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XYLT2 or Xylosyltransferase 2 is an enzyme which is expressed in ubiquitous and is part of the glycosyltransfe-rases family. XYLT2 promotes proteoglycans formation by attaching GAG chains to the substrate protein via transfer of xylose molecule from the donor (nucleoside diphosphate) to the protein’s serine residues. XYLT2 is present in the ER and the cis part of the Golgi, furthermore the protein is released to the extracellular matrix.

Glutaminyl-Peptide Cyclotransferase, also known as QPCT is a member of the glutaminyl-peptide cyclotransferase family. QPCT is responsible for the biosynthesis of pyroglutamyl peptides. Furthermore, QPCT is partial against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length following the second residue. QPCT catalyzes N-terminal pyroglutamate formation, also in vitro, it catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid.

Queuine TRNA-Ribosyltransferase Domain Containing 1, also known as QTRTD1 act together with QTRT1 to form an active queuine tRNA-ribosyltransferase. QTRTD1 exchanges queuine for the guanine at the wobble position of tRNAs along with GUN anticodons (tRNA-Asp,-Asn,-His and -Tyr), in that way forming the hypermodified nucleoside queuosine.

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.

PCMT1 enzyme catalyses the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. PCMT1 is involved in the repair and/or degradation of damaged proteins.

tRNA aspartic acid methyltransferase 1 (TRDMT1) is a member of the C5-methyltransferase family. TRDMT1 specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp). TRDMT1 is a protein responsible for the methylation of aspartic acid transfer RNA, particularly at the cytosine-38 residue in the anticodon loop. In addition, the TRDMT1 enzyme has residual DNA-(cytosine-C5) methyltransferase activity. TRDMT1 is expressed ubiquitously; however it has a higher expression in the testis, ovary and thymus and at much lower levels in the spleen, prostate, colon, small intestine, and peripheral blood leukocytes. Though similar in sequence and structure to DNA cytosine methyltransferases, the TRDMT1 gene is distinctive and extremely conserved in its function between taxa.

COMT catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to catechol substrates such as the neurotransmitters. This O-methylation results in one of the main degradative pathways of the catecholamine transmitters. COMT COMT is located in the postsynaptic neuron and is involved in the metabolism of catechol estrogen drugs used in the treatment of hypertension, asthma, Parkinson disease and the inactivation of catecholamine neurotransmitters though enzymatic degradation. COMT appears in tissues in 2 forms, a soluble form and a membrane-bound form which differ in their N-termini. COMT inhibitors increase its availability and are used in the treatment of patients with Parkinson's disease.

Galactose-1-Phosphate Uridylyltransferase (GALT) catalyzes the 2nd step of the “Leloir pathway” of galactose metabolism, specifically the conversion of UDP-glucose + galactose-1-phosphate to glucose-1-phosphate + UDP-galactose. The deficiency of the GALT enzyme results in typical galactosemia in humans and may be fatal in the newborn stage if lactose is not eliminated from the diet. Galactosemia pathophysiology has not been clearly defined.

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).

NNMT is part of the family of transferases, especially those transferring one-carbon group methyltransferases. NNMT is mostly expressed in the liver, and a lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. NNMT catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is significant for biotransformation of many drugs and xenobiotic compounds. NNMT is accountable for the enzymatic activity which uses S-adenosyl methionine as the methyl donor. NNMT expression is related with tumor stage and DFS time in hepatocellular carcinoma cases. NNMT is a good candidate as a tumor marker of various kinds of cancers. NNMT serum levels have significance in the premature detection and in the management of patients with colorectal cancer.

HNMT is located in the cytosol and uses S-adenosyl-L-methionine as the methyl donor. In the mammal’s brain,N(tau)-methylation controls the neurotransmitter activity of histamine since diamine oxidase is not located in the central nervous system. A well known genetic polymorphism influences the activity levels of HNMT gene product in red blood cells. HNMT inactivates histamine by n-methylation. HNMT is involved in degrading histamine and in regulating the airway response to histamine. Histamine is involved in regulation and modulation of immune response through the stimulation of four distinct subtypes of receptors, H1, H2, H3, and H4, that present on the target cells. Histamine is inactivated by the histamine-metabolizing enzyme HNMT in bronchus, kidney, and the central nervous system.

Histamine N-Methyltransferase or HNMT, is located in the cell cytosol. Sadenosyl-L-methionine acts as a methyl donor for HNMT which inactivates histamine. By inactivation of histamine, it affects the immune system’s response. HNMT acts on histamine in body tissues such as kidney, central nervous system and bronchus. The protein has a crucial part in the airway response to histamine & histamine degradation process and regulation.

ACAA1 is part of the thiolase family of enzymes and is takes part in lipid metabolism. ACAA1 enzyme is localized to the peroxisome and catalyzes the conversion of acyl-CoA and acetyl-CoA to 3-oxoacyl-CoA in the fatty acid oxidation pathway. ACAA1 shows high enzymatic activity in liver, kidney, intestine and white adipose tissue in rats. ACAA1 deficiency causes pseudo-Zellweger syndrome.

SULT2B1 catalyzes the sulfate conjugation of numerous hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation enhances the water solubility of molecules, and therefore their renal excretion, however it can also result in bioactivation to form active metabolites. SULT2B1b is localized in the cytosol and nuclei of human cells. SULT2B1b is selective for the sulfation of 3beta-hydroxysteroids such as dehydroepiandrosterone and pregnenolone, and participates in cholesterol sulfation in human skin.

Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5 or ST6GALNAC5, is part of the glycosyltransferase 29 group of proteins. ST6GALNAC5 is a sialyltransferase that takes part in the synthesis of ganglioside GD1a. This protein is part of the protein glycosylation transduction, meaning, modification of proteins. ST6GALNAC5 is expressed strictly in the brain tissue, and is a crucial component in breast cancer cells metastasis to the brain tissue. It is thought to enable cancer cells to go through the blood-brain barrier.

Carbohydrate Sulfotransferase 3 (CHST3) belong to sulfotransferase 1 family which iincludes 14 enzymes that all members are Golgi-localized type II membrane proteins. These enzymes utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. CHST3 can also sulfate Gal residues of keratan sulfate and Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides. CHST3 is expressed in heart, placenta, skeletal muscle and pancreas. CHST3 takes part in maintenance of naive T-lymphocytes in the spleen.

Probable tRNA (His) guanylyltransferase (THG1L) is a member of the tRNA (His) gyanylytransferase family. THG1L which is localized to the cytoplasm also found adjacent to the nuclear membrane and expressed in various tissues, including liver and lung. THG1L is expressed in a cell cycle-dependent manner and may be involved in cell cycle progression and cell proliferation. THG1L adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is vital for accurate recognition of the tRNA and for the fidelity of protein synthesis. Upon DNA damage, THG1L is phosphorylated, presumably by ATM or ATR.

ST6GAL1 also known as ST6 Beta-Galactosamide Alpha-2,6-Sialyltranferase 1, is part of the glycosyltransferase family 29. ST6GAL1 is a type II membrane protein which catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. Furthermore, ST6GAL1 is normally found in the Golgi however it can be proteolytically processed to a soluble form, ST6GAL1 is also involved in the generation of the cell-surface carbohydrate determinants as well differentiation antigens HB-6, CD75, and CD76.

LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.

PRMT1 Methylates (mono & asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain (may methylate HNRNPA1 and histones). Methylates SUPT5H.
The PRMT1 protein functions as a histone methyltransferase specific for H4.
PRMT1 is an essential factor in oncogenesis and is a potential novel therapeutic target in cancer.
PRMT1-mediated methylation serves as a positive modulator of IR/IRS-1/PI3K pathway and glucose uptake in skeletal muscle cells.
CAF1 is a new regulator of PRMT1-dependent arginine methylation.
PRMT1 arginine-methylates MRE11 therefore it regulates the activity of MRE11-RAD50-NBS1 complex during the intra-S-phase DNA damage checkpoint response.
PRMT1 plays a post-translationally part in regulating the transcriptional activity.
PRMT1is found predominantly in the cytoplasma though a fraction of PRMT1 is located in the nucleus.

NNMT is part of the family of transferases, especially those transferring one-carbon group methyltransferases. NNMT is mostly expressed in the liver, and a lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. NNMT catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is significant for biotransformation of many drugs and xenobiotic compounds. NNMT is accountable for the enzymatic activity which uses S-adenosyl methionine as the methyl donor. NNMT expression is related with tumor stage and DFS time in hepatocellular carcinoma cases. NNMT is a good candidate as a tumor marker of various kinds of cancers. NNMT serum levels have significance in the premature detection and in the management of patients with colorectal cancer.

SULT1B1 enzyme in humans is encoded by the SULT1B1 gene. SULT1B1 holds a binding site for 3-prime-phosphoadenosine 5-prime-phosphosulfate, a sulfate donor, in addition to a cysteine residue conserved in the ST1 gene family of sulfotransferases. Sulfotransferases like SULT1B1 catalyze the biotransformation of a great amount of endogenous amalgams such as bile acids, neurotransmitters, steroids, and thyroid hormones, in addition to drugs and xenobiotics.

Sulfotransferase 1C4 (SULT1C4) is a member of the SULT subfamily. SULT1C4 is responsible for transferring a sulfo moiety from PAPS to phenol-containing compounds. Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. Sulfotransferase enzymes are different in their tissue distributions and substrate specificities. SULT1C4 catalyzes the sulfonation of p-nitrophenol and N-hydroxy-2-acetylaminofluorene.

SULT2A1 is a member fo the sulfotransferase family. SULT2A1 is primarily expressed in liver and adrenal tissues, and to a lesser extent in kidney. SULT2A1 catalyzes the 3'-phosphoadenosine 5'-phosphosulfate-dependent sulfation of an extensive selection of steroids in human liver and adrenal tissues, and in addition is responsible for a larg number of the sulfation of bile acids in human liver.