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NT5C2 (NT5B/PNT5) has a vital role in the maintenance of purine/pyrimidine nucleotides. NT5C2 contains a phosphotransferase active site which catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates. Furthermore, NT5C2 regulates the level of inosine monophosphate (IMP) and guanosine monophosphate (GMP) pools inside cells by way of hydrolysis.

6PGD is the second dehydrogenase in the pentose phosphate shunt. Pentose is neccesary for nucleic acid biosynthesis. The pentose phosphate cycle is a major source of NADPH 6PGD deficiency is usually asymptomatic, and the inheritance of this disorder is autosomal dominant. PGD deficiency raises the erythrocyte pyruvate kinase levels of activity and decreases glutathione synthetase, resulting in hemolysis.

GRHPR located in the cytosol, belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family of proteins. GRHPR is widely expressed in liver. GRHPR has widespread tissue expression and is involved in metabolism. GRHPR is an enzyme with hydroxypyruvate reductase, glyoxylate reductase, and D-glycerate dehydrogenase enzymatic activities.

Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.

Acid Phosphatase-5, also known as ACP5 is a member of the Purple acid phosphatase family. ACP5 is implicated in osteopontin as well as bone sialoprotein dephosphorylation. ACP5 expression appears to increase in certain pathological states for instance Gaucher & Hodgkin diseases, the hairy cell, the B-cell, as well as the T-cell leukemias.

Adenylate kinases play a role in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. There are 3 types of adenylate kinase isozymes, AK1, AK2, and AK3 in vertebrates. Expression of these isozymes are tissue-specific and developmentally regulated. AK2 is localized in the mitochondrial intermembrane space and is involved in apoptosis. AK2 is mutated in individuals with reticular dysgenesis.

DPP4 also called adenosine deaminase complexing protein-2, and T-cell activation antigen CD26 is a serine exopeptidase and complex enzyme that is expressed on the surface of most cell types. DPPIV is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. DPP4 plays a role in t-cell activation. DPP4 is associated with intracellular signal transduction, apoptosis and involved in tumor biology. There are at least 63 substrates which can bind specifically to DPP4 enzyme including growth factors, chemokines, neuro peptides. Furthermore, DPP4 plays a major role in glucose metabolism by cleaving incretins such as glucose-dependent insulinotropic polypeptide (GIP) and GLP-1.

HEXA is the alpha subunit of the lysosomal enzyme beta-hexosaminidase which, combined with the cofactor GM2 activator protein, catalyzes the degradation of the ganglioside GM2, and other molecules having N-acetyl hexosamines terminus. The two subunits composing Beta-hexosaminidase, alpha and beta, belong to the glycosyl hydrolases family and are encoded by distinct genes. Alpha subunit gene mutations can cause Tay-Sachs disease (GM2-gangliosidosis type I).

Phosphopantothenate-cysteine ligase (PPCS) catalyzes the first step in the biosynthesis of coenzyme A (CoA) from pantothenic acid (vitamin B5), which is a vital universal pathway in prokaryotes and eukaryotes. PPCS, being one of the last enzymes in this pathway, converts phosphopantothenate to phosphopantothenoylcysteine.

STK17A belongs to the DAP kinase-associated apoptosis-inducing protein kinase family and encodes an autophosphorylated nuclear protein with a protein kinase domain. STK17A acts as a positive regulator of apoptosis. STK17A is greatly expressed in the placenta with lower levels in the heart, lung, skeletal muscle, kidney and pancreas.

UBE2E1 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2E1 accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. UBE2E1 catalyzes the covalent attachment of ISG15 to other proteins. UBE2E1 mediates the selective degradation of short-lived and abnormal proteins. In vitro, UBE2E1 also catalyzes 'Lys-48'-linked polyubiquitination.

MGLL is a membrane-associated member of the serine hydrolase superfamily. MGLL is expressed in abundance in skeletal muscle and adipose tissue. MGLL functions jointly with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides.

Queuine TRNA-Ribosyltransferase 1 also known as QTRT1 is a member of the queuine tRNA-ribosyltransferase family. QTRT1 interacts with QTRTD1 to form an active queuine tRNA-ribosyltransferase. Furthermore, QTRT1 exchanges queuine for the guanine at the wobble position of tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr), in this manner forming the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).

ADH1C is a member of the zinc-containing alcohol dehydrogenase family which metabolizes a large assortment of substrates, such as ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH1 is a monomorphic and a key factor in fetal and infant livers, becoming less active in gestation and only weakly active during adulthood.

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.

4-Hydroxyphenylpyruvate Dioxygenase Isoform-1 is an Fe-containing enzyme, which catalyzes the second reaction in the catabolism of tyrosine the conversion of 4-hydroxyphenylpyruvate to homogentisate. Present as a homodimer, HPD uses zinc as a cofactor to catalyze the third step in the conversion of L-phenylalanine to fumarate and acetoacetic acid. Flaws in the gene encoding HPD result in tyrosinemia type 3 and hawkinsinuria, two inborn defects of metabolism which are related to a number of symptoms, like mental retardation and seizures and hair and urine abnormalities.

Mimitin (NDUFAF2) is a member of the complex I NDUFA12 subunit family.NADH dehydrogenase is an enzyme located in the inner mitochondrial membrane, which catalyzes the transfer of electrons from NADH to coenzyme Q (CoQ). NDUFAF2 is the "entry enzyme" of oxidative phosphorylation in the mitochondria. Mimitin protein functions as a molecular chaperone for mitochondrial complex I assembly.

Threonyl-tRNA Synthetase is a member of the aminoacyl-tRNA synthetase family, key enzymes of protein biosynthesis which charge tRNA molecules with the respective amino acids. This 83 kDa protein is an autoantigen recognized by PL-7 antibodies which occur in a subset of patients with polymyositis and dermatomyositis. Preliminary data suggest that PL-7 antibodies (similar to Jo-1 antibodies) indicate an increased risk for lung involvement, but this needs to be confirmed for a larger number of cases.

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.

Isocitrate Dehydrogenase is an enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle.

OTC is a member of the ATCase/OTCase family. OTC has a key part in the urea cycle, catalyzing the second step in this pathway: the transformation of L-orthinine and carbamoyl phosphate to L-citrulline. In humans, the urea cycle is a vital pathway to detoxification of ammonia. Alterations in the gene encoding OTC are linked to the X-linked disorder OTCD (ornithine carbamoyltransferase deficiency). OTCD disorder of the urea cycle is characterized by hyperammonemia.

Carbohydrate Sulfotransferase 10, also known as CHST10 is a member of the sulfotransferase 2 family. CHST10 was first recognized as a sulfotransferase which acts on the human natural killer-1 (HNK-1) glycan. Furthermore, CHST10 is a carbohydrate involved in neurodevelopment as well as synaptic plasticity.

ADP-ribosylhydrolase like 2 (ADPRHL2) belongs to the ADP-ribosylglycohydrolase family. ADPRHL2 catalyzes the removal of ADP-ribose from ADP-ribosylated proteins. ADPRHL2, which is ubiquitously expressed, uses magnesium as a cofactor to catalyze the hydrolysis of poly (ADP-ribose) that is synthesized after DNA damage. Furthermore, ADPRHL2 has an essential role in the maintenance of normal neuronal cell function. The ADPRHL2 enzyme localizes to the mitochondria, in addition to the nucleus and cytoplasm.

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.