Argininosuccinate synthase; One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues.

Cytosolic non-specific dipeptidase; Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Catalyzes the production of N- lactoyl-amino acids from lactate and amino acids by reverse proteolysis.

Argininosuccinate synthase; One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues.

Nicotinamide phosphoribosyltransferase; The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma (By similarity). Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. Plays a role in the modulation of circ [...]

Argininosuccinate synthase; One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues.

Xaa-Pro dipeptidase; Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because of the high level of iminoacids in collagen; Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily.

Cytosolic non-specific dipeptidase; Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Catalyzes the production of N- lactoyl-amino acids from lactate and amino acids by reverse proteolysis.

Argininosuccinate synthase; One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues.

Cytosolic non-specific dipeptidase; Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Catalyzes the production of N- lactoyl-amino acids from lactate and amino acids by reverse proteolysis.

Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity).

Cytosolic non-specific dipeptidase; Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Catalyzes the production of N- lactoyl-amino acids from lactate and amino acids by reverse proteolysis.

Diphosphomevalonate decarboxylase; Performs the first committed step in the biosynthesis of isoprenes; Belongs to the diphosphomevalonate decarboxylase family.

Cytosolic non-specific dipeptidase; Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Catalyzes the production of N- lactoyl-amino acids from lactate and amino acids by reverse proteolysis.

Xaa-Pro dipeptidase; Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because of the high level of iminoacids in collagen; Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily.

Lysosomal protective protein 20 kDa chain; Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins.

Diphosphomevalonate decarboxylase; Performs the first committed step in the biosynthesis of isoprenes; Belongs to the diphosphomevalonate decarboxylase family.

Lysosomal protective protein 20 kDa chain; Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins.

Xaa-Pro dipeptidase; Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because of the high level of iminoacids in collagen; Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily.

Dipeptidyl peptidase 3; Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin. Also cleaves Arg-Arg- beta-naphthylamide (in vitro); Belongs to the peptidase M49 family.

Dipeptidyl peptidase 4 membrane form; Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T- cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the mi [...]

Dipeptidyl peptidase 3; Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin. Also cleaves Arg-Arg- beta-naphthylamide (in vitro); Belongs to the peptidase M49 family.

Xaa-Pro dipeptidase; Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because of the high level of iminoacids in collagen; Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily.

Dipeptidyl peptidase 4 membrane form; Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T- cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the mi [...]

Dipeptidyl peptidase 3; Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin. Also cleaves Arg-Arg- beta-naphthylamide (in vitro); Belongs to the peptidase M49 family.

Dipeptidyl peptidase 4 membrane form; Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T- cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the mi [...]

Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity).

Dipeptidyl peptidase 4 membrane form; Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T- cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the mi [...]

Xaa-Pro dipeptidase; Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because of the high level of iminoacids in collagen; Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily.

Guanine deaminase; Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia; Belongs to the metallo-dependent hydrolases superfamily. ATZ/TRZ family.

Diphosphomevalonate decarboxylase; Performs the first committed step in the biosynthesis of isoprenes; Belongs to the diphosphomevalonate decarboxylase family.

Guanine deaminase; Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia; Belongs to the metallo-dependent hydrolases superfamily. ATZ/TRZ family.

Xaa-Pro dipeptidase; Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because of the high level of iminoacids in collagen; Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily.

Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity).

Cytosolic non-specific dipeptidase; Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Catalyzes the production of N- lactoyl-amino acids from lactate and amino acids by reverse proteolysis.

Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity).

Dipeptidyl peptidase 4 membrane form; Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T- cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the mi [...]

Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity).

Nicotinamide phosphoribosyltransferase; The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma (By similarity). Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. Plays a role in the modulation of circ [...]

Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity).

Xaa-Pro dipeptidase; Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because of the high level of iminoacids in collagen; Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily.