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Polypeptide N-Acetylgalactosaminyltransferase 1 (Galnt1) , is part of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. The initial reaction in O-linked oligosaccharide biosynthesis is catalyzed by Glant1, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Moreover, Galnt1 is implicated in the glycosylation of proteins vital for bone formation for instance osteopontin and bone sialoprotein.

Obg-like ATPase 1 (OLA1) acts as a negative regulator of the cellular antioxidant response independent of transcriptional processes. OLA1 curbs the antioxidant response via nontranscriptional mechanisms. OLA1 hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. OLA1 is clearly down-regulated by DNA damage-inducing agents. OLA1 is expressed in all tissues; however it is more abundant in the testis, liver, lung, and brain. OLA1 is overexpressed in a number of malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus.

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.

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.

Dehydrogenase/reductase SDR family member 8 (HSD17B11) is a member of the HSD17B family of proteins, which regulate the availability of steroids within various tissues throughout the body. HSD17B11 is widely expressed with the highest levels found in the retina, pancreas, kidney, liver, lung, adrenal, small intestine, ovary and heart as well as in steroidogenic cells. HSD17B11 converts androstan-3-?,17-?-diol (3-?-diol) to androsterone, suggesting it may participate in androgen metabolism during steroidogenesis.

BLVRB (EC 1.3.1.24) catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. BLVRB is involved in protecting cells from oxidative damage or in regulating iron metabolism. BLVRB converts biliverdin to bilirubin in the liver, converting a double-bond between the second and third pyrrole ring into a single-bond. BLVRB plays a role as in human erythrocytic heme catabolic pathway and most mammalian species. Biliverdin reductase is abundantly expressed in kidney, spleen, liver and brain as well as at lower levels in the thymus and minimal levels being detected in testis.

NAT6 is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to acrylamines. NAT6 is located mainly in the cytoplasm and its activity has been recognized by its feasibility to acetylate the N-terminus of proteins using a ping-pong-like mechanism and by its substrate specificity. Given that the NAT6 gene maps to the chromosomal region 3p21.3, which includes at least one tumor suppressor gene, the function of NAT6 plays an important role in cancer.

AKR1A1 is part of the aldo/keto reductase superfamily, it catalyzes the NADPH-dependent reduction from a range of aromatic and aliphatic aldehydes to their related alcohols. AKR1A1 corresponds (65% identity) to aldose reductase, an enzyme that takes part in the pathogenesis of some diabetic and galactosemic complications. AKR1A1 is involved in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs.

ACADVL is an inner mitochondrial membrane enzyme that is part of the family of acyl-CoA dehydrogenases. ACADVL protein participates in lipid metabolism and has catalytic activity toward esters of long chain and very long chain fatty acids such as palmitoyl-CoA and stearoyl-CoA, and is involved in the first step of the fatty acid β-oxidation pathway. ACADVL deficiency in reduces myocardial fatty acid beta-oxidation and is related with cardiomyopathy.

CysH (Phosphoadenosine phosphosulfate reductase) is a member of the PAPS reductase family, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The 3 substrates of the CysH enzyme are adenosine 3',5'-bisphosphate, sulfite, and thioredoxin disulfide, whereas its two products are 3'-phosphoadenylyl sulfate and thioredoxin.

Phosphomannomutase 1 (PMM1) is an enzyme involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. PMM1 catalyzes the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for the synthesis of dolichol-phosphate-mannose, which is crucial for N-linked glycosylation and accordingly the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol (GPI) anchored proteins. Additionally, PMM1 may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.

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.

THTPA enzyme is part of the THTPase family. THTPA is localized to the cytoplasm and expressed at small quantities in a variety of tissues, including testis, uterus, prostate, bladder, lung and kidney. THTPA is a hydrolase that catalyzes the H2O-dependent hydrolysis of thiamine triphosphate (THTP) to thiamine diphosphate (THDP), the main form of thiamine within the cell. THTPA occurs as a monomer and is activated at an optimal pH of 8.5.

GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.

ALDOB is a tetrameric glycolytic enzyme which catalyzes the reversible cleavage of fructose 1-phosphate into dihydroxyacetone phosphate and glyceraldehyde. Fructose-bisphosphate aldolase B (ALDOB) is one of 3 known aldolase isoenzymes, and is located in the kidney and the small adult intestine where it is linked with aldolases A or C. ALDOB is regulated by Insulin and glucagon and is implicated in hereditary fructose intolerance disease.

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 (NDUFA5) is a member of the complex I NDUFA5 subunit family. The human NDUFA5 gene codes for the B13 subunit of complex I of the respiratory chain that transfers electrons from NADH to ubiquinone. The NDUFA5 protein localizes to the inner mitochondrial membrane as part of the seven component-containing, water soluble 'iron-sulfur protein' (IP) fraction of complex I, even though its exact role is undetermined.

Membrane-bound & Cytosolic forms of GST are encoded by 2 separate supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. There are 8 different classes of soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The GSTA1 is found in a cluster mapped to chromosome 6, and is highly expressed in the liver. GSTA1 protects the cells from reactive oxygen species.

CA14 is a part of the Carbonic anhydrases family. Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. They present wide variety in tissue distribution and in their subcellular localization. CA14 is a type I membrane protein which shares highest sequence similarity with the other transmembrane CA isoform, CA XII. Nevertheless, they have different patterns of tissue-specific expression and therefore take different physiologic parts.

Carbonic anhydrase (carbonate dehydratase) is a family of metalloenzymes (enzymes that contain one or more metal atoms as a functional component of the enzyme) that catalyze the rapid (and reversible) conversion of carbon dioxide to bicarbonate and protons, a reaction that occurs rather slowly in the absence of a catalyst. Carbonic anhydrase greatly increases the rate of the reaction, with typical catalytic rates of the different forms of this enzyme ranging between 104 and 106 reactions per second. The active site of most carbonic anhydrases contains a zincion. CAIII is a cytoplasmic isoenzyme, but is released into the circulation following injury.

Acy1 or Aminoacylase1 is a cytosolic, homodimeric, zinc-binding enzyme which catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been suggested to operate in the catabolism and salvage of acylated amino acids. ACY1 is localized in chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been observed to be reduced or undetectable in SCLC cell lines and tumors.

PCYT2 is a member of the cytidylyltransferase family. PCYT2 is an enzyme which catalyzes the formation of CDP-MEA from CTP and phospho MEA in the Kennedy pathway of phospholipid synthesis. PCYT2 has the strongest expression in the liver, heart, and skeletal muscle.

GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 takes part in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and demonstrate close homology.

Tyrosyl-tRNA synthetase (YARS2) is a mitochondrial protein which catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and afterward transferred to the acceptor end of tRNA(Tyr). YARS2 gene mutations are linked with myopathy with lactic acidosis and sideroblastic anemia type 2 (MLASA2).

Metalloproteinase inhibitor 4 (TIMP4) is a member of a family of secreted proteins which regulate the activation and proteolytic activity of the zinc enzymes known as matrix metalloproteinases. The four known members of this family are TIMP1, 2, 3 and 4. TIMP4 is produced by various tissues, particularly the brain, heart, ovary and skeletal muscle. Limited studies have shown that the TIMP4 protein has a tumor suppressive effect against Wilm92s tumor, exhibiting a negative correlation with glioma malignancy and is found in breast carcinoma cells.