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Serpin Peptidase Inhibitor, Clade C Member 1 (SERPINC1), which is a part of the serpin superfamily, is a plasma protease inhibitor. SERPINC1 inhibits thrombin and other activated serine proteases of the coagulation system, and regulates the blood coagulation cascade. SERPINC1 also inhibits Thrombin and Factors IXa, Xa and XIa. Deficiencies in SERPINC1 can cause ATIII deficiency, an autosomal dominant disease which might lead to a hereditary thrombophilia.

Serpin Peptidase Inhibitor, Clade A Member 8 (SERPINA8), which is a pre-angiotensinogen or angiotensinogen precursor, is expressed in the liver and cleaved by the enzyme renin in response to lowered blood pressure. The ensuing product, angiotensin I, is at that point cleaved by angiotensin converting enzyme (ACE) to produce the physiologically active enzyme angiotensin II. SERPINA8 protein is involved in maintaining blood pressure and in the pathogenesis of essential hypertension and preeclampsia. SERPINA8 gene mutations are linked with susceptibility to essential hypertension, and may cause renal tubular dysgenesis, which is a severe disorder of renal tubular development. Defects in the SERPINA8 gene are also linked with non-familial structural atrial fibrillation, and inflammatory bowel disease.

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.

ABHD14B is a member of the AB hydrolase superfamily. ABHD14B has an alpha/beta hydrolase fold - a catalytic domain found in a large number of enzymes. In molecular biology, the alpha/beta hydrolase fold is common to a number of hydrolytic enzymes of broad differing phylogenetic source and catalytic function. The Ab hydrolase domain containing gene subfamily includes 15 mostly uncharacterized members. ABHD14B has hydrolase activity with p-nitrophenyl butyrate (in vitro) and is able to activate transcription.

Beta-lactamase is a type of enzyme (EC 3.5.2.6) produced by some bacteria that is responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins, cephamycins and carbapenems. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties.

6PGD is the second dehydrogenase in the pentose phosphate shunt. Pentose is neccesary for nucleic acid biosynthesis. The pentose phosphate cycle is a major source of NADPH 6PGD deficiency is usually asymptomatic, and the inheritance of this disorder is autosomal dominant. PGD deficiency raises the erythrocyte pyruvate kinase levels of activity and decreases glutathione synthetase, resulting in hemolysis.

GlpK also known as glycerol kinase, is a member of the FGGY kinase family. GlpK catalyzes the transfer of a phosphate group from ATP to glycerol, thereby forming glycerol phosphate. Furthermore, this intermediate can then be converted to dihydroxyacetone phosphate (DHAP), which is utilized in either glycolysis or gluconeogenesis. The activity of GlpK is affected by numerous metabolites. The non-competitive allosteric inhibition by fructose 1,6-bisphosphate (FBP) triggers modifications in the quaternary structure of Glpk.

SULT2B1 catalyzes the sulfate conjugation of numerous hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation enhances the water solubility of molecules, and therefore their renal excretion, however it can also result in bioactivation to form active metabolites. SULT2B1b is localized in the cytosol and nuclei of human cells. SULT2B1b is selective for the sulfation of 3beta-hydroxysteroids such as dehydroepiandrosterone and pregnenolone, and participates in cholesterol sulfation in human skin.

ICAM-1 also called CD54 is a single chain membrane glycoprotein expressed on the surface of a variety of non-haematopoietic and haematopoietic cell types and has roles in signal transduction, cell signaling and lymphocyte adhesion. ICAM1 binds to integrins such as CD11a / CD18, or CD11b / CD18. ICAM1 is also used by Rhinovirus as a receptor. ICAM-1 is an intercellular adhesion molecule constantly present in low concentrations in the membranes of leukocytes and endothelial cells. When stimulated by cytokine the concentrations significantly increase. ICAM-1 can be stimulated by interleukin-1 (IL-1) and tumor necrosis factor alpha (TNFA) and is expressed by the vascular endothelium, macrophages and lymphocytes. ICAM-1 is a ligand for LFA-1 which is a receptor found on leukocytes. Upon activation, leukocytes bind to endothelial cells via ICAM-1/LFA-1 and then transmigrate into tissues.
ICAM-1 is implicated in subarachnoid hemorrhage (SAH). Levels of ICAM-1 are shown to be notably elevated in patients with SAH.
Soluble ICAM-1 is detectable in the plasma and is elevated in patients with various inflammatory conditions.

Putative peptidyl-tRNA hydrolase PTRHD1 (PTRHD1) is a 140 amino acid protein, which is encoded by a gene located on human chromosome 2p23.3. Chromosome 2 is the second largest human chromosome; it consists of 237 million bases, encodes over 1,400 genes and makes up approximately 8% of the human genome. Several genetic diseases are linked to genes on chromosome 2.

GMP synthase (GMPS) is involved in purine biosynthesis. GMPS, which is a homodimer, catalyzes the last step in the GMP synthesis pathway, specifically the ATP-dependent amination of XMP to GMP. GMPS is comprised of one GMP-binding domain and one glutamine amidotransferase type-1 domain through which it communicates its catalytic activity. GMPS is engaged in the de novo synthesis of nucleotides which are not only vital for DNA and RNA synthesis, but also supply GTP, which is involved in sevral cellular processes important for cell division. GMPS gene chromosomal translocations are linked with acute myeloid leukemias, suggesting a possible role for GMPS in carcinogenesis.

GHBP is a transmembrane receptor for growth hormone. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon three and has been well-characterized. Mutations in this gene have been associated with Laron syndrome, also known as the growth hormone insensitivity syndrome (GHIS), a disorder characterized by short stature. Other splice variants, including one encoding a soluble form of the protein (GHRtr), have been observed but have not been thoroughly characterized.

Inositol oxygenase is a non-heme di-iron enzyme which oxidizes myo-inositol to glucuronic acid. In addition, inositol oxygenase oxidizes the less abundant chiro isomer of inositol. MIOX enzyme is a component of the only known pathway for the catabolism of inositol in humans. MIOX is expressed mostly in the kidneys. Reduction of Inositol Oxygenase and accumulation of polyols, such as inositol and xylitol, have been implicated as contributing factors in complications linked with diabetes.

SORBS3 is an SH3 domain-containing adaptor protein. The existence of SH3 domains in the SORBS3 protein have a role in its capability to attach to other cytoplasmic molecules and contribute to cystoskeletal organization, cell adhesion and migration, signaling, and gene expression. Various transcript variants encoding different isoforms are known for this gene.

NFNB demonstrates the capability to reduce quinines. NFNB enzyme activates prodrugs in antibody directed enzyme prodrug therapy. NFNB reduces nitrofurazone, quinones and anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species.

Kallikrein-3 (KLK3) belongs to the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved 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 is assumed to act 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.

PHPT1 is a member of the Janus protein familyand is 125 amino acid long. PHPT1 appears as a monomer in the cytoplasm and is an EDTA-insensitive phosphohistidine phosphatase. Overexpression of PHPT1 resolts in specific phosphohistidine phosphatase activity towards phosphopeptide I, with no activity detected towards phosphotyrosine, phosphothreonine and phosphoserine peptides.

Catalase (CAT) is a key antioxidant enzyme in the body’s defense against oxidative stress. Furthermore, Catalase is a heme enzyme which is present in the peroxisome of virtually all aerobic cells. Catalase converts the reactive oxygen species hydrogen peroxide to water and oxygen and thus diminishes the toxic effects of hydrogen peroxide. Catalase stimulates growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells. Catalase gene polymorphisms are linked with decreases in catalase activity nevertheless, to date, acatalasemia is the only disease known to be caused by the CAT gene.

Short/branched chain specific acyl-CoA dehydrogenase (ACADSB) belongs to the acyl-CoA dehydrogenase family of enzymes which catalyze the dehydrogenation of acyl-CoA derivatives in the metabolism of fatty acids or branch chained amino acids. ACADSB catalyzes the degradation of L-isoleucine while having the highest affinity for (s)-2-methylbutyryl-CoA, isobutyryl-CoA and 2-methylhexanoyl-CoA as substrates. ACADSB may use valproyl-CoA as substrate. ACADSB gene defects cause the short/branched-chain acyl-CoA dehydrogenase deficiency (SBCADD), which is an autosomal recessive disorder characterized by an increase of 2-methylbutyrylglycine and 2-methylbutyrylcarnitine in blood and urine.

Monoamine Oxidase A, also known as MAOA catalyzes the oxidative deamination of biogenic as well as xenobiotic amines and has significant functions in the metabolism of neuroactive and vasoactive amines in the central nervous system as well as peripheral tissues. Mutation in MAOA results in Brunner syndrome; in addition MAOA has also been linked with a diversity of other psychiatric disorders, which includes antisocial behavior. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT).

Plasminogen activator inhibitor-1 is the principal inhibitor of tissue plasminogen activator(tPA) and uPA, the activators of plasminogenand hence fibrinolysis(the physiological breakdown of blood clots). It is a serine protease inhibitor(serpin) protein (SERPINE1). The other PAI, plasminogen activator inhibitor-2(PAI-2) is secreted by the placentaand only present in significant amounts during pregnancy. In addition, protease nexinacts as an inhibitor of tPA. SERPINE1, however, is the main inhibitor of the plasminogen activators.

Paraoxonase 2 (PON2) is a member of a multigene family whose genes share 65% identity at the amino acid level, and is expressed in a variety of tissues, including the pancreas. PON2 overexpression has been shown to lower the intracellular oxidative state and reduce the cells ability to oxidize LDL. PON2 is therefore implicated in the modulation of oxidative stress.

Glutathione reductase (GSR) belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. The GSR enzyme is a homodimeric flavoprotein and has a role in maintaining glutathione (GSH) in its reduced form by catalyzing the reduction of glutathione disulfide (GSSG): GSSG + NADPH + H+ ->2GSH + NADP+. In the majority of eukaryotic cells, GSR upholds the ratio of [GSH] / [GSSG], and partakes in quite a few critical functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis.