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ST6GAL1 also known as ST6 Beta-Galactosamide Alpha-2,6-Sialyltranferase 1, is part of the glycosyltransferase family 29. ST6GAL1 is a type II membrane protein which catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. Furthermore, ST6GAL1 is normally found in the Golgi however it can be proteolytically processed to a soluble form, ST6GAL1 is also involved in the generation of the cell-surface carbohydrate determinants as well differentiation antigens HB-6, CD75, and CD76.

O-Sialoglycoprotein Endopeptidase, also known as OSGEP is a member of the KAE1 / TsaD family. OSGEP is essential for the formation of threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs which read codons beginning with adenine. OSGEP take a direct catalytic part in the above reaction, however other proteins of the complex are required to fulfill this activity.

L-threonine to glycine degradation consists of a two-step biochemical pathway which involvs the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is initially converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. Glycine C-Acetyltransferase (GCAT) is the 2nd enzyme in this pathway, which subsequently catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The GCAT enzyme is regard as a class II pyridoxal-phosphate-dependent aminotransferase. GCAT is strongly expressed in the heart, brain, liver and pancreas. GCAT is also found in lung.

GGCT is a member of the family of transferases, specifically the aminoacyltransferases. GGCT protein catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and takes an important part in glutathione homeostasis. GGCT induces release of cytochrome c from mitochondria with resultant induction of apoptosis.

QPRT is a key enzyme in the catabolism of quinolinate. QPRT is in between the tryptophannicotinamide adenine dinucleotide (NAD) pathway, resulting in the production of nicotinic acid, carbon dioxide and pyrophosphate. Rise of QPRT levels in the brain is related to the pathogenesis of neurodegenerative disorders such as epilepsy, Alzheimer's disease, and Huntington's disease.

MAT2B is part of the methionine adenosyltransferase family. MAT2B catalyzes the biosynthesis of S-adenosylmethionine from methionine and ATP. MAT2B is the regulatory beta subunit of MAT. MAT2B expression in hepatoma cell lines increases DNA synthesis and thus take part in cell proliferation.

Ubiquitin-conjugating enzyme E2 H (UBE2H) is a member of the ubiquitin-conjugating enzyme family. Protein modification with ubiquitin is a vital cellular apparatus for directing abnormal or short-lived proteins for degradation. Ubiquitination requires at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s) ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2H receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. UBE2H protein sequence is 100% identical to the mouse homolog and 98% identical to the frog and zebrafish homologs.

Ubiquitin-conjugating enzyme E2S (UBE2S) belongs to the ubiquitin-conjugating enzyme family. UBE2S is able to form a thiol ester linkage with ubiquitin in a ubiquitin activating enzyme-dependent manner, a typical property of ubiquitin carrier proteins. UBE2S catalyzes the covalent attachment of ubiquitin to other proteins. UBE2S acts as a crucial factor of the anaphase promoting complex/cyclosome (APC/C), which is a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. UBE2S acts by purposely elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, augmenting the degradation of APC/C substrates by the proteasome and promoting mitotic exit. UBE2S also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is nevertheless uncertain whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. UBE2S is also involved in ubiquitination and consequent degradation of VHL, resulting in an accumulation of HIF1A.

NADH Dehydrogenase 1 Beta Subcomplex 4 (NDUFB4) is a member of the complex I NDUFB4 subunit family. NDUFB4 is a non-catalytic subunit of the multisubunit NADH:ubiquinone oxidoreductase, which is the first enzyme complex in the mitochondrial electron transport chain (complex I). Mammalian complex I is comprised of 45 different subunits and transfers electrons from NADH to ubiquinone.

LYPLA1 is lysophospholipase which performs on biological membranes to regulate the multifunctional lysophospholipids. LYPLA1 protein hydrolyzes fatty acids from S-acylated cysteine residues in proteins like trimeric G alpha proteins or HRAS and in addition has depalmitoylating activity.

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.

NAA10 is a member of the acetyltransferase family. NAA10 interacts with NAA15, HIF-1 and with the ribosome. In its binding to HIF-1, NAA10 functions as a protein acetyltransferase by regulating its stability. In various cell lines, NAA10 is downregulated in response to hypoxia. NAA10 is expressed during the course of the development of the brain.

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).

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.

NNMT is part of the family of transferases, especially those transferring one-carbon group methyltransferases. NNMT is mostly expressed in the liver, and a lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. NNMT catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is significant for biotransformation of many drugs and xenobiotic compounds. NNMT is accountable for the enzymatic activity which uses S-adenosyl methionine as the methyl donor. NNMT expression is related with tumor stage and DFS time in hepatocellular carcinoma cases. NNMT is a good candidate as a tumor marker of various kinds of cancers. NNMT serum levels have significance in the premature detection and in the management of patients with colorectal cancer.

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.

Heparanase is an endo-β-D-glucuronidase, which degrades heparan sulfate side chains of heparan sulfate proteoglycans (HSPGs) in the extracellular matrix. Heparanase plays an important role in ECM degradation, facilitating the migration and extravasation of tumor cells and inflammatory leukocytes (1,2,3). Upon degradation, heparanase releases growth factors and cytokines that stimulate cell proliferation and chemotaxis (4,5). Heparanase is a heterodimer comprised of a 50 kDa subunit harboring the active site and a 8 kDa subunit. It is produced as a latent 65 kDa precursor and proteolytically processed to its active form (1,6). Heparanase is highly expressed in myeloid leukocytes (i.e. neutrophils) in platelets and in human placenta. Human heparanase was found to be upregulated in various types of primary tumors, correlating in some cases with increased tumor invasiveness and vascularity and with poor prospective survival (7,8).

Matrix metalloproteinase-14 (MMP14), is a membrane-anchored zinc-binding endopeptidase which is expressed at the leading edge of different invasive carcinomas and also promotes tumor cell invasion through degradation of the extracellular matrix. MMP14 takes a vital part in extracellular matrix, ECM, remodeling by having the capability to degrade type I collagen, activate pro-MMP-2 and process cell adhesion molecules for instance CD44 and integrin alpha V. MMP14 is a key enzyme in many physiological as well as pathological processes for example angiogenesis & tumor invasion.

Aminoacyl-tRNA synthetases are a class of enzymes which charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase (NARS) is localized to the cytoplasm and is a member of the class II family of tRNA synthetases. The N-terminal domain characterizes the signature sequence for the eukaryotic asparaginyl-tRNA synthetases.

Polyribonucleotide nucleotidyltransferase 1, also known as PNPT1 is predominantly localized in the mitochondrial intermembrane space and is implicated in the import of RNA to mitochondria. Mutations in PNPT1 have been connected with combined oxidative phosphorylation deficiency-13 as well as autosomal recessive nonsyndromic deafness-70. Related pseudogenes have been found on chromosomes 3 & 7.

PLA2G7 is a secreted enzyme which catalyzes the degradation of platelet-activating factor to biologically inactive products. The PLA2G7 enzyme is produced by inflammatory cells and hydrolyzes oxidised phospholipids in LDL. In the blood, PLA2G7 goes mainly with LDL and less than 20% is coupled with HDL.
PLA2G7 is implicated in the development of atherosclerosis and is also a marker for cardiac disease. PLA2G7 might have a major physiologic effect in the presence of inflammatory bodily responses.
PLA2G7 alters the action of PAF (platelet-activating factor) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. PLA2G7 has specificity for substrates with a short residue at the sn-2 position. PLA2G7 is inactive against long-chain phospholipids.
PLA2G7 gene defects are the source of platelet-activating factor acetylhydrolase deficiency, which is a trait that is present in 27% of the Japanese population.

Alanyl-tRNA synthetase is a member of the aminoacyl-tRNA synthetase family, key enzymes of protein biosynthesis which charge tRNA molecules with the respective amino acids. This 108 kDa protein is an autoantigen recognized by PL-12 antibodies which occur in a subset of patients with polymyositis and dermatomyositis. Preliminary data suggest that epitope spreading occurs in the autoimmune PL-12 response such that even antibodies to an isolated alanyl-tRNA molecule can develop.

Methionine sulfoxide reductase B3 (MSRB3) is a member of the methionine sulfoxide reductases (MSR) family proteins. MSRB3 catalyzes the reduction of methionine sulfoxide to methionine. The MSRB3 enzyme acts as a monomer and requires zinc as a cofactor. MSRs are thought to defend against reactive oxygen species-induced oxidative damage in various organs, including the most environmentally exposed organ, the human skin. MSRB3 has a vital role in cold tolerance by eliminating MetO and ROS which accumulate at the ER during cold acclimation.

NNMT is part of the family of transferases, especially those transferring one-carbon group methyltransferases. NNMT is mostly expressed in the liver, and a lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. NNMT catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is significant for biotransformation of many drugs and xenobiotic compounds. NNMT is accountable for the enzymatic activity which uses S-adenosyl methionine as the methyl donor. NNMT expression is related with tumor stage and DFS time in hepatocellular carcinoma cases. NNMT is a good candidate as a tumor marker of various kinds of cancers. NNMT serum levels have significance in the premature detection and in the management of patients with colorectal cancer.