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6PGD is the 2nd dehydrogenase in the pentose phosphate shift. Pentose is crucial for the biosynthesis of nucleic acid. The pentose phosphate cycle is a prominent source of NADPH. 6PGD deficiency is mostly asymptomatic, and the inheritance of this deasis is autosomal dominant. PGD deficiency elevate the erythrocyte pyruvate kinase levels of activity & decreases glutathione synthetase, which causes hemolysis.

Arylsulfatase A (ARSA) hydrolyzes cerebrosidesulfate to cerebroside and sulfate. ARSA is inhibited by phosphate. The phosphate develops a covalent bond with the active site 3-oxoalanine. ARSA gene defects cause metachromatic leucodystrophy (MLD), a progressive demyelination disease which results in various neurological symptoms and ultimately death.

Phosphoribosylaminoimidazole Carboxylase (PAICS) is an enzyme involved in nucleotide biosynthesis and particularly in purine biosynthesis. PAICS is a bifunctional enzyme containing phosphoribosylaminoimidazole carboxylase activity at its N-terminal region and phosphoribosylaminoimidazole succinocarboxamide synthetase at its C-terminal region. PAICS catalyzes the conversion of 5'-phosphoribosyl-5-aminoimidazole(AIR) into 5'-phosphoribosyl-4-carboxy-5-aminoimidazole (CAIR) as described in the reaction. PAICS catalyzes steps six and seven of purine biosynthesis.

NUDT10 belongs to the Nudix hydrolase family of pyrophosphatases. Nudix hydrolases contain a characteristic Nudix domain and are responsible for catalyzing the hydrolysis of nucleoside diphosphate derivatives. NUDT10 functions as a manganese-dependent polyphosphate phosphohydrolase with an optimum pH of 8.5. NUDT10 protein specifically metabolizes diadendosine-polyphosphates and, to a lesser extent, diphosphoinositol polyphosphates.

UbcH10 is an essential mediator of mitotic destruction events and cell cycle progression. It catalyzes the destruction of cyclins A and B in conjunction with the anaphase-promoting complex, and therefore, plays an important role in the control of the cell exit from mitosis This activity is essential at then end of mitosis for the inactivation of their partner kinase Cdc2 and exit from mitosis into G1 of the next cell cycle. In addition, UbcH10 bears homology to yeast PAS2, a gene that is essential for biogenesis of peroxisomes. UbcH10 is useful for in vitro ubiquitinylation reactions.

HIBCH enzyme is in charge of hydrolysis of both HIBYL-CoA and beta-hydroxypropionyl-CoA. Damages in the HIBCH gene linked to 3-hyroxyisobutyryl-CoA hydrolase deficiency. Multiple transcript variants exist as a result of alternative splicing.

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.

HAGH is a part of the glyoxalase family and a thiolesterase which hydrolyses S-lactoyl-glutathione to reduced glutathione and D-lactate. HAGH protein is a detoxifying enzyme of glycolysis byproduct methylglyoxal and a target of p63 and p73 and serves as a pro-survival factor of the p53 family. HAGH appears only as a monomer and binds two zinc ions per subunit.

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.

Rhodanese is a mitochondrial matrix enzyme that is encoded by the nucleus. Rhodanese is involved in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes. Rhodanese catalyzes the chemical reaction of thiosulfate & cyanide to sulfite & thiocyanate (detoxification). Rhodanese is part of the transferase family of proteins. Rhodanese includes two highly conservative domains, identified as rhodanese homology domains. In mammals, the majority of cyanide is converted to thiocyanate. Rhodanese has weak mercaptopyruvate sulfurtransferase activity.

ACADS is a tetrameric mitochondrial flavoprotein, which is part of the acyl-CoA dehydrogenase family. ACADS catalyzes the first step of the mitochondrial fatty acid beta-oxidation pathway. Mutations in ACADS have been associated with Short Chain Acyl-CoA Dehydrogenase Deficiency.

Ornithine decarboxylase is the preliminary and rate-limiting enzyme in the biosynthetic pathway of polyamines and it takes part in the alteration of ornithine to putrescine. ODC1 is a key member of various biological processes, such as cell growth, transformation, differentiation and apoptosis. Overexpression of the ODC1 gene has a vital part in cell proliferation and the progress of cancer.

HAAO is a monomeric cytosolic protein which is a member of intramolecular dioxygenases family containing nonheme ferrous iron. The HAAO protein catalyzes the synthesis of quinolinic acid (QUIN) from 3-hydroxyanthranilic acid. QUIN is an excitotoxin whose toxicity is facilitated by its ability to activate glutamate N-methyl-D-aspartate receptors. Amplified cerebral levels of QUIN may contribute to the pathogenesis of neurologic and inflammatory disorders. HAAO is widely distributed in peripheral organs, such as liver and kidney, and is also present in low amounts in the central nervous system.

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.

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

NDUFS2 is a core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which is a part of the minimal assembly required for catalysis. Complex I takes part in the transfer of electrons from NADH to the respiratory chain. Histidine NADH Dehydrogenase Fe-S Protein 2 (NDUFS2) is required for catalytic activity. Imperfections in NDUFS2 are the source of complex I mitochondrial respiratory chain deficiency, which is characterized by many symptoms including liver failure, cardiomyopathy and neurodegeneration.

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.

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.

Ribulose-phosphate 3-epimerase (RPE) is a member of the ribulose-phosphate 3-epimerase family. RPE is the enzyme which converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. Therefore, the RPE enzyme has one substrate, D-ribulose 5-phosphate, and one product, D-xylulose 5-phosphate. RPE participates in three metabolic pathways: pentose phosphate pathway, pentose and glucuronate interconversions, and carbon fixation.

ALAD form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins) by catalyzing the compression of 2 molecules of delta-aminolevulinate. ALAD catalyzes the second step in the porphyrin and heme biosynthetic pathway; zinc is vital for enzymatic activity. ALAD has 8 identical subunits and its enzymatic activity is inhibited by lead. Mutations in the ALAD structural gene are the source for high sensitivity to lead poisoning and acute hepatic porphyria.

Insulin-Degrading Enzyme (IDE) is a zinc metallopeptidase which degrades intracellular insulin, and thus terminates insulins activity, as well as playing a part in intercellular peptide signaling by degrading various peptides such as amylin, bradykinin, and kallidin. The preferential affinity of the IDE enzyme for insulin results in insulin-mediated inhibition of the degradation of additional peptides such as beta-amyloid. Deficiencies in IDE protein's function are linked with Alzheimer's disease and type 2 diabetes mellitus nevertheless mutations in the IDE gene have not been demonstrated to be causative for these diseases. Insulin-Degrading Enzyme localizes mainly to the cytoplasm however in some cell types it localizes to the extracellular space, cell membrane, peroxisome, and mitochondrion. In addition, IDE degrades amyloid formed by APP and IAPP. Furthermore, IDE plays a part in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.

Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm of Escherichia coli. DsbC is periplasmic enzyme known as a disulfide isomerase and can convert aberrant disulfide bonds to correct ones.

LDHB is part of the lactate dehydrogenase family. LDHB is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. LDHB catalyzes the oxidation of hydroxybutyrate, and frequently called Hydroxybutyrate Dehydrogenase (HBD). The LDH family consists of three members, LDH-A, LDH-B and LDH-C. LDHs function as powerful markers for germ cell tumors.

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.