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Sialidase 1 (NEU1) is a lysosomal enzyme which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, the NEU1 enzyme is part of a heterotrimeric complex in cooperation with beta-galactosidase and cathepsin A. NEU1 gene mutations may lead to sialidosis, a lysosomal storage disease that can be the type 1 (cherry red -myoclonus syndrome or normosomatic type), which is late-onset, or the type 2 (the dysmorphic type), which takes place at an earlier age with increased acuteness.

Deoxyribose-phosphate aldolase (DERA) is a member of the deoC/fbaB aldolase protein family involved in the carbohydrate degradation pathway. DERA catalyzes the conversion of 2-deoxy-D-ribose 5-phosphate to D-glyceraldehyde 3-phosphate and an acetyldehyde.

Enteropeptidase or enterokinase is an enzymeinvolved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberk?hn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen(a zymogen) to trypsin, indirectly activating a number of pancreaticdigestive enzymes.
Enteropeptidase is a serine proteaseenzyme(EC3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.

TEV protease is the common name for the 27 kDa catalytic domain of the Nuclear Inclusion a (NIa) protein encoded by the tobacco etch virus (TEV). Because its sequence specificity is far more stringent than that of factor Xa, thrombin, or enterokinase, TEV protease is a very useful reagent for cleaving fusion proteins. TEV protease recognizes a linear epitope of the general form E-Xaa-Xaa-Y -Xaa-Q-(G/S), with cleavage occurring between Q and G or Q and S. The most commonly used sequence is ENLYFQG.

Isopentenyl-diphosphate Delta-isomerase 2 (IDI2) is a member of the IPP isomerase type 1 family. IDI2 catalyzes the 1,3-allylic reorganization of the homoallylic substrate isopentenyl (IPP) to its extremely electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).

Phospholipase A1 Member A (PLA1A) is a phospholipase which hydrolyzes fatty acids at the sn-1 position of phosphatidylserine and 1-acyl-2-lysophosphatidylserine. The secreted PLA1A protein hydrolyzes phosphatidylserine in liposomes. PLA1A hydrolyzes phosphatidylserine (PS) in the form of liposomes and 1-acyl-2 lysophosphatidylserine (lyso-PS), but not triolein, phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic acid (PA) or phosphatidylinositol (PI). PLA1A isoform 2 hydrolyzes lyso-PS but not PS. The hydrolysis of lyso-PS in peritoneal mast cells activated by receptors for IgE leads to stimulation of histamine production.

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.

Seryl-tRNA synthetase, cytoplasmic (SARS) is a member of the class-II aminoacyl-tRNA synthetase family. Aminoacyl-tRNA synthetases’ role is to catalyze the aminoacylation of tRNAs by their corresponding amino acids, as a result linking amino acids with tRNA-contained nucleotide triplets. The SARS enzyme catalyzes the attachment of serine to tRNA (Ser). SARS enzyme is probably able to aminoacylate tRNA (Sec) with serine, to form the misacylated tRNA L-seryl-tRNA (Sec), which will be then converted into selenocysteinyl-tRNA (Sec).

Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

Beta-galactosidase or GLB1 is a B-galactosidase found in the lysosome. This enzyme hydrolyzes the finale B-galactose from the precursors ganglioside & keratin sulfate. GLB1 has a crucial part in the creation of elastogenesis (extracellular elastic fibers) and connective tissue development. This enzyme is similar to elastin-binding protein which is a key part in non-integrin cell surface receptor. In cells that extort elastin GLB1 is linked to tropoelastin intracellularly and act as recycling molecular chaperone.

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.

MMP-1 can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IL-1?, IGFBP-3, IGFBP-5, casein, gelatin, ?1 antitrypsin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.

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.

N-acylneuraminate-9-phosphatase (NANP) belongs to the haloacid dehalogenase (HAD) family and is responsible for dephosphorylating N-acylneuraminate 9-phosphate to form N-acylneuraminate (N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate). The catalytic activity of NANP is relies on the presence of magnesium and is inhibited by vanadate and calcium, which is typical of the HAD phosphatase family.

Thiosulfate Sulfurtransferase Like Domain Containing 3, also known as TSTD3 contains 1 rhodanese domain which is characterized by an active site cysteine residue that has the ability to bind sulfane sulfur and catalyse sulfur transfer.

Arylsulfatase G (ARSG) is a member of the sulfatase enzyme family. Sulfatases are enzymes which hydrolyze sulfate esters from sulfated steroids, carbohydrates, proteoglycans, and glycolipids. Sulfatases are involved in hormone biosynthesis, modulation of cell signaling, and degradation of macromolecules. The ARSG protein exhibits arylsulfatase activity at acidic pH, as is characteristic of lysosomal sulfatases. The Arylsulfatase G enzyme localizes in the lysosomes. ARSG is inhibited by phosphate, which forms a covalent bond with the active site 3-oxoalanine. Arylsulfatase G is widely expressed, having very low expression in the brain, lung, heart and skeletal muscle.

ENO1 is a homodimeric soluble protein that encodes a smaller monomeric structural lens protein, tau-crystallin. ENO1 is a glycolytic enzyme expressed in mainly all tissues. ENO1 isoenzyme full length protein is found in the cytoplasm. The shorter protein is formed from another translation start that is restricted to the nucleus, and binds to a component in the c-myc promoter. ENO1 is involved in anaerobic metabolism under hypoxic conditions and plays a role as a cell surface plasminogen receptor during tissue invasion. Irregular expression of Enolase-1 is linked with tumor progression in several cases of breast and lung cancer. Enolase-1 is as an auto antigen associated with Hashimoto's encephalopathy and severe asthma. ENO1 is the target protein of serum anti-endothelial antibody in Behcet's disease.

Enoyl-CoA Delta Isomerase 1 (ECI1) is a main mitochondrial enzyme which takes part in beta-oxidation of unsaturated fatty acids. ECI1 is a member of the hydratase/isomerase superfamily. ECI1 catalyzes the transformation of 3-cis and 3-trans-enoyl-CoA esters to the 2-trans-enoylCoA intermediates.

DNA-3-methyladenine glycosylase (MPG) is a member of the DNA glycosylase MPG family. MPG initiates base excision repair in DNA by removing a wide variety of alkylated, deaminated, and lipid peroxidation-induced purine adducts.

Ribose-5-phosphate isomerase (RPIA) is a member of the ribose 5-phosphate isomerase family. RPIA is an enzyme which catalyzes the conversion between ribose-5-phosphate (R5P) and ribulose-5-phosphate (Ru5P). RPI occurs as 2 separate proteins forms, termed RPIA and RPIB. RPIA has a vital role in the metabolism of plants and animals, as it is involved in the Calvin cycle which takes place in plants, and the pentose phosphate pathway which occurs in plants as well as animals.

Beta-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of Beta-galactosides into monosaccharides. Substrates of different Beta-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Beta-galactosidase is produced In E. coli by activation of the lac operon as the lacZ gene.

TPI1 is one of the triosephosphate isomerase family. TPI1 catalyzes the isomerization of glyceraldehydes 3-phosphate (G3P) and dihydroxy-acetone phosphate (DHAP) in glycolysis and gluconeogenesis. Mutations in TPI1 causes triosephosphate isomerase deficiency (TPI deficiency). TPI deficiency is an autosomal recessive disorder which is the most severe clinical disorder of glycolysis and is related to neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection.

Lipase Endothelial (LIPG) has extensive phospholipase activity and may be involved in lipoprotein metabolism and vascular biology. The LIPG protein is considered a member of the TG lipase family through its sequence and characteristic lid region which provides substrate specificity for enzymes of the TG lipase family. In addition, the LIPG has triglyceride lipase activities. LIPG hydrolyzes HDLs more efficiently than other lipoproteins.