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Carbonic Anhydrase 3 (CA3) belongs to the Alpha-Carbonic Anhydrase family that encodes carbonic anhydrase isozymes. These carbonic anhydrases are a class of metalloenzymes that catalyse the reversible hydration of carbon dioxide and are differentially expressed in a number of cell types. The expression of the CA3 gene is strictly tissue specific and it is present at high levels in skeletal muscle with much lower levels found in cardiac and smooth muscle. CA3 is activated by proton donors such as imidazole and the dipeptide histidylhistidine. CA3 is inhibited by coumarins and sulfonamide derivatives such as acetazolamide.

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N-Acetylglucosamine-6-Sulfatase is a member of the Sulfatase family. N-Acetylglucosamine-6-Sulfatase is required for the lysosomal degradation of the Glycosaminoglycans (GAG) Heparan Sulfate and Keratan Sulfate. N-Acetylglucosamine-6-Sulfatase hydrolyses the 6-Sulfate groups of the N-Acetyl-D-Glucosamine 6-Sulfate units of Heparan Sulfate and Keratan Sulfate. N-Acetylglucosamine-6-Sulfatase binds 1 Calcium ion per subunit. N-Acetylglucosamine-6-Sulfatase deficiency are the cause of Mucopolysaccharidosis Type 3D (MPS3D), an inborn error leading to lysosomal accumulation of heparan sulfate. MPS3D has profound mental deterioration, hyperactivity, and relatively mild somatic manifestations.

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Human nicotinate phosphoribosyltransferase (NAPRTase) is localised in the cytoplasm and is involved in biological processes such as NAD biosynthetic and metabolic processes, nicotinamide metabolic process, nicotinate nucleotide salvage, response to oxidative stress and water-soluble vitamin metabolic process. It functions by catalyzing the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN) and is essential for NA to increase cellular NAD levels and prevent oxidative stress of the cells. It is a crucial factor in the NAD+ biosynthesis pathway. Catalytic activity: Beta-nicotinate D-ribonucleotide + diphosphate = nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate.

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Carbonic Anhydrase 5B (CA5B) is a member of alpha-carbonic anhydrase family (CAs) that catalyze the reversible hydration of carbon dioxide. CAs is associated with many biological processes, including calcification, respiration, bone resorption, acid-base balance and the formation of aqueous humor. CA5B is highly expressed in heart, pancreas, kidney, placenta, lung, and skeletal muscle, but it is restricted to the liver. CA5B is localised in the mitochondria and shows the highest sequence similarity to the other mitochondrial CA, CA-VA. CA5B is inhibited by coumarins, sulfonamide derivatives such as acetazolamide (AZA), saccharin, and Foscarnet.

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Endoplasmic Reticulum Mannosyl-Oligosaccharide 1,2- alpha-Mannosidase (MAN1B1) belongs to the glycosyl hydrolase 47 family. MAB1B1 is a single-pass type II membrane protein and widely expressed in many tissues. MAB1B1 is involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. MAB1B1 can be inhibited by both 1-deoxymannojirimycin (dMNJ) and kifunensine. Defects in MAN1B1 are the cause of mental retardation autosomal recessive type 15 (MRT15). Mental retardation is characterised by significantly below average general intellectual functioning, it is also associated with impairments in adaptative behavior and manifested during the developmental period.

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Human Esterase D is a serine hydrolase that is involved in the detoxification of formaldehyde. Esterase D plays a part in a variety of substrates, including O-acetylated sialic acids, which may involves in the recycling of sialic acids. Esterase D can be used as a genetic marker for retinoblastoma and Wilson’s disease.

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GALK2 acts as a galactokinase when galactose is present at high concentrations. GALK2 may be involved in a salvage pathway for the reutilisation of free GalNAc derived from the degradation of complex carbohydrates. GALK2 has been reported to participate in pathways , such as Amino sugar and nucleotide sugar metabolism, Galactose metabolism and Metabolic pathways.

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Lysine-tRNA ligase, also known as Lysyl-tRNA synthetase, LysRS, KARS and KIAA0070, belongs to the class-II aminoacyl-tRNA synthetase family. The N-terminal cytoplasmic domain (1-65) is a functional tRNA-binding domain, which is required for nuclear localisation, is involved in the interaction with DARS, but has a repulsive role in the binding to EEF1A1. A central domain (208-259) is involved in homodimerisation and is required for interaction with HIV-1 GAG and incorporation into virions. KARS catalyses the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Defects in KARS are the cause of Charcot-Marie-Tooth disease recessive intermediate type B (CMTRIB).

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NAD kinase catalyses the transfer of a phosphate group from ATP to NAD+ to generate NADP+, which in its reduced form acts as an electron donor for biosynthetic reactions. NADP+ is an essential coenzyme in metabolism and provides reducing power to biosynthetic processes such as fatty acid biosynthesis.

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Sulfotransferase 1A3/1A4 (SULT1A3) is 295 amino acids in length and localises to the cytoplasm. It is a member of the Sulfotransferase 1 family. SULT1A3 can be found in the liver, colon, kidney, lung, brain, spleen, small intestine, placenta, and leukocytes. SULT1A3 exists as a homodimer and it catalyses the sulfation of phenolic monoamines, such as dopamine, norepinephrine and serotonin, and phenolic and catecholic drugs.

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Carboxypeptidase Q (Cpq) is a member of the peptidase M28 family. PGCP is involved in a number of fundamental biological processes such as the hydrolysis of circulating peptides, catalyzing the hydrolysis of dipeptides with unsubstituted terminals into amino acids. Carboxypeptidase may play an important role in the liberation of thyroxine hormone from its thyroglobulin (Tg) precursor. The monomeric form is inactive while the homodimer is active.

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Carnosine Dipeptidase 1 (CNDP1) belongs to the M20 metalloprotease family. CNDP1 is specifically expressed in the brain, serum and adult nervous central system. It is identified as human carnosinase. CNDP1 contains trinucleotide (CTG) repeat length polymorphism in the coding region and is inhibited by the metal chelator 1,10-o-phenantrolin. In addition, CNDP1 can hydrolyse the beta-Ala|-His dipeptide (carnosine), anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine. CNDP1 deficiency has been associated with homocarnosinosis disease.

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beta -1,4-galactosyltransferase 4 (B4GALT4) is a single-pass type II membrane protein that belongs to the Glycosyltransferase 7 family. B4GALT4 consist of the following 2 domains: N-Acetyllactosamine Synthase and beta -N-Acetylglucosaminyl-Glycolipid beta -1,4-Galactosyltransferase. B4GALT4 is highly expressed in the heart, placenta, kidney, and pancreas; it is lowly expressed in the brain, colon, lung, muscle, ovary, testis, and uterus. B4GALT4 function is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.

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Isocitrate Dehydrogenase [NADP] Cytoplasmic (IDH1) belongs to the isocitrate and isopropylmalate dehydrogenases family. IDH1 exists as a homodimer, binding one magnesium or manganese ion per subunit. Mutations of IDH1 have been shown to cause metaphyseal chondromatosis with aciduria and are involved in the development of glioma IDH plays a role in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid.

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Isocitrate Dehydrogenase [NADP] Cytoplasmic (IDH1) belongs to the isocitrate and isopropylmalate dehydrogenases family. IDH1 exists as a homodimer, binding one magnesium or manganese ion per subunit. Mutations of IDH1 have been shown to cause metaphyseal chondromatosis with aciduria and are involved in the development of glioma IDH plays a role in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid.

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Ribonuclease 3 (RNASE3) is a basic protein that is localised to the eosinophil primary matrix and belongs to the pancreatic ribonuclease family. RNASE3 is released during degranulation of eosinophils. RNASE3 possesses a wide variety of biological activities. RNASE3 interacts with bacterial lipopolysaccharide (LPS) and lipoteichoic acid (LTA). RNASE3 exhibits antibacterial activity, including cytoplasmic membrane depolarisation of preferentially Gram-negative, but also Gram-positive strains. It promotes E. coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.

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Deoxyuridine 5'-Triphosphate Nucleotidohydrolase Mitochondrial (dUTPase) belongs to the dUTPase family. dUTPase exits as a homotrimer and is involved in nucleotide metabolism. dUTPase produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. The dUTPase increase in PCR product yield, length and fidelity enables further down-stream applications. These effects make dUTPase useful in PCR fidelity and yield-sensitive applications. dUTPase is specific for dUTP and is critical for the fidelity of DNA replication and repair.

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Peptidyl-Prolyl Cis-Trans Isomerase FKBP7 (FKBP7) is a member of the FKBP-type peptidyl-prolyl cis/trans isomerase (PPIase) family. FKBP7 contains two EF-hand domains and one PPIase FKBP-type domain. FKBP7 exhibits PPIase activity and function as molecular chaperones. In addition, FKBP7 accelerates the folding of proteins during protein synthesis. It has been shown that Hsp90 complex to the nucleus bind its PPIase domain to cytoplasmic dynein, the motor protein responsible for retrograde movement along microtubules.

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Thimet Oligopeptidase (THOP1) belongs to the peptidase M3 family which includes neurolysin and mitochondrial intermediate peptidase. THOP1 is located in Cytoplasm. THOP1 is widely expressed in human tissues and can detected in different subcellular locations. THOP1 is preferential cleavage for bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues. THOP1 is involved in the metabolism of neuropeptides under 20 amino acid residues and degradation of cytoplasmic peptide. In addition, THOP1 also can degrade the beta-amyloid precursor protein and generate amyloidogenic fragments.

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Inositol Monophosphatase 1 (IMPA1) belongs to the inositol monophosphatase family. IMPA1 is responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides, IMPA1 can use myo-inositol-1,3-diphosphate, myo-inositol-1,4-diphosphate, scyllo-inositol-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2-AMP as substrates. IMPA1 has been implicated as the pharmacological target for lithium action in brain. IMPA1 shows magnesium-dependent phosphatase activity and is inhibited by therapeutic concentrations of lithium. In addition, IMPA1 plays a improtant role in intracellular signal transduction.

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Carbonic Anhydrase 8 (CA8) belongs to the alpha-carbonic anhydrase family. Alpha-carbonic anhydrase is a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. Because CA8 has some sequence similarity with other known carbonic anhydrase genes, it was firstly called as CA-related protein. Nevertheless, CA8 does not have a carbonic anhydrase catalytic activity. Defects in CA8 are the cause of cerebellar ataxia mental retardation and dysequilibrium syndrome type 3 (CMARQ3), which is a congenital cerebellar ataxia associated with dysarthia, quadrupedal gait and mild mental retardation.

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Brain-Specific Serine Protease 4 (BSSP-4) is a serine protease that preferentially cleaves the synthetic substrate H-D-Leu-Thr-Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA. BSSP-4 is expressed abundantly in the epithelial cells of the airways, including trachea, esophagus and fetal lung, but scarce in adult lung and expressed at low levels in placenta, pancreas, prostate and thyroid gland. BSSP-4 belongs to the peptidase S1 family and related to trypsin, referentially hydrolyzing substrates after arginine and lysine residues. However, BSSP-4 is less susceptible to inhibition by common trypsin inhibitors such as aprotinin, alpha1-antitrypsin and secretory leukocyte protease inhibitor. BSSP-4 efficiently converts pro-urokinase- type plasminogen activator to its mature, active form.

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Lon Protease, is a member of the Lon protease family. They are found in archaea, bacteria and eukaryotes. Lon protease is ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins, including some antitoxins. It required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. It degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long and binds to DNA in a double-stranded, site-specific manner. Endogenous substrates include the regulatory proteins RcsA and SulA, the transcriptional activator SoxS, and UmuD. Its overproduction specifically inhibits translation through at least two different pathways, one of them being the YoeB-YefM toxin-antitoxin system.

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Collagenases are enzymes that break the peptide bonds in collagen.

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Collagenases are enzymes that break the peptide bonds in collagen.

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Ascorbate Oxidase is an enzyme belonging to the family of oxidoreductases that catalyses the reaction: Ascorbic acid +¹/₂ O₂ ascorbate oxidase → Dehydroascorbic acid +H₂O.

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Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) is a cytosolic enzyme in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH).

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One bacterial amylase unit is defined as that quantity of enzyme which will dextrinise one milligram of starch per minute at pH 6,6 and 30 °C.

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Papain, powder, purified, is a cysteine protease enzyme the is present in the papaya fruit.

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Collagenases degrade native helical collagen fibrils. The enzyme has an important role in connective tissue metabolism and is produced by specific cells involved in repairs and remodelling processes. It is a type II enzyme that contains greater clostripain activity. It is generally used for heart, bone, muscle, thyroid, cartilage, and liver cells. Ca²⁺ is required for its activation while metal chelating agents such as cysteine, EDTA or o-phenanthroline inhibits its activity.