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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.

PDXP is the active form of vitamin B6 that functions as a coenzyme in preserving biochemical homeostasis. The desired degradation route from PLP to 4-pyridoxic acid involves the dephosphorylation of PLP by PDXP. PDXP shows activity to pyridoxal 5''-phosphate (PLP), pyridoxine 5''-phosphate (PMP) and Pyridoxine 5''-phosphate (PNP), with a highest activity with PLP followed by PNP.

Glutathione reductase (Gor) is a member of the class-I pyridine nucleotide disulfide oxidoreductase family. The main role of the Gor protein is to uphold high levels of reduced glutathione in the cytosol. With the associated oxidation of NADPH, Gor transforms oxidized glutathione to the reduced form. The active site of the Gor protein is a redox-active disulfide bond.

DsbA appears to be necessary for correct formulation of disulfide bonds in exported proteins in vivo. DsbA is useful as a standard in immunoblotting. This protein catalyses the reduction and exchange of disulfide bonds and the oxidation of free sulfhydryl groups in vitro. It is the strongest oxidant of the thioredoxin superfamily. This thio/disulfide oxidoreductase is required for efficient disulfide bond formation in the periplasm of E. coli.

3-ketodihydrosphingosine reductase (KDSR) is a 332 amino acid multi-pass membrane protein which localizes to the ER and is a member of the short-chain dehydrogenases/reductases (SDR) family. KDSR is a secreted protein that is weakly expressed in hematopoietic tissue. Furthermore, KDSR catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS). The putative active site residues of KDSR are found on the cytosolic side of the endoplasmic reticulum membrane. Chromosomal rearrangement in the KDSR gene is a cause of follicular lymphoma, aka type II chronic lymphatic leukemia.

CBR4 is a member of the short-chain dehydrogenase/reductase family. CBR4 has a role in biosynthesis of fatty acids in the mitochondria and a broad substrate specificity and reduces 9,10-phenanthrenequinone, 1,4-benzoquinone and a range of other o-quinones and p-quinones (in vitro). CBR4 formation of a heteroteramer with HSD17B8 has NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity for o- and p-quinones.

Epoxide Hydrolase 1 Microsomal (EPHX1) is a vital biotransformation enzyme which transfers epoxides from the degradation of aromatic compounds to trans-dihydrodiols that can be conjugated and excreted from the body. Epoxide hydrolase plays a role in both activation and detoxification of epoxides. Mutations in EPHX1 trigger preeclampsia, epoxide hydrolase deficiency or increased epoxide hydrolase activity.

TDO2 is a ferrous heme enzyme that catalyzes the first and rate-limiting step in the kynurenine pathway which is the major pathway of tryptophan metabolism. TDO2 integrates oxygen into the indole moiety of tryptophan. TDO2 has broad specificity towards tryptamine and derivatives including D- and L-tryptophan, 5-hydroxytryptophan and serotonin.

Paraoxonase-1 or PON1 is part of the paraoxonase group of proteins. PON1 is an enzyme, responsible to the toxic metabolites of a different of organophosphorus insecticides hydrolyzation. Furthermore, PON1 is a dominant anti-atherosclerotic part of HDL. The enzyme needs PPAR-gamma for activation, leading to synthesis and release of paraoxonase 1 from the liver tissue, resulting in atherosclerosis reduction. PON1 has many qualities for atheroprotective through inflammatory lipid peroxides metabolism. This enzyme can hydrolyze a large number of substrates, for example cyclic carbonates, lactones, nerve gases etc.

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.

CDO1 (Cysteine dioxygenase) is a mammalian non-heme iron enzyme that initiates a number of significant metabolic pathways associated with pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. CDO1 catalyzes the conversion of L-cysteine to cysteine sulfinic acid (cysteine sulfinate) by incorporation of dioxygen. CDO1 is a vital regulator of cellular cysteine concentrations and has an essential role in maintaining the hepatic concentration of intracellular free cysteine within a proper narrow range. CDO1 is able to alter intracellular cysteine levels and glutathione levels. CDO1 is highly expressed in the liver and placenta. On the other hand CDO1 has a low expression in heart, brain and pancreas. CDO1 can also be detected in hepatoblastoma HepG2 cells.

ME2 catalyzes the oxidative decarboxylation of malate to pyruvate, malat + NAD(P)+? pyruvate + CO2 + NAD(P)H+, and is found both in eukaryotic and prokaryotic cells. Three different isoforms of ME are known to be in mammalian tissues: a strictly cytosolic NADP+-dependent enzyme, an NADP+-dependent mitochondriail isoform, and a mitochondrial isoenzyme that is able to use both NAD+ and NADP+ but is more effective with NAD+. The mammalian isoforms size is about 62-64 kDa. A native size of 240,000 Da proposes a tetrameric structure for the active enzyme.
Mitochondrial NAD+-dependent ME 2 activity is seen in tissues that experience many cell divisions, like spleen, thymus, and the basal cells of the small intestinal mucosa. ME2 is also expressed all through the rapid cleavage stages of early Xenopus development. Activity for this isoform is low or nonexistent in brain, muscle, and normal and regenerating liver tissue from rat but was observed in rat adrenal cortex, pigeon and human skeletal muscle, and in heart muscle of some species. In addition, it is expressed in mitochondria of all tumor cells inspected to detain ascites tumors, hepatoma cells, and a variety of other tumors and transformed cell lines.

Methionine sulfoxide reductase A (MSRA) is a member of the MsrA Met sulfoxide reductase family. The MSRA enzyme has a vital function as a repair enzyme for proteins which have been inactivated by oxidation. MSRA catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. The three substrates of the MSRA enzyme are peptide-L-methionine, thioredoxin disulfide, and H2O, while its 2 products are peptide-L-methionine (R)-S-oxide and thioredoxin. The MSRA protein is ubiquitous and extremely conserved. Human and animal studies have shown the ultimate levels of expression in kidney and nervous tissue.

Peroxisomal 2,4-dienoyl-CoA reductase (DECR2) is an supporting enzyme of beta-oxidation. DECR2 partakes in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. DECR2 catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.

PCK1 is a central regulating point for the regulation of gluconeogenesis. PCK1 has a vital part in this process by stimulating hepatic glucose production. The expression of PCK1 is controlled by cAMP, glucocorticoids, diet etc. Modulation of the signals controlling PCK1 levels offers a possible therapeutic tactic to the treatment of Diabetes and subsequently obesity.

QDPR belongs to the short-chain dehydrogenases/reductase (SDR) family of enzymes. Operating as a homodimer, QDPR has an imperative role in the recycling of tetrahydrobiopterin (BH4), a vital cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine). More precisely, QDPR catalyzes the regeneration of BH4 from quinonoid dihydrobiopterin (qBH2), the product generated from the hydroxylation reactions. Mutations in the QDPR gene may lead to phenylketonuria II.

Pyrroline-5-Carboxylate Reductase Like (PYCRL) is a member of the pyrroline-5-carboxylate reductase family and acts as a homodecamer. PYCRL plays a key role in proline bio-synthesis. Proline serves as a non-enzymatic antioxidant to reduce damage caused by reactive oxygen species (ROS) in microorganisms, animals and plants. In the final stage of proline biosynthesis, PYCRL catalyzes the reduction of aldehyde dehydrogenase 4A1 (ALDH4A1) to proline with NAD(P)H as the cofactor.

AKR1B10 efficiently reduces aliphatic and aromatic aldehydes, and it is less active on hexoses. AKR1B10 is highly expressed in adrenal gland, small intestine, and colon, and may play an important role in liver carcinogenesis. AKR1B10 is a monomeric protein that competently catalyzes the reduction of aromatic and aliphatic aldehydes and ketones. AKR1B10 is widely expressed in numerous human tissues, small intestine, colon and adrenal gland. AKR1B10 is pathogenically involved in diabetic complications and is overexpressed in human tumors, such as liver, breast, and lung cancer, AKR1B10 is involved in the development and progression of cancer.

Aldo-keto reductase family 1 member C1 or AKR1C1 is an enzyme, part of the aldo/keto reductase family that holds over 40 familiar proteins. AKR1C1 promotes the conversion of ketones & aldehydes to their alcohol forms by using cofactors such as NADH & NADPH. AKR1C1 promotes the progesterone reduction to its inactive molecule form 20-alpha-hydroxy-progesterone.

ALDH5A1 is a mitochondrial NAD(+)-dependent succinic semialdehyde dehydrogenase, which is a member of the aldehyde dehydrogenase family of proteins. The ALDH5A1 protein functions as a mediator to the NADP+-dependent oxidation of aldehydes into acids and has an imperative role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH5A1 is expressed in various tissues, including the liver, heart, lung, brain, kidney and placenta. Deficiency in the ALDH5A1 enzyme, known as 4-hydroxybutyricaciduria, is a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA). In response to this defect, physiologic fluids from patients accumulate GHB, which is a compound with numerous neuromodulatory properties.

PRRX1 is part of the paired family of homeobox proteins. PRRX1 functions as a transcription co-activator, enhancing the DNA-binding activity of serum response factor, a protein required for the induction of genes by growth and differentiation factors. PRRX1 also regulates muscle creatine kinase, and therefore has a part in the establishment of diverse mesodermal muscle types. The protein binds to an A/T-rich element in the muscle creatine enhancer. Among the diseases associated with PRRX1 are agnathia-otocephaly complex, and pleomorphic liposarcoma.

Ubiquinol-Cytochrome C Reductase (UQCRQ) is a small core-associated protein and a subunit of ubiquinol-cytochrome c reductase complex III that belongs to the mitochondrial respiratory chain. UQCRQ is also a ubiquinone-binding protein of low molecular mass.

HAAO is a monomeric cytosolic protein which is a member of intramolecular dioxygenases family containing nonheme ferrous iron. The HAAO protein catalyzes the synthesis of quinolinic acid (QUIN) from 3-hydroxyanthranilic acid. QUIN is an excitotoxin whose toxicity is facilitated by its ability to activate glutamate N-methyl-D-aspartate receptors. Amplified cerebral levels of QUIN may contribute to the pathogenesis of neurologic and inflammatory disorders. HAAO is widely distributed in peripheral organs, such as liver and kidney, and is also present in low amounts in the central nervous system.