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GCK is an enzyme that expedite the formation of glucose-6-phosphate for glucose by phosphorylation. Humans and other vertebrates have GCK in the cells of the pancreas and liver. In both organs, the enzyme has an important role in carbohydrate metabolism regulation by sensing sugar levels and acting according to the change in glucose levels, that can rise after a meal or fall during fasting. Mutations in the gene that codes for this enzyme can cause hypoglycemia or diabetes.

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Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.

DUSP3 belongs to the dual specificity protein phosphatase subfamily which inactivates their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. DUSP3 negatively regulate members of the mitogen-activated protein kinase superfamily that are related to cellular proliferation and differentiation. DUSP3 is expressed in both breast and ovarian tissues and displays activity both for tyrosine-protein phosphate and serine-protein phosphate, but exhibits a strong preference toward phosphotyrosines, specifically dephosphorylates and inactivates ERK1 and ERK2.

Salmonella Typhi is a pathogen causing typhoid fever, affecting over 17 million people with approximately 600,000 deaths annually worldwide. If untreated, typhoid fever cases result in mortality rates ranging from 12-30%.

Listeriolysin O (aka LLO) is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene and composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents and inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes (average pH ~ 5.9) of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, and the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system and antibodies. LLO also brings about dephosphorylation of histone H3 and deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO and is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST's supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO.

Syntaxin-2 (STX2) is a member of the syntaxin/epimorphin family of proteins. Syntaxin family members are cellular receptors for transport vesicles which participate in exocytosis in neutrophils. STX2 regulates epithelial-mesenchymal interactions and epithelial cell morphogenesis and activation. STX2 is a t-SNARE which localizes to the apical plasma membrane and intracellular vesicular structures. In addition, STX2, along with SNAP-23, is essential for regulated surfactant secretion.

TDP1 belongs to the phospholipase D family and contains two PLD phosphodiesterase domains. TDP1 is involved in repairing stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of the phosphodiester bond between the tyrosine residue of topoisomerase I and the 3-prime phosphate of DNA. TDP1 may also remove glycolate from single-stranded DNA containing 3-prime phosphoglycolate, suggesting a role in repair of free-radical mediated DNA double-strand breaks. Mutations in the TDP1 gene are linked to the disease spinocerebellar ataxia with axonal neuropathy (SCAN1).

A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

ACADS is a tetrameric mitochondrial flavoprotein, which is part of the acyl-CoA dehydrogenase family. ACADS catalyzes the first step of the mitochondrial fatty acid beta-oxidation pathway. Mutations in ACADS have been associated with Short Chain Acyl-CoA Dehydrogenase Deficiency.

Small Ubiquitin-like Modifiers (SUMOs) are a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation. Unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. All SUMO proteins share the conserved ubiquitin domain and the C-terminal diglycine cleavage/attachment site. Human SUMO2, also known as Sentrin2 and SMT3B is synthesized as a 95 amino acid (aa), 11 kDa propeptide that contains a two aa C-terminal prosegment, and an 18 aa N-terminal protein interacting region (aa 33 -50). Following prosegment cleavage, the C-terminal glycine is enzymatically attached to a lysine on a target protein. Human SUMO2 shares 100% sequence identity to SUMO-2 from mouse. SUMO2 also has very high sequence homology to SUMO3 and SUMO4, 86 % and 85%, respectivel

Glycerol-3-phosphate dehydrogenase 1-like protein (GPD1L) converts sn-glycerol 3-phosphate to glycerone phosphate. GPD1L is found in the cytoplasm, associated with the plasma membrane, where it binds the sodium channel, voltage-gated, type V, alpha subunit (SCN5A). Mutations in the GPD1L gene are the cause of SIDS (sudden infant death syndrome) and Brugada syndrome type 2 (an autosomal dominant tachyarrhythmia).

A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

Full-length recombinant human neutrophil pro-collagenase (MMP-8), latent form.
Matrix metalloproteinase 8 (MMP-8), or neutrophil collagenase, degrades interstitial collagens, acting preferentially on collagen type I.
Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, which are the major cell type that expresses MMP-8.
MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation.Once released and activated through proteolytic or oxidative mechanisms, MMP-8 plays a major role in the connective tissue turnover that accompanies inflammatory processes.

Syntaxin 4 (STX4) is a member of the syntaxin/epimorphin family of proteins. The Syntaxin family is cellular receptors for transport vesicles which participate in exocytosis in neutrophils. Syntaxin 4 is vital for normal regulation of glucose metabolism uptake in skeletal muscle and decline in STX4 protein levels lead to reduction of whole-body hormone-stimulated glucose metabolism. STX4 is expressed in neutrophils and neutrophil-differentiated HL-60 cells. The STX4 expression in neutrophils increases with differentiation.

Ubiquitin-Conjugating Enzyme E2G2 (UBE2G2) is a protein coding gene which is a part of the E2 ubiquitin-conjugating enzyme family. UBE2G2 accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to various proteins. UBE2G2 is ubiquitously expressed mainly in adult muscle. UBE2G2 also takes part in endoplasmic reticulum-associated degradation (ERAD).

GST family of enzymes comprises a long list of cytosolic, mitochondrial, and microsomal proteins that are 45-55 kDa (dimer form) size and are capable of multiple reactions with a multitude of substrates, both endogenous and xenobiotic. GST catalyses the conjugation of reduced glutathione meaning the sulfhydryl group, to electrophilic centers on a wide variety of substrates. This activity is useful in the detoxification of endogenous compounds such as peroxidised lipids, as well as the metabolism of xenobiotics. GST binds toxins and function as transport protein. Glutathione S-transferase is used to create the so-called 'GST gene fusion system'. The GST is used to purify and detect proteins of interest. In a GST gene fusion system, the GST sequence is incorporated into an expression vector alongside the gene sequence encoding the protein of interest. Induction of protein expression from the vector's multiple cloning sites results in expression of a fusion protein - the protein of interest fused to the GST protein. This GST-fusion protein can then be purified from cells via its high affinity for glutathione. Fusion proteins offer an important biological assay for direct protein-to-protein interactions. The GST tag has the size of 220 amino acids, which, compared to other tags like the myc- or the FLAG-tag, is quite big. It is fused to the N-terminus of a protein. However, many commercially-available sources of GST-tagged plasmids include a thrombin domain for cleavage of the GST tag during protein purification. A GST-tag is often used to separate and purify proteins that contain the GST-fusion. GST-fusion proteins can be produced in Escherichia coli, as recombinant proteins.

Coproporphyrinogen Oxidase (CPOX) which is localized to the internal membrane space of erythrocytes takes part in the 6th phase of heme biosynthesis. CPOX catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III. Mutations in human CPOX gene forecast the clinical result of the disease, with either hepatic hereditary coproporphyria or hematological manifestations of erythropoietic harderoporphyria.

CA, also known as carbonic anhydrase is an enzyme that functions around the involvement of CO2 + H2O to HCO3- + H+ (conversion of CO2 to bicarbonate & protons). This enzyme holds a Zn ion as part of its active site. The central function of CA is to preserve the acid-base homeostasis within the blood and various organs. carbonic anhydrase assists Carbonic Anhydrase I to move CO2 to and from tissues.

Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and member of the peptidase C1 family. CTSZ, which has been also known as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and, similar to other members of this family, takes part in tumorigenesis.

SARS Membrane protein is a membranal protein which plays a crucial role in the virus’ life cycle. This protein has 3 outer cell structural antigens, the envelope (E), membrane (M)and spike (S) antigens. SARS Membrane protein is essential to the process of assembly, budding, creation of the envelope and pathogenesis.

SARS or severe acute respiratory syndrome is a lethal kind of pneumonia generated by coronavirus. Coronaviruses are a family of viruses that causes a mild respiratory tract infection is a large type of creatures such as humans, pigs, cows, mice, cats etc. up to this day, the origin of the coronavirus is still unknown.

Salmonella Typhi is a pathogen causing typhoid fever, affecting over 17 million people with approximately 600,000 deaths annually worldwide. If untreated, typhoid fever cases result in mortality rates ranging from 12-30%.

CD4 is a cell-surface glycoprotein found on the mature helper T cells and immature thymocytes, as well as on monocytes and macrophages. (Some cytotoxic T cells have CD4 protein as well.) Normally, about 65% of T cells in the blood are CD4+ (have CD4 protein protruding from their membrane). A mature T cell with either have CD4 or CD8, but not both. During one stage of development T cells develop CD4 and CD8 receptors, but they eventually are differentiated in the thymus and become more specialized.

Angiotensin Converting Enzyme (ACE) is a zinc metallopeptidase vital for blood pressure control and salt and water metabolism.ACE converts angiotensin I to angiotensin II by release of the terminal His-Leu which causes the vasoconstrictor activity of angiotensin to increase.ACE inactivates bradykinin, a potent vasodilator and has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.