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PRCP is a plasma protein which takes part in the cleavage of C-terminal amino acids linked to proline in proteinfor example angiotensin-2 & 3 at acidic pHenvironment rather than at neutral pHwhich exhibit less activity. This cleavage is important since Angiotensin-2 takes part in regulation of blood pressure & electrolyte balance which is essential to hypertension.

Gltathione S-transferase PI 2, also known as GSTP2 is multifunctional enzyme which is involved in theprotection of cellular components against anti-cancer drugs or peroxidative stress. Furthermore, down regulation of GSTP2induces an increase of oxidative damage in the pyramidal cells of the CA1&CA3 regions as well as in the granular layer ofthe dentate gyrus, which at the end leads to structural and functional damage.

Adenine DNA glycosylase (mutY) is an adenine DNA glycosylase active on DNA substrates including A/G, A/8-oxoG, or A/C mismatches and also has a weak guanine glycosylase activity on G/8- oxoG-containing DNA. mutY is essential for the prevention of mutations resulting from oxidative DNA impairment. Rising levels of mutY in A549 cells exposed to oxygen and infrared radiation leads to improvements in cell survival. mutY is common in neurons where mitochondrial genomes exposed to reactive oxygen species that damage DNA must uphold integrity over the whole mammalian life span.

PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 has protein disulfide isomerase activity. Complexes of lectins and PDIA3 mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. PDIA3 is expressed in the lumbar spinal cord from rats submitted to peripheral lesion during neonatal period. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.

GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.

SURA is a PPIase enzyme and chaperone of Escherichia coli and other Gram-negative bacteria. SURA is a key player in the biogenesis of beta-barrel outer membrane proteins and is involved in cell envelope homeostasis and cell envelope functions. SURA is necessary for the survival of E.coli in stationary phase and needed for pilus biogenesis.

Kallikrein-3 (KLK3) is a part of the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins take part in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 acts normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.

Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as the immunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which are involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes.
SIRPA can be phosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2 domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part in signal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand for SIRPA.

Helicobacter pylori, a Gram-negative, microaerophilic bacterium that populates in the stomach, predominantly at the antrum. Helicobacter pylori causes a chronic inflammation of the mucoid lining of stomach and is highly related to the growth of duodenal and gastric ulcers and stomach cancer. Over 50% of the world's population harbor H. pylori in their upper gastrointestinal tract, infection is more prevalent in developing countries. Thus far, no ideal target H. pylori antigen has been developed for the diagnostic purpose. 23 kDa H. pylori outer membrane protein was identified with a good sensitivity and coverage in the diagnosis of H. pylori infection.

ANPEP or aminopeptidase N, is an enzyme, found in the small-intestinal and renal microvillar membrane and other plasma membranes. The enzyme has a critical part in the digestion of peptides after their hydrolysis by gastric and pancreatic proteases. ANPEP is also part ofthe processing of different peptides as well as peptide hormones, neuropeptides & chemokines. The protein takes part in angiogenesis, enhancing cholesterol crystallization &amino acid transport by formatting with SLC6A19 transport protein and regulating its activity.

NT5E, also known as CD73, is a plasma membrane protein which catalyzes the conversion of extracellular nucleotides into membrane-permeable nucleosides. NT5E is functions as a determinant of lymphocyte differentiation. Defects in NT5E can cause the calcification of joints and arteries.

Formylglutathione hydrolase (Esterase D) is a member of the esterase D family. Esterase D is a serine hydrolase involved in the detoxification of formaldehyde. Esterase D is active toward various substrates including O-acetylated sialic acids, and it may possibly be involved in the recycling of sialic acids. Esterase D is used as a genetic marker for retinoblastoma and Wilson's disease.

CA, also known as carbonic anhydrase is an enzyme that functions around the involvement of CO2 + H2O to HCO3- + H+ (conversion of CO2 to bicarbonate & protons). This enzyme holds a Zn ion as part of its active site. The central function of CA is to preserve the acid-base homeostasis within the blood and various organs. carbonic anhydrase assists Carbonic Anhydrase I to move CO2 to and from tissues.

ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters and goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Further isoforms diverge mainly in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum.

CTSW protein belongs to the peptidase C1 family. CTSW is a cysteine proteinase with a detailed role in the regulation and mechanism of T-cell cytolytic activity. The encoded CTSW is linked to the membrane inside the endoplasmic reticulum of natural killer and cytotoxic T-cells. CTSW expression is up-regulated by interleukin-2.

Folate Hydrolase 1 (Folh1) is a single pass type 2 membrane protein which is expressed mainly in prostate epithelium. Folh1 which is a part of the peptidase M28 family and M28B subfamily has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase activity. Folh1 can be found in urinary bladder, kidney, testis, ovary, stomach, small intestine colon, and the capillary endothelium of various tumors. Therefore, Folh1 plays a role in directed imaging and therapy of recurrent of metastatic disease.

GLYAT is a mitochondrial acyltransferase that conjugates glycine with acyl-CoA substrates in the mitochondria. GLYAT is vital to the detoxification of endogenous and xenobiotic acyl-CoA's.

Sulfite oxidase, also known as SUOX is a homodimeric protein localized to the intermembrane space of mitochondria. Each subunit includes a heme domain as well as a molybdopterin-binding domain. The SUOX enzyme catalyzes the oxidation of sulfite to sulfate, the last reaction in the oxidative degradation of the sulfur amino acids cysteine and methionine. In addition, the deficiency of SUOX results in neurological abnormalities which are often fatal at an early age.

CBR3 catalyzes the reduction of a large number of biologically and pharmacologically active carbonyl compounds to their corresponding alcohols. CBR3 is one of several monomeric NADPH-dependent oxidoreductases. Furthermore, CBR3 contains 3 exons spanning 11.2 kilobases and is strongly linked to another carbonyl reductase gene, the CBR1. It was suggested that CBR3 mediates 9-cis-retinoic acid-induced cytostatis and is a potential prognostic marker for oral malignancy.
CBR3 is identified in the ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate and the testis.

GAPDH is a catalytic enzyme normally known to play a role in glycolysis. GAPDH exists as a tetramer composed of 36-kDa subunits and has a range of intracellular functions. GAPDH catalyzes the reversible reduction of 1,3-bisphosphoglycerate to glyceraldehyde 3-phosphophate in the presence of NADPH. Besides functioning as a glycolytic enzyme in cytoplasm, GAPDH has function in intracellular processes such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication and DNA repair. GAPDH catalyzes a vital energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). The enzyme exists as a tetramer of identical chains.

Glutamate dehydrogenase 1, mitochondrial precursor (GLUD1) is a member of the Glu/Leu/Phe/Val dehydrogenases family. GLUD1 is a mitochondrial glutamate dehydrogenase, which converts L-glutamate into alpha-ketoglutarate. GLUD1 has a pivotal role in nitrogen metabolism in plants and animals. GLUD1 is observed in all organisms and catalyzes the oxidative deamination of 1-glutamate to 2-oxoglutarate. The GLUD1 enzyme has a vital role in regulating amino acid induced insulin secretion. GLUD1 gene mutations cause hyperinsulinism-hyperammonemia syndrome (HHS), which is an inherited condition characterized by high insulin and ammonia levels in the blood. GLUD1 enzyme is allosterically activated by ADP and inhibited by GTP and ATP.

MGLL is a membrane-associated member of the serine hydrolase superfamily. MGLL is expressed in abundance in skeletal muscle and adipose tissue. MGLL functions jointly with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides.

NEIL1 is a member of a class of DNA glycosylases homologous to the bacterial Fpg/Nei family. These glycosylases initiate the first step in base excision repair by cleaving bases damaged by reactive oxygen species and introducing a DNA strand break via the associated lyase reaction. NEIL1 participates in the DNA repair pathway by initiating base excision repair by removing damaged bases, primarily oxidized pyrimidines.

AK1 is a small ubiquitous enzyme which is essential for maintenance and cell growth. It is involved in the regulation of adenine nucleotide composition within a cell by catalyzing the reversible transfer of the terminal phosphate group between ATP and AMP. The AK1 protein is found in the cytosol of skeletal muscle, brain and erythrocytes. Defects in the AK1 gene are the cause of a form of hemolytic anemia.