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Antioxidant enzyme Glutathione S- Transferase (GST) is thought to do the primary cellular defense mechanism against reactive oxygen species. GST reduces lipid hydroperoxides through its Se-independent glutathione peroxidase activity. The enzyme also detoxifies lipid peroxidation end products such as 4-hydroxynonenal (4-HNE).
The soluble GST is a 26 kDa protein which occurs as a dimer in all aerobic organisms. Each monomer has two domains, one that binds GSH and is an /-structure similar to thioredoxin and the other, all helical, that binds the hydrophobic substrate. The GST -fusion protein expression system is a widely used recombinant protein expression system that allows a peptide or a regulatory protein domain to be expressed as a fusion to the C-terminus of Schistosoma japonicum GST. Fusion proteins also possess GST -enzymatic activity and can undergo dimerization similar to in vivo. The fusion protein can be purified via GST -affinity column chromatography. In most cases, the desired peptides or domains are removed from GST by applying a specific protease that recognizes and cleaves the linker between the protein domain and GST. The technique has been widely used to generate different kinds of proteins for crystallization, molecular immunology studies, the production of vaccines and studies involving protein-protein and protein-DNA interactions.

PDE6H belongs to the rod/cone cGMP-PDE gamma subunit family, which selectively catalyze the hydrolysis of 3 cyclic phosphate bonds in adenosine and/or guanine 3,5 cyclic monophosphate (cAMP and/or cGMP). This family regulates the cellular levels, localization and duration of action of these second messengers by controlling the rate of their degradation. PDE6H is the inhibitory (or gamma) subunit of the cone-specific cGMP phosphodiesterase, which is atetramer composed of two catalytic chains (alpha and beta), and two inhibitory chains (gamma). PDE6H is particularly expressed in the retina, and is implicated in the transmission and amplification of the visual signal. Mutations in PDE6H have been associated with retinal cone dystrophy type 3A.

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, 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.

HEXA is the alpha subunit of the lysosomal enzyme beta-hexosaminidase which, combined with the cofactor GM2 activator protein, catalyzes the degradation of the ganglioside GM2, and other molecules having N-acetyl hexosamines terminus. The two subunits composing Beta-hexosaminidase, alpha and beta, belong to the glycosyl hydrolases family and are encoded by distinct genes. Alpha subunit gene mutations can cause Tay-Sachs disease (GM2-gangliosidosis type I).

Neuron-specificenolase also caled NSE is a glycolytic isoenzyme which is situated in central and peripheral neurons and neuroendocrine cells. Enolase-2 is released into the CSF when neural tissue is injured. Neoplasms derived from neural or neuroendocrine tissue release Enolase-2 into the blood. Enolase-2 is a useful substance that has been detected in patients with certain tumors, such as neuroblastoma, small cell lung cancer, medullary thyroid cancer, carcinoid tumors, pancreatic endocrine tumors, and melanoma. ENO2 is 1 of the 3 enolase isoenzymes found in mammals. ENO2 isoenzyme, is found in mature neurons and cells of neuronal origin. An exchange from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates.

UPP1 catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate which are used as carbon and energy sources or in the release of pyrimidine bases for nucleotide synthesis. UPP1 is part of the family of glycosyltransferases, specifically the pentosyltransferases. Pyrimidine nucleoside phosphorylases add ribose or deoxyribose to pyrimidine bases to form nucleosides that can be incorporated into RNA or DNA.

Glycogen phosphorylase (PYGL) converts from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 15. Activity of the PYGL enzyme is further regulated by numerous allosteric effectors and hormonal controls. The liver isozyme supplies the glycemic demands of the body in general whereas the brain and muscle isozymes supply just those tissues.

Alanine aminotransferase 2 (GPT2), catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids. Multiple transcript variants encoding various isoforms have been found for GPT2.

Ribonuclease 3 (RNASE3) is cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. RNASE3 possesses a broad diversity of biological activities. RNASE3 protein has shown antibacterial activity such as cytoplasmic membrane depolarization of preferentially Gram-negative and Gram-positive strains and promotes E. coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.

ATP-dependent Clp protease proteolytic subunit (CLPP) is a member of the peptidase family S14. CLPP cleaves peptides in a variety of proteins in a manner which requires ATP hydrolysis. CLPP being the catalytic core of the Clp proteolytic complex is commonly involved in many cellular processes via the regulation of intracellular protein quality. CLPP is responsible for a somewhat general and central housekeeping function rather than for the degradation of specific substrates.

SDSL belongs to the serine/threonine dehydratase family and function as a serinespecific dehydratase. SDSL utilizes pyridoxal phosphate and is one of three key enzymes which take part in the metabolism of Glycine and serine.

ADP-ribosylarginine hydrolase (ADPRH) is a member of the ADP-ribosylglycohydrolase family. ADPRH catalyzes the removal of mono-ADP-ribose from arginine residues of proteins in the ADP-ribosylation cycle. The human ADPRH enzyme is DTT-independent as opposed to the rat and mouse enzymes, which require DTT for maximal activity.

CNDP Dipeptidase 2 (CNDP2), is a cytosolic, non-specific dipeptidase which is a part of the peptidase M20A protein family. CNDP2 is a secreted peptidase homologous to M20 peptidases. CNDP2 expresses through all adult and fetal tissue, though, an isoform missing exons 3 and 4 expresses in all fetal tissue in adult liver. Over expression of CPGL-B in hepatocellular carcinoma cells results in significant inhibition of HC cell viability, colony formation, cell invasiveness and tumor configuration.

Porphobilinogen deaminase (HMBS) belongs to the hydroxymethylbilane synthase superfamily. HMBS is a cytoplasmic enzyme found in the heme synthesis pathway. HMBS is the 3rd enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of 4 porphobilinogen molecules into the linear hydroxymethylbilane. HMBS gene mutations cause errors in pyrrole metabolism which in turn lead to the autosomal dominant disease acute intermittent porphyria.

Aspartoacylase is a homodimer which catalyzes the deacetylation of N-acetylaspartic acid (NAA) (a protein whose hydrolysis is crucial to maintenance of intact white matter) to generate acetate and L-aspartate. Aspartoacylase (ASPA) is expressed in the liver, lung and kidney tissue, as well as in the skeletal muscle and in cerebral white matter. NAA is ample in the brain where hydrolysis by aspartoacylase is believed to aid maintain white matter. In other tissues ASPA functions as a scavenger of NAA from body fluids. ASPA gene mutations cause Canavan disease (CAND or spongy degeneration of the brain).

Fucosidase Alpha-L- 2 Plasma (FUCA2) is a plasma alpha-L-fucosidase, which represents 10-20% of the total cellular fucosidase activity. FUCA2 protein belongs to the glycosyl hydrolase 29 family, and catalyzes the hydrolysis of the alpha-1,6-linked fucose fused to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. FUCA2 is crucial for Helicobacter pylori adhesion to human gastric cancer cells.

Serine protease 28, also known as Prss28, is a member of the S1 serine proteinase family with a conserved Histidine-Aspartic Acid-Serine catalytic triad. Prss28 shows mixed substrate specificity which silences signaling through proteinase-activated receptors. Furthermore, Prss28 is involved with embryo hatching and its activity is vital for successful implantation.

Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

Amine Oxidase Copper Containing 3 , also referred to AOC3, a copper amine oxidase with a topaquinone cofactor.
AOC3 is a cell adhesion protein which participates in recirculation & extravasation of lymphocyte by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin independent fashion.
Amine Oxidase Copper Containing 3 acts in adipogenesis.
The protein catalyzes the oxidative deamination of small primary amines such as methylamine, benzylamine & aminoacetone in a reaction that produces an aldehyde, ammonia and H2O2.

MECR catalyzes the reduction of trans-2-enoyl-CoA to acyl-CoA with chain length from C6 to C16 in an NADPH dependent manner with preference to medium chain length substrate. MECR protein takes part in the mitochondrial synthesis of fatty acids.

Single-strand-selective monofunctional uracil-DNA glycosylase (SMUG1) is an enzyme responsible for recognizing base lesions in the genome and initiating base excision DNA repair. SMUG1 participates in base excision repair by removing uracil from single- and double-stranded DNA. SMUG1 serves as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA and has inclination for single-stranded DNA substrates. SMUG1 activity is greater against mismatches (U/G) than against matches (U/A).

Ubiquitin carboxyl-terminal hydrolase isozyme L3 belongs to a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to produce the ubiquitin monomer. UCHL3 takes part in the regulation of neuronal development and spermatogenesis and is associated to neurodegenerative diseases. UCHL3 has a 54% homology to UCHL1.