CPDW-II

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Introductions

Carboxypeptidases (CPs) are a class of peptide chain exonucleases that specifically degrade and release free amino acids from the C-terminus of peptide chains one by one. In animal and plant tissues and organs, carboxypeptidases play an important physiological function. Carboxypeptidases are widely used in pharmaceuticals, food an d other industrial fields. In the field of medicine. Since carboxypeptidase is widely involved in biochemical reactions of the body, it can be used to diagnose and treat diseases through the detection of carboxypeptidase in the body, and in addition, it can be used in medicine for the degradation of undesirable substances (toxins, etc.) in the body. In the food industry, it can be used for the preparation of high F-value oligopeptides, the removal of ochratoxin from food and feed, and as a de-bittering agent, etc.

Source

According to the source classification, carboxypeptidases can be classified as animal carboxypeptidases, plant carboxypeptidases and microbial carboxypeptidases. A series of metallopeptidases are contained in different blockages of mammals to perform the corresponding physiological functions. For example, pancreatic carboxypeptidases A and B mainly help to digest food, carboxypeptidase E selectively processes. Bioactive peptides, carboxypeptidase M is selectively involved in the processing of peptide hormones, and carboxypeptidase D (in Golgi) and carboxypeptidase N (in plasma) are involved in the processing of peptides and proteins. Studies on animal-derived carboxypeptidases. The main focus is on human, pig, bovine, and small house mouse.

Carboxypeptidase D

Carboxypeptidase D can refer to one of several enzymes. A family of serine carboxypeptidases (i.e. enzymes that use an active site serine residue) includes (EC 3.4.16.6, cereal serine carboxypeptidase II, Saccharomyces cerevisiae KEX1 gene product, carboxypeptidase Kex1, gene KEX1 serine carboxypeptidase, KEX1 carboxypeptidase, KEX1 proteinase, KEX1DELTAp, CPDW-II, serine carboxypeptidase, Phaseolus proteinase) is an enzyme. This enzyme has an optimal pH of 4.5-6.0, is inhibited by diisopropyl fluorophosphate, and catalyses the following chemical reaction

Metallocarboxypeptidase

A completely different enzyme has also been named carboxypeptidase D. This second enzyme is a metallocarboxypeptidase (i.e., it uses zinc ions in the active site instead of serine residues) and is widely expressed in mammalian tissues. Metallocarboxypeptidases are a group of extracellular carboxypeptidases with high activity under neutral or weakly basic conditions, including carboxypeptidases A and B, lysine carboxypeptidase (EC3.4.17.3). Glycine carboxypeptidase (EC3.4.17.4) and glutamate carboxypeptidase (EC3.4.17.11), etc. Among them, carboxypeptidase A can release C-terminal amino acids (except proline, hydroxyproline, arginine and lysine) and has a strong hydrolysis ability for carboxy-terminal amino acids with aromatic side chains and large aliphatic side chains. In comparison, carboxypeptidase A releases non-polar amino acids, histidine, threonine, and homoserine relatively quickly, but releases aspartic acid, serine, methionine, and lysine more slowly, but with increasing pH, the rate of action on macroaspartic acid, serine, and methionine continues to accelerate.

Applications

• Pharmaceutical Lead City
• Potentially important drug target
• Food industry
• Hydrolysis of ochratoxin A in food or feed products
• Detoxification of soy protein hydrolysate
• Biotechnology
• Model enzymes designed for use as specific inhibitors of zinc proteases
• Insulin production
• Peptide synthesis