this distinction in mind.
CNDP2 hydrolyses L-cysteinylglycine, an intermediate of the gamma-glutamyl cycle, making it relevant to studies of glutathione turnover.
CNDP2 can generate N-[(S)-lactoyl]-L-phenylalanine, an exercise-induced metabolite that influences food intake and systemic energy balance.
CNDP2 has a reported role in regulating cell cycle arrest and apoptosis, making it a subject in cell fate research.
As a broad-specificity M20A metallodipeptidase, CNDP2 is used to study substrate selectivity and reverse proteolysis in dipeptide and N-lactoyl-amino acid chemistry.
CNDP2 is a cytosolic metallodipeptidase that hydrolyses amide bonds in dipeptides and pseudopeptides, including L-cysteinylglycine from the gamma-glutamyl cycle. It can also synthesise N-lactoyl-amino acids by reverse proteolysis and has a reported role in cell cycle arrest and apoptosis.
CNDP2 is also called cytosolic non-specific dipeptidase, tissue carnosinase, peptidase A, CN2, CPGL, HsT2298 and FLJ10830. Despite the carnosinase name, it is a nonspecific dipeptidase, and carnosine is probably not a physiological substrate.
Yes. Mouse and rat each have an ortholog named Cndp2, so the enzyme can be studied in rodent models. Researchers should check the datasheet of any product for its validated reactivity before using it with a given species.
A related carnosine dipeptidase from the M20 metallopeptidase group, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q96KP4; product specifications from Assay Genie datasheets.