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Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig.
Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site amino acid eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and the enzyme's secondary GTPase activity. This engineering assures reproducible properties of the antigen preparations through the absence of variable and ill-defined covalent aggregates of tTG antigen and host cell proteins.

MAT1A catalyzes a two-step reaction that involves the transfer of the adenosyl moiety of ATP to methionine to form S-adenosylmethionine and tripolyphosphate, which is subsequently cleaved to PPi and Pi. S-adenosylmethionine is the source of methyl groups for most biological methylations. MAT1A is found as a homotetramer (MAT I) or a homodimer (MAT III) whereas a third form, MAT II (gamma), is encoded by the MAT2A gene. Mutations in MAT1A gene are associated with methionine adenosyltransferase deficiency. MAT1A expression also correlates with a differentiated phenotype, whereas liver cells expressing MAT2A present a dedifferentiated phenotype and lowered AdoMet synthesis. Likewise, NFκB and TNFα cause a switch from MAT1A to MAT2A expression in human hepatocellular carcinoma (HCC), which facilitates cancer cell growth.

CTD small phosphatase-like protein (CTDSPL) specially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residues repeats in the C-terminal domain (CTD) of the biggest RNA polymerase II subunit POLR2A. CTDSPL negatively regulates RNA polymerase II transcription, probably by directing the transition from initiation/capping to processive transcript elongation. CTDSPL is employed by REST to neuronal genes which contain RE-1 elements, directing to neuronal gene silencing in non-neuronal cells.

Cathepsin S (CTSS) belongs to the peptidase C1 family. CTSS is a lysosomal cysteine proteinase that participates in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. CTSS functions as an elastase over a broad pH range in alveolar macrophages.

HtrA2 also called Omi is a mammalian serine protease at high temperatures and has a chaperone activity at low temperature. The full-length HtrA2 is synthesized as a precursor protein and then targeted to the mitochondria where it is matured by the removal of N-terminal 133 residues. Mature HtrA2 consists of a putative transmembrane domain; an inhibitor of apoptosis protein (IAP)-binding motif; a single C-terminal PDZ domain that mediates protein-protein interactions. Recently, HtrA2 has known to contribute both to caspase-dependent and caspase-independent cell death.

Aspartic Peptidase, Retroviral-Like 1 (ASPRV1) is a protein which contains one peptidase A2 domain. ASPRV1 undergoes autocleavage which is essential for activation of the protein. ASPRV1 is expressed mostly in the granular layer of the epidermis and inner root sheath of hair follicles and localized to membrane region. In the psoriatic skin, ASPRV1 is expressed throughout the stratum corneum. In the ulcerated skin, ASPRV1 is expressed in the stratum granulosum of intact epidermis; however it is virtually nonexistent from ulcerated regions. In addition, ASPRV1 is expressed in differentiated areas of squamous cell carcinomas but not in the undifferentiated tumors.

SSU72 is an extremely conserved homologue of yeast Ssu72, a CTD phosphatase and a component of the polyadenylation/termination machinery. SSU72 interacts with TFIIB, Rb and DNAM-1 and operates to catalyze the dephosphorylation of target proteins, and taking part in RNA processing and termination via dephosphorylation of Pol II. SSU72 is found in multiple alternatively spliced isoforms.

Phosphoribosylaminoimidazole Carboxylase (PAICS) is an enzyme involved in nucleotide biosynthesis and particularly in purine biosynthesis. PAICS is a bifunctional enzyme containing phosphoribosylaminoimidazole carboxylase activity at its N-terminal region and phosphoribosylaminoimidazole succinocarboxamide synthetase at its C-terminal region. PAICS catalyzes the conversion of 5'-phosphoribosyl-5-aminoimidazole(AIR) into 5'-phosphoribosyl-4-carboxy-5-aminoimidazole (CAIR) as described in the reaction. PAICS catalyzes steps six and seven of purine biosynthesis.

Human Phosphoserine phosphatase (hPSP) is an important enzyme in the phosphorylated pathway of serine biosynthesis, which contributes a major portion of the endogenous L-serine. Similar to known L-3-phosphoserine phosphatases, it catalyzed the Mg2+-dependent hydrolysis of L-phosphoserine and an exchange reaction between L-serine and L-phosphoserine. Recently, its complex structures reveal that the open-closed environmental change of the active site, generated -helical bundle domain, is important to substrate by local rearrangement of the recognition and hydrolysis.

GSTK1 is involved in cellular detoxification. GSTK1 is localized to the peroxisome and catalyzes the conjugation of the thiol group of glutathione (GSH) to the electrophilic groups of a broad range of hydrophobic substrates, leading to an easier removal of the latter from the cells.

Ornithine Aminotransferase is a mitochondrial enzyme which is an important factor that converts arginine and ornithine into the major excitatory and inhibitory neurotransmitters glutamate and GABA. Ornithine Aminotransferase mutations result in a deficiency that cause the autosomal recessive eye disease Gyrate Atrophy.

Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase 2 is the predominant form found in skeletal muscle. It localizes to the outer membrane of mitochondria. Expression of this gene is insulin-responsive, and studies in rat suggest that it is involved in the increased rate of glycolysis seen in rapidly growing cancer cells.

ACE-2 (Angiotensin converting enzyme 2) an enzyme bound to cell membranes in various organs such as intestines arteries , lungs, heart & kidney. ACE2 an entry receptor of SARS coronaviruses as well as SARS-CoV-2,.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen located on the external envelope of the virion that takes part in a critical part in viral infection by identifying host cell receptors and facilitating fusion of the viral and cellular membranes. 2 main domains in coronavirus S1 have been recognized, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains function as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 obtains a signal peptide, a transmembrane domain, and a single metalloproteinase active site containing an HEXXH zinc-binding domain. ACE-2 plays a role as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.

Aldo-Keto Reductase Family 7 Member A3 or AKR7A3, is an enzyme, it is part of the detoxification of aldehydes and ketones process. AKR7A3 diminishes the dialdehyde protein-binding form of aflatoxin B1 to the non-binding AFB1 dialcohol. The enzyme takes partin protection of liver from toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.

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.

PRCP is a plasma protein which takes part in the cleavage of C-terminal amino acids linked to proline in proteinfor example angiotensin-2 & 3 at acidic pHenvironment rather than at neutral pHwhich exhibit less activity. This cleavage is important since Angiotensin-2 takes part in regulation of blood pressure & electrolyte balance which is essential to hypertension.

ANXA1 is part of the family of Ca(2+)-dependent phospholipid binding proteins which have a Mw between 35kDa-40kDa and are situated on the cytosolic face of the plasma membrane. ANXA1 protein has a Mw of 40kDa, with phospholipase A2 inhibitory activity to bind from two to four calcium ions with high affinity. Since phospholipase A2 is necessary for the biosynthesis of the potent mediators of inflammation, prostaglandins and leukotrienes, ANXA1 might have potential anti-inflammatory activity. ANXA1 promotes membrane fusion and iplays a role in exocytosis. The recognition of ANXA1 protein by immunocytochemical leads a simple, highly sensitive and specific assay for diagnosis of hairy cell leukemia.

PPM1G is part of the PP2C family of Ser/Thr protein phosphatases which are known to be negative regulators of cell stress response pathways. PPM1G is accountable for the dephosphorylation of Pre-mRNA splicing factors, an important factor for the formation of functional spliceosome. PPM1G regulates cell cycle progression. PPM1G mediates histone dephosphorylation/exchange in response to DNA damage or checkpoint recovery in higher eukaryotes. The degradation of p21/WAF1 induced by PPM1G is mediated in a proteasome-dependent manner. Protein phosphatase 1G regulates assembly and function of the beta-catenin degradation complex.

Myeloid differentiation antigen Gr1 (Ly6G) is a GPI-anchored protein, which is briefly expressed on monocytes in the bone marrow. The level of the Ly6G expression in the bone marrow completely correlates with granulocyte differentiation and maturation. Ly6G ligation on murine neutrophils inhibits neutrophil recruitment, thus providing the first evidence of a function for the Ly6G molecule. Ly6G is seen primarily on neutrophils, also in a subgroup of eosinophils, differentiating pre-monocytes and plasmacytoid dendritic cells.

Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.

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.

DUSP23 is a member of the protein-tyrosine phosphatase family. DUSP23 is a protein phosphatase which facilitates dephosphorylation of phosphorylated proteins on Tyr and Ser/Thr residues. In vitro, DUSP23 dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10). In addition, DUSP23 enhances activation of JNK and p38(MAPK14).