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GLRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GLRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.

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.

UBE2N belongs to the E2 ubiquitin-conjugating enzyme family. UBE2N catalyzes the ATP-dependent synthesis of non-canonical polyubiquitin chains, a process which doesn’t set in motion proteasomal degradation. UBE2N mediates the transcription of some target genes and is believed to have a role in cell cycle progression; cellular differentiation and DNA repair mechanisms which ensure cell survival after DNA damage.

Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.

The Proteinase K enzyme is a member of the Peptidase family S8. Proteinase K is a broad-spectrum serine protease. Proteinase K is capable of digesting hair (keratin), henceforth, the name "Proteinase K". Proteinase K is activated by calcium, the enzyme digests proteins especially after hydrophobic amino acids (aliphatic, aromatic and other hydrophobic amino acids). Proteinase K is frequently utilized in molecular biology to digest protein and remove contamination from preparations of nucleic acid. Addition of Proteinase K to nucleic acid preparations rapidly inactivates nucleases which may otherwise degrade the DNA or RNA during purification. Proteinase K is greatly fitting to this application as the enzyme is active in the presence of chemicals which denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is utilized for the destruction of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids, given that it quite effectively inactivates DNases and RNases.

ACADM enzyme is essential for the degradation a certain group of fats called medium-chain fatty acids. ACADM is essential for converting specific fatty acids to energy, mainly during fasting periods. ACADM functions in mitochondria, the energy-producing centers within cells. ACADM is localized in the mitochondria of numerous tissue types, predominantly the liver.

AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.

GZMK is a part of a group of related serine proteases from the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes and natural killer cells have the outstanding ability to bind, recognize and lyse specific target cells. They defend their host by lysing cells bearing on their surface 'nonself' antigens, usually peptides or proteins resulting from infection by intracellular pathogens.

GALK1 enzyme is needed in the first step of the galactose metabolism pathway.
(ATP + D-galactose = ADP + alpha-D-galactose 1-phosphate). GALK1 deficinecy lead galactosemia II which is an autosomal recessive deficiency known by congenital cataracts during infancy and presenile cataracts in the adult population. The cataracts are secondary to accumulation of galactitol in the lenses.

Mimitin (NDUFAF2) is a member of the complex I NDUFA12 subunit family.NADH dehydrogenase is an enzyme located in the inner mitochondrial membrane, which catalyzes the transfer of electrons from NADH to coenzyme Q (CoQ). NDUFAF2 is the "entry enzyme" of oxidative phosphorylation in the mitochondria. Mimitin protein functions as a molecular chaperone for mitochondrial complex I assembly.

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.

PRPS1 catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. PRPS1 catalyzes the phosphoribosylation of ribose 5-phosphate to 5-phosphoribosyl-1-pyrophosphate, which is essential for purine metabolism and nucleotide biosynthesis. Defects in PRPS1 result in phosphoribosylpyrophosphate synthetase superactivity, Charcot-Marie-Tooth disease X-linked recessive type 5 and Arts Syndrome.

Proteasome subunit alpha type-8 (PSMA8) is a member of the peptidase T1A family. PSMA8 is a multicatalytic proteinase complex which is distinguished by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. The PSMA8 subunit may be testis-specific.

LPL is a lipoprotein lipase, which is expressed in the heart, muscle, and adipose tissue. LPL acts as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Type I hyperlipoproteinemia is a result of severe mutations which cause LPL deficiency, whereas less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism. Lipoprotein lipase (LPL) is a fundamental enzyme in plasma triglyceride hydrolysis and is secreted by macrophages in the subendothelial space. LPL also promotes the development of atherosclerosis through facilitation of monocyte adhesion to endothelial cells, stimulation of tumor necrosis factor alpha (TNF) secretion and induction of vascular smooth muscle cell proliferation.

ALKBH2 is a member of the ALKB family.ALKBH2 is expressed in the heart, colon, liver, testis, ovary, prostate and the small intestine. ALKBH2 uses iron as a cofactor and acts as a dioxygenase which catalyzes the repair of alkylated DNA and RNA containing 1-methyladenine and 3-meth-ylcytosine. ALKBH2 is functionally activated by ascorbate and requires oxygen and ?-ketoglutarate for enzymatic activity.

Protein Tyrosine Phosphatase Type IVA Member 3 (PTP4A3) is a member of a small class of prenylated protein tyrosine phosphatases (PTPs) which remove phosphate modifications from tyrosine residues on proteins. PTP4A3 enhances cell proliferation, cell motility and invasive activity. PTP4A3 functions as a protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. PTP4A3 is mostly expressed in cardiomyocytes and skeletal muscle; it is also found in the pancreas.
PTP4A3 is always overexpressed in colon cancer metastasis. PTP4A3 is notably overexpressed in liver metastasis of colorectal cancer. High levels of PTP4A3 expression are linked to tumorigenesis and metastasis; therefore it is overexpressed in metastatic colorectal, ovarian, liver and skin cancers. PTP4A3 may be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II. PTP4A3 is inhibited by sodium orthovanadate and peroxovanadium compounds.

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.

Candida albicans is a diploid fungus, which grows both as yeast and filamentous cells and a contributory agent of opportunistic oral and genital infections in humans, and candidal onychomycosis (an infection of the nail plate). Systemic fungal infections (fungemias) including those by C. albicans are regarded as key causes of morbidity and mortality in immunocompromised patients (e.g., AIDS, cancer chemotherapy, organ or bone marrow transplantation). C. albicans biofilms may develop on the surface of implantable medical devices. C. albicans is commensal and a constituent of the normal gut flora containing microorganisms which live in the human mouth and gastrointestinal tract. Overgrowth of the fungus leads to in candidiasis (candidosis). Candidiasis is frequently detected in immunocompromised persons, including HIV-infected patients. To infect host tissue, the habitual unicellular yeast-like form of C. albicans reacts to environmental signals and changes into an invasive, multicellular filamentous form, a phenomenon which is known as dimorphism.

Adenosine Kinase is an abundant enzyme in mammalian tissues which catalyzes the transfer of the gamma-phosphate from ATP to adenosine, thus is as a regulator of concentrations of both extracellular adenosine and intracellular adenine nucleotides. Adenosine has extensive effects on the cardiovascular, nervous, respiratory, and immune systems and inhibitors of the enzyme take a crucial pharmacological part in growing intravascular adenosine concentrations and acting as anti-inflammatory agents.

AKR7A2 participates in the detoxification of aldehydes and ketones. AKR7A2 catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. AKR7A2 is involved in producing the neuromodulator gamma-hydroxybutyrate (GHB). AKR7A2 has extensive substrate specificity. AKR7A2 shows NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2 reduces 1,2-naphthoquinone and 9,10-phenanthrenequinone (in vitro). AKR7A2 reduces the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. AKR7A2 takes part in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.

ALDH2 is part of the aldehyde dehydrogenase family of proteins which catalyze the chemical transformation from acetaldehyde to acetic acid. ALDH2 is the second enzyme of the major oxidative pathway of alcohol metabolism. ALDH2 has 2 major liver isoforms: cytosolic and mitochondrial, which differ by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Nearly all Caucasians have 2 major isozymes, whereas roughly 50% of Orientals have only the cytosolic isozyme, omitting the mitochondrial isozyme. The extremely higher rate of acute alcohol intoxication with Orientals compared to Caucasians is due to the fact of the absence of mitochondrial isozyme. ALDH2 has a low Km for acetaldehydes, and is localized in mitochondrial matrix.

ECH1 is a member of the hydratase/isomerase superfamily. ECH1 demonstrates high sequence similarity to enoyl-coenzyme A (CoA) hydratases of more than a few species, mostly within a conserved domain characteristic of these proteins. ECH1 contains a C-terminal peroxisomal targeting sequence, localizes to both the peroxisome and the mitochondria. peroxisomal takes part in the auxiliary step of the fatty acid beta-oxidation pathway specifically functioning to catalyze the isomerization of 3-trans, 5-cis-dienoyl-CoA to 2-trans, 4-transdienoyl-CoA.

Coagulation factor VIII participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder.