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Indoleamine 2,3-Dioxygenase 1 (IDO1) catalyzes the primary and rate-limiting stage in tryptophan catabolism to N-formyl-kynurenine. IDO1 affects on various tryptophan substrates including D-tryptophan, and serotonin and is expressed in dendritic cells, monocytes, and macrophages. IDO1 takes part in a range of pathophysiological processes like neuropathology, antimicrobial and antitumor defense, immunoregulation, and antioxidant activity. IDO1 regulates T-cell behavior by its pericellular catabolization of the necessary amino acid tryptophan.

GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.

CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.

SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

NADH Dehydrogenase1 Alpha Subcomplex 4 (NDUFA4) is a member of the complex I 9kDa subunit family. Mammalian complex I of mitochondrial respiratory chain is comprised of 45 different subunits. NDUFA4 protein has NADH dehydrogenase activity and oxidoreductase activity. NDUFA4 transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the NDUFA4 enzyme is assumed to be ubiquinone.

Chitodextrinase is a unique membrane-bound endoenzyme. The chitodextrinase enzyme cleaves soluble oligomers, but not chitin, to the di- and trisaccharides. Chitodextrinase is unable to solubilize chitin, but it can catalyze the hydrolysis of high to low molecular weight soluble chitin oligosaccharides.

GLRX2 is a 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. Glutaredoxins are a family of glutathione-dependent hydrogen donors that participate in a variety of cellular redox reactions.

Dihydroorotate dehydrogenase quinone (DHODH) is a member of the dihydroorotate dehydrogenase family. DHODH is a mitochondrial protein found on the outer surface of the inner mitochondrial membrane. DHODH catalyzes the 4th enzymatic step, the ubiquinone-mediated oxidation of dihydroorotate to orotate (with quinone as electron acceptor), in de novo pyrimidine biosynthesis. DHODH gene defects cause the postaxial acrofacial dysostosis (POADS), also known as Miller syndrome.

SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function and its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, and TNF-alpha in murine and human macrophages.

DIM1 dimethyladenosine transferase 1 homolog (DIMT1) is a member of the methyltransferase superfamily. The DIMT1 enzyme specifically dimethylates 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. DIMT1 is restricted to the nucleolus.

Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.

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.

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.

SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

Deoxyuridine Triphosphatase (DUT) is a ubiquitous enzyme that functions in nucleotide metabolism. Deoxyuridine Triphosphatase, in the presence of magnesium ions, is responsible for hydrolyzing dUTP to dUMP and diphosphate. This reaction is imperative for keeping the intracellular dUTP concentration low so that uracil does not become incorporated into DNA. Extensive integration of uracil into DNA can eventually lead to cell death. This suggests that DUT is crucial for cell viability, further implying that it is a prospective target for anticancer therapy.

NUDT10 belongs to the Nudix hydrolase family of pyrophosphatases. Nudix hydrolases contain a characteristic Nudix domain and are responsible for catalyzing the hydrolysis of nucleoside diphosphate derivatives. NUDT10 functions as a manganese-dependent polyphosphate phosphohydrolase with an optimum pH of 8.5. NUDT10 protein specifically metabolizes diadendosine-polyphosphates and, to a lesser extent, diphosphoinositol polyphosphates.

Tryptophanase, also known as tnaA, catalyzes chemical reaction using 2 substrates which are L-tryptophan and H2O. tnaA protein's three products are indole, pyruvate, and NH3.

D-lactate dehydrogenase (ldha) is a member of the D-isomer specific 2-hydroxyacid dehydrogenase family. In enzymology, an ldha (cytochrome) is an enzyme which catalyzes the chemical reaction. Therefore, the 2 substrates of the ldha enzyme are (D)-lactate and ferricytochrome c, whereas its 2 products are pyruvate and ferrocytochrome c.

GPD1 enzyme catalyzes the reduction of dihydroxyacetone phosphate to sn-glycerol 3-phosphate. (sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH) previous names for glycerol-3-phosphate dehydrogenase include alpha glycerol-3-phosphate dehydrogenase and glycerolphosphate dehydrogenase. However, GPD1 differs from glyceraldehyde 3-phosphate dehydrogenase (GAPDH) whose substrate is an aldehyde not an alcohol.

Monoamine Oxidase A, also known as MAOA catalyzes the oxidative deamination of biogenic as well as xenobiotic amines and has significant functions in the metabolism of neuroactive and vasoactive amines in the central nervous system as well as peripheral tissues. Mutation in MAOA results in Brunner syndrome; in addition MAOA has also been linked with a diversity of other psychiatric disorders, which includes antisocial behavior. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT).

Hydroxyacid Oxidase 1 (HAO1) is a part of the superfamily of the alpha hydroxy acid oxidases (HAO) enzymes. HAO1 catalyses the FMN mediated oxidation of glycolate to glyoxylate and glyoxylate to oxalate by reducing oxygen to hydrogen peroxide. HAO1 is expressed mainly in the liver and pancreas and is most active on twocarbon substrates such as glycolate. HAO1 isthe main cause of hyperoxaluria, a disorder in which large deposits of calcium oxalate form kidney stones.

Dopachrome Tautomerase also known as DCT, belongs to the tyrosinase family. DCT takes a significant part in the synthesis of the melanin pigment including tyrosinase (Tyr), tyrosinase-related protein 1 (Tyrp1). Which are highly involved in eumelanin synthesis. The change among the eumelanin and the pheomelanin pathways is assumed to depend on the presence of cysteine. Hence, in the lack of cysteine, dopaquinone, the product of tyrosinase action, is transformed to cyclodopa (leucodopachrome) and afterwards to dopachrome (and DOPA).

P450 Oxidoreductase, also known as POR is a flavoprotein which contributes electrons to all microsomal P450 enzymes. POR is localized to the endoplasmic reticulum, where it is also capable of transfering electrons to heme oxygenase as well as cytochrome b5. POR is structurally related to two separate flavoprotein families; first one is ferredoxin nucleotide reductase and the second flavodoxin.