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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.

N-alpha-acetyltransferase 50 (NAA50) consists of 169 amino acid cytoplasmic protein belonging to the acetyltransferase family and GNAT subfamily. NAA50 is a likely catalytic component of the ARD1A-NARG1 complex which displays alpha acetyltransferase activity. NAA50 has also been shown to interact with MAK10 and is encoded by a gene that maps to human chromosome 3q13.2.

Histone deacetylase 8 (HDAC8) is a member of the class 1 of the histone deacetylase/acuc/apha family. HDAC8 is biologically involved in skull morphogenesis and metabolic control of the ERR-alpha/PGC1-alpha transcriptional complex. Histones play a key role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation modifies chromosome structure and affects transcription factor access to DNA.

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.

Phosphoglycerate mutase 2 (PGAM2) is a member of the phosphoglycerate mutase family. PGAM is a dimeric enzyme which contains in separate tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM (Phosphoglycerate mutase) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM2 gene mutations cause muscle phosphoglycerate mutase efficiency, otherwise known as glycogen storage disease X.

Human Ubquitin Conjugating Enzyme 9 (Ubc9) is a member of the E2 family and is specific for the conjugation of SUMO to a variety of target proteins. SUMO conjugation to target proteins is mediated by a different, but analogous, pathway to ubiquitinylation. This E2 is unusual in that it interacts directly with protein substrates that are modified by sumolyation, and may play a role in substrate recognition. Ubc9 can mediate the conjugation of SUMO-1 to a variety of proteins including RanGAP1, I?B?, and PML without the requirement of an E3 ligase.

Alanine transaminase or ALT is a transaminaseenzyme.
ALT is found in serumand in various bodily tissues, but is most commonly associated with the liver; It catalyzes the transfer of an aminogroup from alanineto a-ketoglutarate, the products of this reversible transaminationreaction being pyruvateand glutamatealanine+ a-ketoglutarate= pyruvate+ glutamate
It is commonly measured clinically as a part of a diagnostic liver function test, to determine liver health. It is also called serum glutamate pyruvate transaminase (SGPT) or alanine aminotransferase (ALAT). Diagnostically, it is almost always measured in units/litre (U/L).

OGG1 is a DNA glycosylase enzyme which takes part in base excision repair. OGG1 protein is the main enzyme accountable for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which arises as a result of exposure to reactive oxygen species (ROS). OGG1 shows beta lyase activity that nicks DNA 3 to the lesion.

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.

Porphobilinogen deaminase (HMBS) belongs to the hydroxymethylbilane synthase superfamily. HMBS is a cytoplasmic enzyme found in the heme synthesis pathway. HMBS is the 3rd enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of 4 porphobilinogen molecules into the linear hydroxymethylbilane. HMBS gene mutations cause errors in pyrrole metabolism which in turn lead to the autosomal dominant disease acute intermittent porphyria.

CysH (Phosphoadenosine phosphosulfate reductase) is a member of the PAPS reductase family, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The 3 substrates of the CysH enzyme are adenosine 3',5'-bisphosphate, sulfite, and thioredoxin disulfide, whereas its two products are 3'-phosphoadenylyl sulfate and thioredoxin.

HMOX2 cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently transferred to bilirubin by biliverdin reductase. Under physiological conditions, the activity of HMOX2 is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. HMOX2 participates in the production of carbon monoxide in the brain where it operates as a neurotransmitter. HMOX2 is an essential enzyme in heme catabolism and is involved in cellular response to oxidative stress.

OXSM, a beta-ketoacyl synthetase, is essential for elongation of fatty acid chains in the mitochondria. Alternatively spliced transcript variants were found.

COMT catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to catechol substrates such as the neurotransmitters. This O-methylation results in one of the main degradative pathways of the catecholamine transmitters. COMT COMT is located in the postsynaptic neuron and is involved in the metabolism of catechol estrogen drugs used in the treatment of hypertension, asthma, Parkinson disease and the inactivation of catecholamine neurotransmitters though enzymatic degradation. COMT appears in tissues in 2 forms, a soluble form and a membrane-bound form which differ in their N-termini. COMT inhibitors increase its availability and are used in the treatment of patients with Parkinson's disease.

Glycolate oxidase (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.

Sulfite oxidase, also known as SUOX is a homodimeric protein localized to the intermembrane space of mitochondria. Each subunit includes a heme domain as well as a molybdopterin-binding domain. The SUOX enzyme catalyzes the oxidation of sulfite to sulfate, the last reaction in the oxidative degradation of the sulfur amino acids cysteine and methionine. In addition, the deficiency of SUOX results in neurological abnormalities which are often fatal at an early age.

Alanine aminotransferase 2 (GPT2), catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids. Multiple transcript variants encoding various isoforms have been found for GPT2.

Isopentenyl-diphosphate isomerase 1 (IDI1) belongs to the IPP isomerase type I family and is involved in cholesterol biosynthesis. IDI1 is a peroxisomally-localized enzyme which catalyzes the interconversion of isopentenyl diphosphate (IPP) to its highly electrophilic isomer, dimethylallyl diphosphate (DMAPP), which is the substrate for the sequential reaction that results in the synthesis of farnesyl diphosphate and, eventually, cholesterol. Peroxisomal deficiency diseases such as Zellweger syndrome and neonatal adrenoleukodystrophy show a reduction in IPP isomerase activity.

Thiosulfate sulfurtransferase like domain containing 1 (TSTD1) is a member of a family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. TSTD1 is localized around the nuclear membranes. TSTD1 is expressed in a number of human tissues, including the kidney, liver, skeletal muscle, heart, colon, thymus, spleen, placenta and lung. TSTD1 may participate in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes.

Magnesium-dependent phosphatase 1 (MDP1) is a memeber of the HAD-like hydrolase superfamily. MDP1 is a magnesium-dependent phosphatase which may act as a tyrosine phosphatase. MDP1 is inhibited by vanadate and zinc, and slightly by calcium.

ENO3 is one of three enolase isoenzymes in mammals. The homodimer ENO3 is located in skeletal muscle cells of adults and has a part in converting phosphoglyceric acid to phosphenolpyruvic acid in the glycolytic pathway. Mutations in ENO3 gene is linked to metabolic myopathies which is caused by low stability of the enzyme.

Methionine sulfoxide reductase B (MsrB) from Escherichia coli is a member of the msrB Met sulfoxide reductase family. The E.coli msrB carries out the reduction of methionine-R-sulfoxide to methionine. msrB possess a metal binding site composed of 2 CXXC motifs. The bound metal (zinc or iron) may stabilize the conformation of the enzymes.

Aldolase C Fructose-Bisphosphate (ALDOC) belongs to the class I fructose-bisphosphate aldolase family. ALDOC is a glycolytic enzyme which catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehydes respectively. ALDOC is expressed exclusively in the hippocampus and Purkinje cells of the brain.

L-threonine to glycine degradation consists of a two-step biochemical pathway which involvs the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is initially converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. Glycine C-Acetyltransferase (GCAT) is the 2nd enzyme in this pathway, which subsequently catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The GCAT enzyme is regard as a class II pyridoxal-phosphate-dependent aminotransferase. GCAT is strongly expressed in the heart, brain, liver and pancreas. GCAT is also found in lung.