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SAE1 is part of the ubiquitin-activating E1 family of proteins and participates in the significant first step of the UBL1 conjugation pathway. Proteins conjugated to Ub are marked for progressive degradation by the 26S Proteasome. SAE1 acts as a UBLI E1 ligase mediating the ATP-dependent activation of UBL1. SAE1 binds with UBLE1A and UBLE1B to form a heterodimer which can bind UBL1. SAE1 is a dimeric enzyme that takes part as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. SAE1 regulates ATP-dependent activation of SUMO proteins and formation of a thioester with a conserved cysteine residue on SAE2.

RDH12 is a member of the short-chain Dehydrogenases / Reductases (SDR) family. RDH12 is found generally in brain, stomach, eye, skeletal muscle and kidney. RDH12 is a NADPH-dependent retinal reductase whose main activity is toward 9-cis and all-trans-retinol. In addition, RDH12 takes part in the metabolism of short-chain aldehydes but does not display steroid dehydrogenase activity.

ACADL is a homotetramer belonging to the acyl-CoA dehydrogenase family. ACADL takes part in the catabolism of fatty acids and amino acids and is a key source of energy for the heart and skeletal muscle. Mutation in the ACADL gene results in non-ketotic hypoglycemia and hypotonia (muscle weakness).

ACADVL is an inner mitochondrial membrane enzyme that is part of the family of acyl-CoA dehydrogenases. ACADVL protein participates in lipid metabolism and has catalytic activity toward esters of long chain and very long chain fatty acids such as palmitoyl-CoA and stearoyl-CoA, and is involved in the first step of the fatty acid β-oxidation pathway. ACADVL deficiency in reduces myocardial fatty acid beta-oxidation and is related with cardiomyopathy.

Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

Pleckstrin homology-like domain family A member 2 (PHLDA2) is a cytoplasmic protein, which is involved in fetal and placental growth. PHLDA2 is an apoptosis-related protein, which acts as a negative growth regulator and is expressed during normal human development. PHLDA2 is imprinted on placenta, liver and fetal tissues during embryogenesis and is removed once development is complete. The PHLDA2 gene is one of a number of genes in the imprinted gene domain of 11p15.5 which is considered to be an important tumor suppressor gene region. Changes in this region may be linked to the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung, ovarian, and breast cancer. PHLDA2 is expressed in placenta (present in all cells of the villous cytotrophoblast) and adult prostate gland. Furthermore, PHLDA2 is expressed in adult brain and neuroblastoma, medullablastoma and glioblastoma cell lines and at low levels in adult liver and lung, and fetal liver.

TKT is a thiamine-dependent enzyme that takes part in the channeling of leftover sugar phosphates to glycolysis in the pentose phosphate pathway. Multiple alternatively spliced variants are known that encode the same protein.

Phosphomannomutase 1 (PMM1) is an enzyme involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. PMM1 catalyzes the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for the synthesis of dolichol-phosphate-mannose, which is crucial for N-linked glycosylation and accordingly the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol (GPI) anchored proteins. Additionally, PMM1 may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.

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.

UPRT is a uracil phosphoribosyltransferase, that catalyzes the alteration of uracil and 5-phosphoribosyl-1-R-diphosphate to uridine monophosphate (UMP). This reaction is a significant part of nucleotide metabolism, specifically the pyrimidine salvage pathway. UPRT is restricted to the nucleus and cytoplasm and is a possible target for rational design of drugs to cure cancer and parasitic infections.

Cytosolic and membrane-bound types of GST are encoded by 2 different supergene families. There are 8 classes of the soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are arranged in a gene cluster on chromosome 1p13.3 and aare highly polymorphic. These genetic differences can change an individual's resistance to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with the rise in a number of cancers.

Glutathione S-transferase omega 2 (GSTO2) is a member of the GST superfamily. GSTO2 is involved in catalyzing the reaction of glutathione with a broad range of organic compounds to form thioethers, a process which is vital for the metabolism and detoxification of a variety of xenobiotics and carcinogens. GSTO2 displays glutathione-dependent thiol transferase activity. GSTO2 has a high dehydroascorbate reductase activity and may be a factor in the recycling of ascorbic acid. GSTO2 also participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA). GSTO2 is expressed in an array of tissues, including the liver, kidney, skeletal muscle and prostate, while the strongest expression is seen in the testis.

BDH2 is a member of the short-chain dehydrogenases/reductases (SDR) family. BDH2 protein has a significant part in the peripheral utilization of 3-hydroxybutyrate. BDH2 can convert high levels of circulating 3-hydroxybutyrate into acetoacetate due to cytoplasmic localization in high ratio of oxidized NAD+, the NAD+ dependence and the kinetic parameters.

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.

Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.

Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.

Mercaptopyruvate Sulfurtransferase (MPST) catalyzes the transfer of a sulfur ion from 3-mercaptopyruvate to cyanide or other thiol compounds. MPST might be involved in cysteine degradation and cyanide detoxification. The MPST enzyme is regulated by oxidative stress and thioredoxin. In oxidative stress conditions, the catalytic cysteine site is transformed to a sulfenate which inhibits the MPST enzyme activity. The reduced thioredoxin cleaves an intersubunit disulfide bond to activate the redox switch and reactivate the enzyme. A deficiency in MPST activity is implicated in a rare inheritable condition known as MCDU (mercaptolactate-cysteine disulfiduria).

AnsA is a cytoplasmic asparaginase from E.coli involved in intracellular asparagine utilization. E.coli has 2 L-asparaginases: the cytoplasmic type I form (ansA) and the periplasmic type II form (ansB). AnsA (Type L asparaginase) is constitutively expressed and is obligatory for the growth of the bacteria on asparagine as the sole nitrogen source.

Beta-secretase 1 or BACE1 or beta-site amyloid precursor protein cleaving enzyme 1, is a protein that is encoded by the BACE1 gene in humans. Expression of BACE1 is seen primarily in neurons as it is crucial for the creation of myelin sheats in the peripheric nervous system. Beta-secretase 1 is a proteas that is located in the cell membrane (transmembrane). The enzyme consists of 2 active sites (aspartate residues) in the extracellular domain that can act as a dimer.

SRM is an enzyme which catalyzes the transfer of the propylamine group from S-adenosylmethioninamine to putrescine in the biosynthesis of spermidine. The polyamines putrescine, spermine and spermidine are ubiquitous polycationic mediators of cell growth and differentiation. The SRM protein is one of four enzymes in the polyamine-biosynthetic pathway and completes the final step of spermidine biosynthesis.

Fatty Acid Amide Hydrolase 2 (FAAH2) shares a conserved protein motif with the amidase signature family of enzymes. FAAH2 catalyzes the hydrolysis of a broad range of bioactive lipids, including those from the 3 main classes of fatty acid amides; N-acylethanolamines, fatty acid primary amides and N-acyl amino acids. FAAH2 is also degrades bioactive fatty acid amides to their corresponding acids, thus helping to end the signaling functions of these molecules. FAAH2 prefers monounsaturated acyl chains as a substrate.

Human Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor suppressor protein p53, and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1.

Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso-PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats.

GALE is an enzyme that participates as the third enzyme in the Leloir pathway of galactose metabolism. GALE is a homodimeric epimerase localized in bacterial, plant, and mammalian cells. GALE inhances the reverse chemical reaction, the conversion of UDP-glucose to UDP-galactose. UDP-galactose builds galactose-containing proteins and fats, which have a crucial part in chemical signaling, building cellular structures, transporting molecules, and producing energy.