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CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.

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.

Farnesyl-Diphosphate Farnesyltransferase 1, also known as FDFT1 is a membrane-associated enzyme sited at a branch point in the mevalonate pathway. FDFT1belongs to the phytoene/squalene synthase family. FDFT1 is the 1st specific enzyme in cholesterol biosynthesis, which catalyzes the dimerization of 2 molecules of farnesyl diphosphate in a two-step reaction to form squalene.

Carbonic Anhydrase XIII, also known as CA13 is a member of the alpha-carbonic anhydrase family, which catalyzes the rapid interconversion of carbon dioxide and water tobicarbonate and protons, a reversible reaction which occurs relatively slowly in the absence of catalyst. Furthermore, the active siteof nearly all carbonic anhydrases contains a zinc ion; they have been classified as metalloenzymes. At least fivedistinct CA families (?, ?, ?, ? and ?) have been found. These families have no significant a.a sequence resemblance and in just about allcases are considered to be an example of convergent evolution. The ?-CAs have been demonstrated in humans.

RRM2 catalyzes the formation of deoxyribonucleotides from ribonucleotides. Synthesis RRM2 is regulated in a cell-cycle dependent method. RRM2 supplies the precursors essential for DNA synthesis. RRM2 catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RRM2 Inhibits Wnt signaling.

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.

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.

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.

Glycylpeptide N-tetradecan-oyltransferases 2 (NMT2) is a cytoplasmic protein which is a member of the NMT family of proteins. The proteins in the NMT family catalyze the addition of a myristoyl group to the N-terminal glycine residue of eukaryotic, fungal and viral proteins. These proteins are mostly detected in the heart, gut, kidney, liver and placenta. NMT catalyzes the reaction of N-terminal myristoylation of various signaling proteins. NMT transfers myristic acid from myristoyl coenzyme A to the amino group of a protein's N-terminal glycine residue. There are several distinct NMTs which vary in the molecular weight and /or subcellular distribution.

Sepiapterin Reductase is an aldo-keto reductase that catalyzes the NADPH-dependent reduction of pteridine derivatives and is essential in the biosynthesis of BH4. Mutations in Sepiapterin Reductase gene result in DOPA-responsive dystonia due to sepiaterin reductase deficiency defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Sepiapterin reductase is part of the short-chain dehydrogenase/reductase family which reduces exogenous carbonyl compounds as well as phenylpropanedione. Sepiapterin reductase is an important enzyme for the biosynthesis of tetrahydrobiopterin, an necessary cofactor for aromatic amino acid hydrolases together with tyrosine hydroxylase, the rate-limiting enzyme in dopamine synthesis.

Enolase-phosphatase E1 (ENOPH1) belongs to the MasA family of the HAD (halo-acid dehalogenase)-like hydrolase superfamily. ENOPH1 is a bifunctional enzyme which demonstrates both phosphatase and atypical enolase activities. ENOPH1 has a significant role in the ubiquitous methionine salvage pathway which is a biochemical pathway found in all organisms that regulate methionine levels in the cell.

GGH is a homodimeric protein which catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates. GGH is a vital enzyme in folyl and antifolyl poly-gamma-glutamate metabolism and it has a significant part in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of antifolates and pteroylpolyglutamates.

GNPDA1, catalyzes the conversion of glucosamine-6-phosphate to fructose-6-phosphate, a reaction that under physiological conditions proceeds to the formation of fructose-6-phosphate. GNPDA1 is widely expressed with highest expression in testes, ovary and heart. GNPDA1 triggers calcium oscillations in mammalian eggs. These oscillations are as the necessary trigger for egg activation and early development of the embryo.

Glycogenin-1 (GYG1) is an enzyme involved in glycogen biosynthesis. GYG1 is the chief enzyme involved in glycogen polymerisation. Glycogenin-1 is vital for the function of self-glucosylates, using an inter-subunit mechanism, to form an oligosaccharide primer which acts as substrate for glycogen synthase. In addition, GYG1 has a role in regulating glycogen metabolism and the achievement of maximal glycogen levels in skeletal muscle. GYG1 mRNA and protein content and activity increase in the muscle during recovery from prolonged and exhaustive exercise. GYG1 is inactivated with glycogen catabolism which concurs with an increase in glycogenin gene expression as exercise and glycogenolysis advance. Glycogenin will remain covalently attached to the reducing end of the glycogen molecule.

Fumarase is an enzymatic factor of Krebs cycle, which catalyzes the formation of L-malate from fumarate. Fumarase exists in both a cytosolic form and an N-terminal extended form, differing only in the translation start site used. The N-terminal extended form is aimed to the mitochondrion, where the removal of the extension results in the same form as in the cytoplasm. Fumarase is similar to a number of thermostable Class-2 fumarases and functions as a homotetramer. Mutations in the Fumarase gene causes fumarase deficiency and leads to progressive encephalopathy, cerebral atrophy and developmental delay. Fumarase enzyme is also thought to act as a tumor suppressor. Leydig cell tumors are caused by Fumarase mutations and represents one of the first reports of germline mutations in any type of adult testicular tumor.

Uridine diphosphate glucose pyrophosphatase (NUDT14), is a part of the nudix hydrolase family. NUDT14 is a cytoplasmic protein which contains one nudix hydrolase domain and acts as the sugar donor in numerous glycosylation reactions, including those involved in the production of glycogen. NUDT14 hydrolyzes ADP-ribose into ribose 5-phosphate and AMP, and UDP-glucose to glucose 1-phosphate and UMP. NUDT14 is a homodimer which binds magnesium as a cofactor and is encoded by a gene located on human chromosome 14.

UBE2D2 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2D2 takes part in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. UBE2D2 catalyzes ubiquitination of IkB-alpha in a SCFB-TRCP and phosphorylation dependent method.

Placental alkaline phosphatase also known as PLAP is a membranal siaglycoprotein enzyme typicallyfoundin high concentration in syncytiotrophoblasts in the placenta amid the 3th trimester of gestation. The expression of PLAP was at firstconsidered to be onlyin the term placenta, though, a human PLAP-like variant has been found,thathas more than 85% homology with PLAP itself. PLAP is expressed strictly in normal term placenta, endocervix & fallopian tube and in ovarian and proximal gastrointestinal tumors. It is also widely expressed in germ cell tumors and more recently found in seminomas.

N-6 Adenine-Specific DNA Methyltransferase 1, also known as N6AMT1 is part of the methyltransferase family. N6AMT1 is implicated in the methylation of release factor I during translation termination. In addition, N6AMT1 is involved in converting the arsenic metabolite monomethylarsonous acid to the less toxic dimethylarsonic acid.

NEIL1 is a member of a class of DNA glycosylases homologous to the bacterial Fpg/Nei family. These glycosylases initiate the first step in base excision repair by cleaving bases damaged by reactive oxygen species and introducing a DNA strand break via the associated lyase reaction. NEIL1 participates in the DNA repair pathway by initiating base excision repair by removing damaged bases, primarily oxidized pyrimidines.

Deoxyribodipyrimidine photo-lyase (phrB) is a member of the DNA photolyase class-1 family. phrB takes part in repair of UV radiation-inducedDNA damage. phrB catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidinedimers (in cis-syn configuration), which are formed between closest bases on the same DNA strand uponexposure to ultraviolet radiation.

HPSE also known as Heparanase-1 is an enzyme which cleaves heparan sulfate proteoglycans to allow cell movement through changing the extracellular matrix. In fact, the Heparan sulfate proteoglycans are major components of the basement membrane and extracellular matrix. In addition, this cleavage can release bioactive molecules from the extracellular matrix. HPSE is significant for the overall degradation of proteins in lysosomes.

ATP-dependent Clp protease proteolytic subunit (CLPP) is a member of the peptidase family S14. CLPP cleaves peptides in a variety of proteins in a manner which requires ATP hydrolysis. CLPP being the catalytic core of the Clp proteolytic complex is commonly involved in many cellular processes via the regulation of intracellular protein quality. CLPP is responsible for a somewhat general and central housekeeping function rather than for the degradation of specific substrates.

Glutamic-Pyruvate Transaminase 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.