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Asparagine synthetase (ASNS) is a cytoplasmic enzyme that turns aspartate toasparagine and functions mostly in mammalian organs. ASNS is responsible for cell growthand its mRNA content is associated with changes in the cell cycle. ASNS may also play a role as a biomarker for ovarian cancer.

OGG1 is a DNA glycosylase enzyme which takes part in base excision repair. OGG1 protein is the main enzyme accountable for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which arises as a result of exposure to reactive oxygen species (ROS). OGG1 shows beta lyase activity that nicks DNA 3'' to the lesion.

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.

PCBD1 enzyme takes part in phenylalanine hydroxylation. PCBD1 deficiency results in hyperphenylalaninemia. PCBD1 enzyme controls the homodimerization of HNF1. PCBD1 takes part in tetrahydrobiopterin biosynthesis. PCBD1 prevents the formation of 7-pterins and accelerate the formation of quinonoid-BH2. PCBD1 is a coactivator for HNF1A-dependent transcription.

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.

Phosphoribosyl Pyrophosphate Synthetase 2, also known as PRPS2 is a member of the ribose-phosphate pyrophosphokinase family. PRPS2 catalyzes the synthesis of 5-phosphoribosyl 1-pyrophosphate from ATP and D-ribose 5-phosphate.

Rhodanese is a mitochondrial matrix enzyme that is encoded by the nucleus. Rhodanese is involved in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes. Rhodanese catalyzes the chemical reaction of thiosulfate & cyanide to sulfite & thiocyanate (detoxification). Rhodanese is part of the transferase family of proteins. Rhodanese includes two highly conservative domains, identified as rhodanese homology domains. In mammals, the majority of cyanide is converted to thiocyanate. Rhodanese has weak mercaptopyruvate sulfurtransferase activity.

PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.

HIBCH enzyme is in charge of hydrolysis of both HIBYL-CoA and beta-hydroxypropionyl-CoA. Damages in the HIBCH gene linked to 3-hyroxyisobutyryl-CoA hydrolase deficiency. Multiple transcript variants exist as a result of alternative splicing.

Arylsulfatase A (ARSA) hydrolyzes cerebrosidesulfate to cerebroside and sulfate. ARSA is inhibited by phosphate. The phosphate develops a covalent bond with the active site 3-oxoalanine. ARSA gene defects cause metachromatic leucodystrophy (MLD), a progressive demyelination disease which results in various neurological symptoms and ultimately death.

D-gluconate kinase or idnk is a thermosensitive protein, consists of 187 a.a and part of the gluconokinase gntK/gntV protein family. Idnk enhances the conversion of ATP + D-gluconate => ADP + 6-phospho-D-gluconate. Idnk has a crucial part in determination of gender, removal of a certain portion of 9p may result in the making of male to female (reversal of sex), that leads to a female that has the genotype of male X, Y.

EEF1A1 is an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible forthe enzymatic release of aminoacyl tRNAs to the ribosome. EEF1A1 is expressed in brain, placenta, lung, liver, kidney, and pancreas, and the other isoform (alpha 2) is expressed in brain, heart and skeletal muscle. EEF1A1 is recognized as an autoantigen in 66% of patients with Felty syndrome. EEF1A1 has multiple copies on numerous chromosomes, part of them, if not all, symbolize different pseudogenes. Among the diseases associated with EEF1A1 are tinea nigra and andcervical cancer.

SULT1E1 catalyzes the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. Decreased SULT1E1 expression is linked with estrogen-dependent endometrial carcinomas. Altered cellular proliferation was detected in cells stably expressing SULT1E1.

BPHL is a Serine hydrolase that is a part of the AB hydrolase superfamily which catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs. BPHL is expressed large quantities in liver and kidney and in minor quantities in heart, intestine and skeletal muscle. BPHL takes part in detoxification processes and is a specific alpha-amino acid ester hydrolase which favors small, hydrophobic, and aromatic side chains and does not have a strict necessity for the leaving group except for favoring a primary alcohol.

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.

Glucosidase Beta Acid 3, also known as GBA3, hydrolyzes various types of glycosides. GBA3 takes part in a nonlysosomal catabolic pathway of glycosylceramide. GBA3 is a protein coding gene which acts as beta-glycosylceramidase.

Alpha-galactosidase A (GLA) is a homodimeric glycoprotein which hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. GLA catalyzes the hydrolysis of melibiose into galactose and glucose. Various mutations in the GLA gene affect the synthesis, processing, and stability of this enzyme, which causes Fabry disease (a rare lysosomal storage disorder which results from a failure to catabolize alpha-D-galactosyl glycolipid moieties).

Thiosulfate Sulfurtransferase Like Domain Containing 3, also known as TSTD3 contains 1 rhodanese domain which is characterized by an active site cysteine residue that has the ability to bind sulfane sulfur and catalyse sulfur transfer.

Glycogen phosphorylase is one of the phosphorylaseenzymes(EC2.4.1.1). It breaks up glycogeninto glucosesubunits. Glycogenis left with one less glucosemolecule, and the free glucosemolecule is in the form of glucose-1-phosphate. In order to be used for metabolism, it must be converted to glucose-6-phosphateby the enzyme phosphoglucomutase.
Glycogen phosphorylase can only act on linearchainsof glycogen(a 1-4 glycosidic linkage). Its work will immediately come to a halt four residues away from a 1-6 branch(which are exceedingly common in glycogen). In these situations, a debranching enzymeis necessary, which will straighten out the chain in that area. Additionally, an alpha 1-6 glucosidaseenzymeis required to break the remaining 1-6 residue that remains in the new linear chain. After all this is done, glycogen phosphorylase can continue.
An insulinstimulated enzyme known as phosphoprotein phosphatase(PP-1) inactivates glycogen phosphorylase to prevent glycogen break up.
GPBB - a sensitive marker for the AMI diagnosis within 4 hours after the onset of chest pain. It has also been shown that GPBB is increased in a considerable proportion of AMI patients within 2-3 hours from chest pain onset. GPBB is increased early in patients with unstable angina. GPBB can also be a sensitive marker for the detection of peri-operative myocardial ischaemia and infarction in patients undergoing coronary artery bypass grafting.

PTGES2 is a membrane-associated prostaglandin E synthase, which catalyzes the conversion of prostaglandin H2 to prostaglandin E2. Additionally, PTGES2 activates the transcription regulated by a gamma-INF-activated transcription element. PTGES2 is widely expressed- in the heart, including apex, inter-ventricular septum, both atria and ventricles, but not in the aorta. PTGES2 is also expressed in fetal heart. PTGES2 is detected in various regions of the brain: cerebellum; occipital, frontal and parietal lobes. It is also expressed in the lymph nodes, skeletal muscle, kidney and trachea, but not in the thymus or lung. PTGES2 is overexpressed in colorectal cancer.

Glutathione S-transferase Mu 2 (GSTM2) belongs to the glutathione s-transferase (GST) family of proteins. GSTM2 is a glutathione S-transferase that belongs to the mu class. There are 8 families of GST proteins, specifically: alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is composed of proteins that have various functions throughout the cell. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are structured in a gene cluster on chromosome 1p13.3 and are proven to be highly polymorphic. These genetic variants can change an individual''s susceptibility to carcinogens and toxins as well as have an effect on the toxicity and efficacy of several drugs.

GSTO1 belongs to the theta class glutathione S-transferase-like (GSTTL) protein family. GSTO1 is expressed in a broad array of human tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities as well as catalyzing the reduction of monomethylarsonate which is an intermediate in the pathway of arsenic biotransformation. Furthermore, GSTO1 shields from oxidative stress which is a risk factor for Alzheimer disease, vascular dementia and stroke. GSTO1 is abundant in alveolar macrophages and airway secretions, with the levels reduced in chronic obstructive pulmonary disease patients. In mouse, the GSTO1 protein acts as a small stress response protein, probably involved in cellular redox homeostasis.

MDH2 catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in the citric acid cycle. MDH2 is localized to the mitochondria and takes part in the malate-aspartate shuttle that functions in the metabolic coordination between cytosol and mitochondria. MDH2 is highy expressed in the adrenal system, small intestine, heart and pancreas.