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Creatine Kinase MM is a cytoplasmic enzyme involved in energy homeostasis and is an important serum marker for myocardial infarction. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in striated muscle as well as in other tissues, and as a heterodimer with a similar brain isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family.

Adenylate kinases play a role in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. There are 3 types of adenylate kinase isozymes, AK1, AK2, and AK3 in vertebrates. Expression of these isozymes are tissue-specific and developmentally regulated. AK2 is localized in the mitochondrial intermembrane space and is involved in apoptosis. AK2 is mutated in individuals with reticular dysgenesis.

This E2 enzyme encodes for the human homolog of the yeast DNA repair gene RAD6, which is induced by DNA damaging agents. UBE2B can conjugate ubiquitin to histone H2A in an E3- independent manner in vitro, and is essential for the multi-ubiquitination and degradation of N-end rule substrates. Additionally, UBE2B may have a role in sepsis-induced muscle protein proteolysis and cancer-induced cachexia.

Kallikrein-15 (KLK15) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. KLK15 contains numerous polyadenylation sites and alternative splicing results in multiple transcript variants encoding different isoforms. KLK15 is over expressed in prostate cancer and therefore uses as a diagnostic or prognostic marker for prostate cancer.

UBE2E3 or Ubiquitin-conjugating enzyme E2 E3 is part of the E2 ubiquitinconjugating enzyme family. UBE2E3 is needed for the destruction of mitotic cyclins and for cell cycle progression. The ubiquitination process covalently attaches to a short protein of 76 amino acids called ubiquitin, to a lysine residue on the target protein. When a protein has been tagged with one ubiquitin molecule, other rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein which grants passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell.

Human Ubquitin Conjugating Enzyme 7 (UbcH7) is a class I enzyme which functions in the stress response and the control of transcription factors. The enzyme is ubiquitously expressed with high levels of expression seen in adult muscle. UbcH7 mediates the selective degradation of short-lived and abnormal proteins and is highly homologous to UbcH5. It has been demonstrated to participate in the ubiquitinylation of p53, c-Fos and NF-?B. UbcH7 is one of two E2s (UbcH5 being the other) with which HECT domain proteins interact with UbcH7 being able to efficiently substitute for UbcH5 in E6-AP-dependent ubiquitinylation.

Antioxidant enzyme Glutathione S- Transferase (GST) is thought to do the primary cellular defense mechanism against reactive oxygen species. GST reduces lipid hydroperoxides through its Se-independent glutathione peroxidase activity. The enzyme also detoxifies lipid peroxidation end products such as 4-hydroxynonenal (4-HNE).
The soluble GST is a 26 kDa protein which occurs as a dimer in all aerobic organisms. Each monomer has two domains, one that binds GSH and is an /-structure similar to thioredoxin and the other, all helical, that binds the hydrophobic substrate. The GST -fusion protein expression system is a widely used recombinant protein expression system that allows a peptide or a regulatory protein domain to be expressed as a fusion to the C-terminus of Schistosoma japonicum GST. Fusion proteins also possess GST -enzymatic activity and can undergo dimerization similar to in vivo. The fusion protein can be purified via GST -affinity column chromatography. In most cases, the desired peptides or domains are removed from GST by applying a specific protease that recognizes and cleaves the linker between the protein domain and GST. The technique has been widely used to generate different kinds of proteins for crystallization, molecular immunology studies, the production of vaccines and studies involving protein-protein and protein-DNA interactions.

Gltathione S-transferase PI 2, also known as GSTP2 is multifunctional enzyme which is involved in the protection of cellular components against anti-cancer drugs or peroxidative stress. Furthermore, down regulation of GSTP2 induces an increase of oxidative damage in the pyramidal cells of the CA1&CA3 regions as well as in the granular layer of the dentate gyrus, which at the end leads to structural and functional damage.

GSTT2 belongs to the glutathione s-transferase (GST) family of proteins. There are eight GST proteins families, named alpha, kappa, mu, omega, pi, sigma, theta and zeta. Each one of the GST families has several proteins with different functions throughout the cell. The theta type members GSTT1 and GSTT2 have a 55% aa sequence homology and hold a vital role in human carcinogenesis. The theta genes are structurally similar – each has five exons with identical exon/intron boundaries.

Tri a 14.0101 is a non-specific lipid transfer protein and a major wheat allergen. Those who are sensitive to this allergen may have baker’s asthma, a frequent occupational allergic disease caused mainly by inhalation of cereal flour, especially wheat flour. Tri a 14.0101 consists of 4 helical fragments and irregular C-terminal regions which are highly stable to heat treatment and proteolytic attack.

PPP1CC is vital for cell division and takes part in the regulation of protein synthesis, muscle contractility and glycogen metabolism. Additionally, PPP1CC has a role in long-term synaptic plasticity and regulation of ionic conductance, and has a significant role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II.

Glutathione S-transferase A4 (GSTA4) is a member of the GST superfamily. The GSTA4 enzyme is involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. GSTA4 shows an especially high activity with reactive carbonyl compounds such as alk-2-enals. GSTA4 is extremely effective in catalyzing the conjugate addition of reduced glutathione to 4-hydroxynonenal, which is an important product of peroxidative degradation of arachidonic acid and a frequently used biomarker for oxidative damage in tissue. The GSTA4 enzyme is expressed at a high level in the brain, placenta, and skeletal muscle and much lower in the lung and liver.

Cytochrome b5 reductase 2 (CYB5R2) is involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. CYB5R2 is responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1).

UBE2D1 is a member of the ubiquitin-conjugating enzyme family. Ubiquitination involves at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2D1 is strongly related to a stimulator of iron transport (SFT), and is up-regulated in hereditary hemochromatosis. In addition, UBE2D1 functions in the ubiquitination of the tumor-suppressor protein p53 and the hypoxia-inducible transcription factor HIF1alpha by interacting with the E1 ubiquitin-activating enzyme and the E3 ubiquitin-protein ligases.

Glutathione S-transferase mu 5 (GSTM5) belongs to the glutathione s-transferase (GST) family of proteins. There are 8 families of GST proteins, specifically alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is comprised of proteins which have various functions throughout the cell. GSTM5 belongs to the mu class of enzymes which function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. GSTM5 has an imperative role in detoxification. GSTM5 conjugates reduced glutathione to a large number of exogenous and endogenous hydrophobic electrophiles.

ATP synthase subunit O (ATP5O) localizes to the mitochondria and catalyzes ATP synthesis. ATP5O is a component of the F-type ATPase found in the mitochondrial matrix. F-type ATPases are composed of a catalytic core and a membrane proton channel. ATP5O seems to be part of the connector connecting these two components and may be involved in transmission of conformational changes or proton conductance.

Phosphoribosyltransferase domain-containing protein 1 (PRTFDC1) is a member of the purine/pyrimidine phosphoribosyltransferase family. PRTFDC1 has a low, barely measurable phosphoribosyltransferase activity (in vitro). PRTFDC1 can bind GMP, IMP and alpha-D-5-phosphoribosyl 1-pyrophosphate (PRPP). PRTFDC1 is not expected to impact purine metabolism or GMP salvage.

Protein tyrosine phosphatase mitochondrial 1 (PTPMT1) is a broadly expressed PTP membrane protein with high expression levels in pancreatic beta cells. The PTPMT1 protein is completely restricted to the matrix face of the inner membrane of the mitochondrion. PTPMT1 is responsible for dephosphorylating mitochondrial proteins and thus has a major role in the production of ATP. PTPMT1 exhibits a specific preference for the lipid signaling molecule phosphatidylinositol 5-phosphate as substrate.

Carbohydrate Sulfotransferase 5 (CHST5) is a Golgi-embedded enzyme that is found in B cells, T cells and intestinal epithelium and is also mediates sulfation of keratan in cornea. CHST5 is a sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine residues of keratan. CHST5 works on the non-reducing terminal GlcNAc of short andlong carbohydrate substrates that have poly-N-acetyllactosamine structures.

SEPSECS catalyzes the last step of sec synthesis by converting O-phosphoseryl-tRNA(sec) to selenocysteinyl-tRNA(sec) using selenophosphate as the selenium donor. Furthermore, SEPSECS protein is considered a specific marker of autoimmune hepatitis.

KLK2 is a part of the grandular kallikrein protein family whose Members are engaged in a diverse array of biological functions. Kallikreins are a subgroup of serine proteases which are clustered on chromosome 19. KLK2 is a highly active trypsin-like serine protease which selectively cleaves at arginine remains. KLK2 is mostly expressed in prostatic tissue and is accountable for cleaving pro-prostate-specific antigen into its enzymatically active form. KLK2 is greatly expressed in prostate tumor cells and may possibly be a prognostic maker for prostate cancer risk.

PPCDC is a member of the HFCD (homo oligomeric flavin containing Cys decarboxylase) superfamily which takes a part in the biosynthesis of coenzyme A (CoA) from pantothenate (Vitamin B). The biosynthesis of CoA from pantothenate needs several steps: the phosphorylation of pantothenate, the conversion of 4’-hosphopantothenate to 4''-phosphopantetheine, the adenylation by phosphopantetheine adenylyltransferase to form dephospho-CoA and the phosphorylation by dephospho-CoA kinase to form CoA. PPCDC is a key player in this pathway. PPCDC converts 4''-phosphopantothenate into 4''-phosphopantetheine.

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.

Kallikrein-5 (KLK5) is a member of the serine protease family of proteolytic enzymes. KLK5 is expressed in various tissues including the salivary gland, stomach, uterus, lung, thymus, prostate, colon, brain, thyroid, and trachea. KLK5 expression is up-regulated by estrogens and progestins. KLK5 is secreted and may be involved in desquamation in the epidermis. Kallikreins which are a subgroup of serine proteases, have distinct physiological functions. Many kallikreins are associated with carcinogenesis and some have potential as novel cancer and other disease biomarkers. The KLK5 gene is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19.