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MUTM is a base excision repair enzyme that identifies and eliminates a large variety of oxidized purines from correspondingly impaired DNA. MUTM is nondismissable and essential to remove quickly its substrate lesions on the chromosome. MUTM, additionally, mends a large number of the lesions recognized by Endo III, signifying that MUTM takes a prominent part in the overall repair of both purine damage and pyrimidine damage in vivo.

ENO1 is a homodimeric soluble protein that encodes a smaller monomeric structural lens protein, tau-crystallin. ENO1 is a glycolytic enzyme expressed in mainly all tissues. ENO1 isoenzyme full length protein is found in the cytoplasm. The shorter protein is formed from another translation start that is restricted to the nucleus, and binds to a component in the c-myc promoter. ENO1 is involved in anaerobic metabolism under hypoxic conditions and plays a role as a cell surface plasminogen receptor during tissue invasion. Irregular expression of Enolase-1 is linked with tumor progression in several cases of breast and lung cancer. Enolase-1 is as an auto antigen associated with Hashimoto's encephalopathy and severe asthma. ENO1 is the target protein of serum anti-endothelial antibody in Behcet's disease.

Carbonic Anhydrase VIII or CA8 was previously called CA-related protein due to its sequence resemblance to additional recognized carbonic anhydrase genes. Nonetheless CA8 doesn’t have carbonic anhydrase function. This protein keeps bearing a carbonic anhydrase classification because of coherent sequence similarity to additional proteins in carbonic anhydrase family. Mutations in this protein may lead to cerebellar dysequilibrium syndrome type 3 or ataxia mental retardation.

GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 is invloved in amino acid metabolism and the urea and tricarboxylic acid cycles. The 2 enzymes are homodimeric and demonstrate close homology.

HDAC2 is a member of the histone deacetylase family that performs through the construction of large multiprotein complexes and are in charge of the deacetylation of lysine residues on the N-terminal region of the core histones. HDAC2 forms transcriptional repressor complexes by relating to a diversity of proteins, like YY1- a mammalian zinc-finger transcription factor.
In addition, HDAC2 has a vital part in transcriptional regulation, cell cycle progression and developmental procedures.

BAT1 belongs to the DEAD box family of RNA-dependent ATPases that mediate ATP hydrolysis during pre-mRNA splicing. UAP56 protein is a vital splicing factor which is needed for connecting U2 small nuclear ribonucleoprotein with pre-mRNA, as well as takes a key part in mRNA export from the nucleus to the cytoplasm. Mutations in this protein may be connected to rheumatoid arthritis.

PRSS3 is a trypsinogen, and a member of the trypsin family of serine proteases. PRSS3 is expressed in the pancreas and brain and is unaffected by common trypsin inhibitors. It is active on peptide linkages involving the carboxyl group of lysine or arginine. PRSS3 is restricted to the locus of T cell receptor beta variable orphans on chromosome 9. 4 different isoforms encoded by 4 transcript variants were identified for this gene.

Adenosine deaminase-like protein (ADAL) is a putative nucleoside deaminase. ADAL catalyzes the hydrolytic deamination of adenosine or some similar substrate and has a role in purine metabolism.

Cytochrome b5 reductase 1 (CYB5R1) is a part of the flavoprotein pyridine nucleotide cytochrome reductase family. CYB5R1 is engaged in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin decrease.

Arsenic Methyltransferase (AS3MT) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to trivalent arsenical and may have a role in arsenic metabolism. AS3MT methylates arsenite to produce methylarsonate, Me-AsO3H2, which is reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2. Methylarsonite which is also a substrate, is transformed into the much less toxic complex dimethylarsinate (cacodylate), Me2As(O)-OH.

Creatine Kinase BB is a cytoplasmic enzyme involved in energy homeostasis. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in brain as well as in other tissues, and as a heterodimer with a similar muscle isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. A pseudogene of this gene has been characterized.

SDSL belongs to the serine/threonine dehydratase family and function as a serinespecific dehydratase. SDSL utilizes pyridoxal phosphate and is one of three key enzymes which take part in the metabolism of Glycine and serine.

Glutamyl-TRNA Amidotransferase, Subunit C also known as GATC allows the formation of properly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction occurs in the attendance of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). In addition, GATC is subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (PET112) and C (GATC) subunits.

NADH Dehydrogenase 1 Beta Subcomplex 4 (NDUFB4) is a member of the complex I NDUFB4 subunit family. NDUFB4 is a non-catalytic subunit of the multisubunit NADH:ubiquinone oxidoreductase, which is the first enzyme complex in the mitochondrial electron transport chain (complex I). Mammalian complex I is comprised of 45 different subunits and transfers electrons from NADH to ubiquinone.

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.

Paraoxonase 1 also called Esterase-A is involved in the detoxification of organophosphate insecticides such as parathion. Paraoxonase 1 may also confer protection against coronary artery disease by destroying proinflammatory oxidized lipids present in oxidized low-density lipoproteins (LDLs).

METTL1 is recognized as tRNA (guanine-N(7)-)-methyltransferase that is a part of the methyltransferase superfamily. METTL1 displays high sequence similarity to yeast ORF YDL201w and can be inactivated by phosphorylation. METTL1 protein has a conserved S-adenosylmethionine-binding motif and ccatalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.

Alcohol dehydrogenase 1A (ADH1A) is a member of the alcohol dehydrogenase family. ADH1A has a key role in ethanol metabolism. ADH1A along with coenzyme NAD catalyzes the reversible conversion of organic alcohols to ketones or aldehydes. The physiologic function of ADH1A in the liver is the elimination of ethanol formed by microorganisms in the intestinal tract. ADH1A is monomorphic and predominant in fetal and infant livers, growing to be less active in gestation and only weakly active during adulthood.

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.

Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase1 encodes a ubiquitous form of hexokinase which localizes to the outer membrane of mitochondria. Mutations in this gene have been associated with hemolytic anemia due to hexokinase deficiency. Alternative splicing of HXK1 results in five transcript variants which encode different isoforms, some of which are tissue-specific. Each isoform has a distinct N-terminus; the remainder of the protein is identical among all the isoforms. A sixth transcript variant has been described, but due to the presence of several stop codons, it is not thought to encode a protein.

Pyridoxal phosphate phosphatase PHOSPHO2, orphan 2 (PHOSPHO2) is a member of the haloacid dehalogenase (HAD) superfamily. Phosphatase has an elevated activity toward phosphoethanolamine (PEA) and phosphocholine (PCho). PHOSPHO 1, a phosphoethanolamine/phosphocholine phosphatase, is upregulated in mineralizing cells and is believed to be implicated in the production of inorganic phosphate for bone mineralization. PHOSPHO2 is a recognized phosphatase sharing a 42% sequence identity with PHOSPHO1. PHOSPHO1 and PHOSPHO2 are especially similar, however surprisingly recombinant PHOSPHO2 hydrolyses phosphoethanolamine and phosphocholine comparatively inadequately.

GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.

Obg-like ATPase 1 (OLA1) acts as a negative regulator of the cellular antioxidant response independent of transcriptional processes. OLA1 curbs the antioxidant response via nontranscriptional mechanisms. OLA1 hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. OLA1 is clearly down-regulated by DNA damage-inducing agents. OLA1 is expressed in all tissues; however it is more abundant in the testis, liver, lung, and brain. OLA1 is overexpressed in a number of malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus.