Enzymes

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Sulfotransferase 4A1 (ST4A1) is a member of the Sulfotransferase 1 family. ST4A1 is highly expressed in the cerebral cortex and frontal lobe, but no expression is detected in the pancreas. ST4A1 is a brain-specific sulfotransferase believed to be involved in the metabolism of neurotransmitters. ST4A1 acts on catecholamines and T4 in a manner that may not involve sulfonation. ST4A1 may have a role in the metabolism of drugs and neurotransmitters in the CNS. In addition, ST4A1 is related to schizophrenia.

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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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LTA4H, which is short for Leukotriene A-4 hydrolase, is a 611 aa. protein. It belongs to the peptidase M1 family, and exists in cytoplasm. This protein has at least 4 isforms produced by alternative splicing, and two of them are expressed in monocytes, lymphocytes, neutrophils, reticulocytes, platelets and fibroblasts. LTA4H involves in lipid metabolism and leukotriene B4 biosynthesis. It is a epoxide hydrolase that catalyses the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. It also has aminopeptidase activity.

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Nicotinate Phosphoribosyltransferase (NAPRTase) is involved in the biological processes of pyridine nucleotide biosynthesis and nicotinate nucleotide salvage and functions by catalyzing the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN). 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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Carboxypeptidase B1 is an exopeptidase which specifically cleaves the C-terminal Arg and Lys residues with a preference for Arg. Expressed mainly in pancreas, CPB1 is a useful serum marker for acute pancreatitis and pancreatic graft rejection.Human CPB1 consists of a signal peptide, a pro region, and a mature chain. The purified rhCPB1 corresponds to the pro form, which can be activated by trypsin, the only pancreatic protease capable of generating active enzyme from the zymogen in vitro.

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Nicotinate-Nucleotide Pyrophosphorylase (QPRT) belongs to the nadC/modD family. QPRT plays an improtant role in catabolism of quinolinate which acts as a potent endogenous exitotoxin to neurons. In addition, QPRT serves as an an intermediate in the Tryptophan-Nicotinamide Adenine Dinucleotide pathway. QPRT participates in some pathways including Cofactor biosynthesis, NAD(+) biosynthesis and the Nicotinate D-Ribonucleotide from Quinolinate. In addition, QPRT is involved in the catabolism of Quinolinic Acid (QA). The activity toward QA is slightly repressed by phosphoribosylpyrophosphate (PRPP) in both a competitive and a non-competitive manner.

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Aminoglycoside 3'-phosphotransferase (APH(3')), also known as aminoglycoside kinase, is an aminoglycoside-modifying enzyme and widely presented in resistant bacteria. These ATP-dependent enzymes phosphorylate the 3'-hydroxyl of a variety of aminoglycosides including kanamycins, neomycins, paromomycins, neamine, ribostamycin, geneticin, and paromamine. These phosphorylated aminoglycosides fail to bind to their respective ribosomal binding sites with high affinity; hence resistance is conferred to the drugs that are phosphorylated. APH(3') is primarily found in certain species of gram-positive bacteria.

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Dipeptidase 1 (DPEP1) is a kidney membrane enzyme that belongs to the peptidase M19 family. DPEP1 is a homodimer and is inhibited by L-penicillamine. DPEP1 hydrolyses a variety of dipeptides and is implicated in renal metabolism of glutathione and its conjugates. DPEP1 is responsible for hydrolysis of the beta-lactam ring of antibiotics, such as penem and carbapenem. DPEP1 may play an important role in the regulation of leukotriene activity. DPEP1 expression in cancer is significantly higher than that in normal tissue. However, DPEP1 expression decreased with pathological differentiation, lymph-node and distant metastasis.

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Fructose-bisphosphate aldolase C (ALDOC) belongs to the class I fructose-bisphosphate aldolase family. It is an enzyme that, in humans, is encoded by the ALDOC gene. ALDOC is expressed exclusively in the hippocampus and Purkinje cells of the brain. ALDOC is a glycolytic enzyme which catalyses the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehydes respectively

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Lysosomal Pro-X Carboxypeptidase (PRCP) belongs to the peptidase S28 family. PRCP is detected in many tissues, with highest levels observed in placenta, lung, and liver. It is also present in the heart, brain, pancreas, and kidney. PRCP exists as a homodimer. PRCP cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH. PRCP has been shown to be an activator of the cell matrix-associated prekallikrein.

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Carboxypeptidase A1 (CPA1) is secreted as a pancreatic peptidase that comes from the precursor form of inactive procarboxypeptidase. CPA1 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. It has a free C-terminal carboxyl group, with the preference of residues with aromatic or branched aliphatic side chains. CPA1 cleaves the C-terminal amide or ester bond of peptides and involves in zymogen inhibition. Three different forms of human pancreatic procarboxypeptidase A have been isolated. In contrast to procarboxypeptidase B which was always secreted by the pancreas as a monomer, procarboxypeptidase A occurs as a monomer and/or associated to one or two functionally different proteins, such as zymogen E.

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The active form of CPE cleaves C-terminal amino acid residues of the peptide, and is thus involved in the biosynthesis of peptide hormones and neurotransmitters including insulin, enkephalin, etc. It is thought that membrane-associated CPE acts as a sorting receptor for targeting regulated secretory proteins which are mostly prohormones and neuropeptides in the trans-Golgi network of the pituitary and in secretory granules into the secretory pathway. Defects in this protein are implicated in type II diabetes due to impaired glucose clearance and insulin resistance.

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Tryptophan synthase is a multienzyme alpha2 beta 2 complex composed of two protein subunit. Tryptophan synthase catalyses the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyses cleavage of 3-indole-d-glycerol 3′-phosphate (IGP) to give indole and D-glyceraldehyde 3′-phosphate (G3P). Indole is then transferred through a 25-Å hydrophobic tunnel to the beta -subunit. The beta 2 subunit contains pyridoxal 5'-phosphate and catalyses several pyridoxal 5'-phosphate-dependent reactions, including/3-elimination reactions 6 and a thiol-dependent transamination reaction. This enzyme is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from Animalia. As humans do not have tryptophan synthase, this enzyme has been explored as a potential drug target.

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Beta-D-glucuronidase from E. coli is a  highly specific enzyme in hydrolysing glucuronides. Beta-D-glucuronidase (GLUase) activity can be measured as the rate of production of fluorescent methylumbelliferone (MU), resulting from the hydrolysis of the substrate 4-methylumbelliferyl- beta -d-glucuronide (MUGLU), which is an effective and rapid method for detection and verification of E. coli in food, water, and environmental samples. High purity recombinant beta-Glucuronidase is used in research, biochemical enzyme assays and in vitro diagnostic analysis, detecting a wide range of drugs such as opioids, benzodiasepines, steroids, cannabinoids, and others.

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Aldo-Keto Reductase 1C4/AKR1C4 is a member of the aldo/keto reductase family that consists of more than 40 known enzymes and proteins. AKR1C4 has highly expressed in Liver. It can catalyses the bioreduction of chlordecone, a toxic organochlorine pesticide, to chlordecone alcohol in liver. AKR1C4 catalyses the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5- alpha-Androstan-3- alpha,17- beta -diol (3- alpha-diol). In addition, AKR1C4 also has some 20- alpha-Hydroxysteroid Dehydrogenase activity.

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Thymidine kinase 1(TK1) belongs to the thymidine kinase family. It is located in the cytoplasm, and phosphorylated on Ser-13 in mitosis during post-translational modification. Two forms of this protein have been identified in animal cells, one in cytosol TK1 and one in mitochondria TK2. Thymidine kinases have a key function in the synthesis of DNA and thereby in cell division, as they are part of the unique reaction chain to introduce deoxythymidine into the DNA. Activity of the cytosolic enzyme is high in proliferating cells and peaks during the S-phase of the cell cycle, while it is very low in resting cells. TK1 acts as a homotetramer, and can transform thymidime to thymidine 5'-phosphate with the help of ATP.