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Arylsulfatase G (ARSG) is a member of the sulfatase enzyme family. Sulfatases are enzymes which hydrolyze sulfate esters from sulfated steroids, carbohydrates, proteoglycans, and glycolipids. Sulfatases are involved in hormone biosynthesis, modulation of cell signaling, and degradation of macromolecules. The ARSG protein exhibits arylsulfatase activity at acidic pH, as is characteristic of lysosomal sulfatases. The Arylsulfatase G enzyme localizes in the lysosomes. ARSG is inhibited by phosphate, which forms a covalent bond with the active site 3-oxoalanine. Arylsulfatase G is widely expressed, having very low expression in the brain, lung, heart and skeletal muscle.

Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and a member of the peptidase C1 family. CTSZ, which is known also as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and as other members of this family, takes part in tumorigenesis.

PRSS3 is a trypsinogen, and a member of the trypsin family of serine proteases. PRSS3 is expressed in the pancreas and brain and is unaffected by common trypsin inhibitors. It is active on peptide linkages involving the carboxyl group of lysine or arginine. PRSS3 is restricted to the locus of T cell receptor beta variable orphans on chromosome 9. 4 different isoforms encoded by 4 transcript variants were identified for this gene.

Hyaluronidase-1 or HYAL1 is a protein, part of the endolytic glycoside hydrolase proteins group. Human hyaluronidases proteins, are 5 endo­β­N­acetyl­hexosaminidases (including HYAL1, HYAL2, HYAL3). Hyaluronidase-1 causes degradation to hyaluronic acid in the extracellular matrix of somatic tissues. HYAL1 needs an acidic environment and is the most common hyaluronidase in the plasma. Mutations in this protein can lead to mucopolysaccharidosis type IX and hyaluronidase deficiency.

Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases that break down extracellular matrix proteins. The MMP9 is secreted as a 92kDa zymogen. Cleavage of ProMMP-9 results in the active enzyme, having a molecular weight of approximately 82kDa. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by the several cell types: monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells. MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. MMP9 cleaves type IV and type V collagens into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. MMP9 can also degrade fibronectin but not laminin or Pz-peptide.
MMP9 defects may be a cause of susceptibility to intervertebral disc disease (IDD), also known as lumbar disk herniation (LDH).

Glutaminyl-Peptide Cyclotransferase, also known as QPCT is a member of the glutaminyl-peptide cyclotransferase family. QPCT is responsible for the biosynthesis of pyroglutamyl peptides. Furthermore, QPCT is partial against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length following the second residue. QPCT catalyzes N-terminal pyroglutamate formation, also in vitro, it catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid.

Kallistatin (SERPINA4) inhibits human amidolytic and kininogenase activities of tissue kallikrein. This inhibition is attained by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and production of a small C-terminal fragment of the inhibitor as a result of cleavage at the reactive site by tissue kallikrein.

DCTPP1, also known as dCTP pyrophosphatase 1, contains an epilepsy-associated repeat (EAR) domain that is predicted to participate in protein-protein interactions, most likely involved in ligand recognition. This protein functions to hydrolyze abnormal nucleotide triphosphates (NTPs) in cancer cells that, if unregulated, could be incorporated into nascent DNA or RNA.

MMP-1 (interstitial collagenase) can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IGFBP-3, IGFBP-5, casein, gelatin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.

G3BP1 belongs to the heterogeneous nuclear RNA-binding proteins and is also an element of the Ras signal transduction pathway. G3BP1 is one of the DNA-unwinding enzymes that favors partially unwound 3'-tailed substrates and is also able to unwind partial RNA/DNA and RNA/RNA duplexes in an ATP-dependent fashion. G3BP1 binds specifically to the Ras-GTPase-activating protein by associating with its SH3 domain. In addition, G3BP1 cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR.

Urokinase (UK) is a serine protease, which is one of biological plasminogen activators.
It is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing.
It can be obtained from human urine or kidney cell culture.

MMP-3 enzyme is also known as Stromelysin-1or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. It dissolves the intervertebral nucleus pulposus and annulus fibrosus of Herniated Lumbar Intervertebral Disk . MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta.

Trypsin is a serine protease that hydrolyses proteins, it is found in the digestive system of numerous vertebrates. Trypsin is produced as the inactive proenzyme trypsinogen in the pancreas. Trypsin cleaves peptide chains at the carboxyl side of the amino acids lysine and arginine, except when either is followed by proline. Trypsin is secreted into the duodenum, where it acts to hydrolyses peptides into amino acids, which is necessary for the uptake of protein in the food even though peptides are smaller than proteins; they are still too big to be absorbed through the lining of the ileum. The optimal operating pH for Trypsins is about 8 and about 37°C temperature. In cystic fibrosis disease there is a deficiency in transport of trypsin and other digestive enzymes from the pancreas. Trypsin is widely used in various biotechnological processes since it’s available in high quantity in the pancreases, and can be purified rather easily.

Phosphoglycolate phosphatase (PGP) is discovered in all tissues including red cells, lymphocytes and cultured fibroblasts (at protein level). PGP is most active in skeletal muscle and cardiac muscle. The catalytic activity of PGP is 2-phosphoglycolate + H2O = glycolate + phosphate. Diseases associated with PGP include tardive dyskinesia and polycystic kidney disease.

MCEE catalyzes the interconversion of D- and L-methylmalonyl-CoA throughout the degradation of branched chain amino acids, odd chain-length fatty acids, and other metabolites. MCEE protein deficiency is an autosomal recessive inborn error of amino acid metabolism, involving valine, threonine, isoleucine and methionine. This organic aciduria can appear in the neonatal period with life-threatening metabolic acidosis, hyperammonemia, feeding difficulties, pancytopenia and coma.

MMP-1 can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IL-1?, IGFBP-3, IGFBP-5, casein, gelatin, ?1 antitrypsin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.

Phosphoglycolate phosphatase (PGP) is discovered in all tissues including red cells, lymphocytes and cultured fibroblasts (at protein level). PGP is most active in skeletal muscle and cardiac muscle. The catalytic activity of PGP is 2-phosphoglycolate + H2O = glycolate + phosphate. Diseases associated with PGP include tardive dyskinesia and polycystic kidney disease.

Glucuronidase Beta (GUSB) is a lysosomal hydrolase which is taking part in the stepwise degradation of glucuronic acid-containing glycosaminoglycans and plays a significant role in the degradation of dermatan and keratin sulfates. GUSB is comprised of heparin sulfate, chondroitin sulfate and hyaluronan.

Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

Aspartylglucosaminidase, also known as AGA, takes part in the catabolism of Nlinked oligosaccharides of glycoproteins. AGA is a protein coding gene which cleaves asparagine from N-acetylglucosamines in the lysosomal breakdown of glycoproteins.

Ribulose-phosphate 3-epimerase (RPE) is a member of the ribulose-phosphate 3-epimerase family. RPE is the enzyme which converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. Therefore, the RPE enzyme has one substrate, D-ribulose 5-phosphate, and one product, D-xylulose 5-phosphate. RPE participates in three metabolic pathways: pentose phosphate pathway, pentose and glucuronate interconversions, and carbon fixation.

Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases that break down extracellular matrix proteins. The MMP9 is secreted as a 92kDa zymogen. Cleavage of ProMMP-9 results in the active enzyme, having a molecular weight of approximately 82kDa. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by the several cell types: monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells. MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. MMP9 cleaves type IV and type V collagens into large C-terminal three qu

SERPINA5 up regulates TAFI activation by inhibiting the protein C activation. SERPINA5 is a significant regulator in the equilibrium between coagulation and fibrinolysis by differentially inhibiting the activation of TAFI and of Protein-C. SERPINA5 belongs to the serpin serine proteinase inhibitor family. SERPINA5 protein inhibits plasminogen activators as well as activated protein C.
SERPINA5 is secreted in plasma & liver. SERPINA5 is involved in cell inflammation, proliferation, apoptosis, tumour cell migration, invasion, and metastasis. Moreover, SERPINA5 controls the invasive potential of renal cell carcinoma by inhibiting urinary plasminogen activator secreted by the cells. SERPINA5 participtes in regulating key serine proteases which are involved in metastatic prostate disease.