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MGAT2 is an enzyme which takes part in the catalyzation of a crucial step in the reaction of oligomannose which converts to complex N-glycans. MGAT2 has three domains, classic to glycosyltransferase: short N-terminal cytoplasmic domain, a C-terminal catalytic domain and hydrophobic non-cleavable signal-anchor domain. The enzyme MGAT2 is encoded by the MGAT2 gene in humans. There are no introns in the DNA coding the gene, therefore mutations in the MGAT2 will result in carbohydrate-deficient glycoprotein syndrome, type II.

Aspartylglucosaminidase, also known as AGA, takes part in the catabolism of Nlinked oligosaccharides of glycoproteins. AGA is a protein coding gene which cleaves asparagine from N-acetylglucosamines in the lysosomal breakdown of glycoproteins.

Metallophosphoesterase domain containing 2 (MPPED2) is a member of the UPF0046 family. MPPED2 displays low metallophosphoesterase activity, in vitro. In addition, MPPED2 encodes a metallophosphoesterase. MPPED2 may take part in the development of the nervous system, brain development. Among the diseases associated with MPPED2 are wagr syndrome, and aniridia.

The enzyme Arylsulfatase A, also known as cerebroside-sulfatase, is responsible to break down sulfatides. The main molecule that Arylsulfatase A breaks down is cerebroside 3-sulfate into cerebroside and sulfate. The enzyme is encoded by the ARSA gene in humans. Phosphate can form a covalent bond with the Arylsulfatase A’s active site 3-oxoalanine, thus, inhibits the protein.

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.

Progastricsin-C (PGC) is an aspartic proteinase which is synthesized in the gastric mucosa as inactive precursors. PGC is a part of the peptidase family A1 and contains a prosegment which is responsible for stabilizing the inactive form and preventing the entrance of the substrate to the active site. PGC is used as a biomarker for various gastric diseases including Helicobacter pylori related gastritis. PGC is also hydrolyzes various proteins.

Tubulointerstitial Nephritis Antigen Like 1 also known as TINAGL1 is similar in sequence to tubulointerstitial nephritis antigen, a secreted glycoprotein which is identified by antibodies in several types of immune-related tubulointerstitial nephritis. Three transcript variants encoding different isoforms are known for TINAGL1.

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.

Tyrosylprotein Sulfotransferase 1, also known as TPST1 is the enzyme which catalyzes the sulfation reaction of protein tyrosines, a post-translational modification of proteins. TPST1 belongs to the protein sulfotransferase family. In addition, TPST1 utilizes 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) as the sulfonate donor and also binds proteins with target tyrosine residues to eventually form the tyrosine O-sulfate ester group in addition to the desulfonated 3’-phosphoadenosine-5’-phosphate.

Tyrosyl-tRNA synthetase (YARS2) is a mitochondrial protein which catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and afterward transferred to the acceptor end of tRNA(Tyr). YARS2 gene mutations are linked with myopathy with lactic acidosis and sideroblastic anemia type 2 (MLASA2).

YOD1 is a Hydrolase which removes conjugated ubiquitin from proteins and takes part in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. YOD1 is a highly conserved deubiquitinating enzyme belonging to the ovarian tumor (otubain) family, whose function has yet to be determined in mammalian cells. YOD1 is a component of a multiprotein complex with p97 as its nucleus, proposing a functional link to a pathway responsible for the dislocation of misfolded proteins from the endoplasmic reticulum. YOD1 variant xpression deprived of its deubiquitinating activity compels a halt on the dislocation reaction, as concluded by the stabilization of various dislocation substrates.

Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.

IMPDH1 is a rate limiting enzyme in the de novo synthesis of guanine nucleotides and consequently participates in the regulation of cell growth. IMPDH1 takes part in the development of malignancy and the growth progression of some tumors. IMPDH1 performs as a homotetramer to regulate cell growth. IMPDH1 catalyzes the synthesis of xanthine monophosphate (XMP) from inosine-5''-monophosphate (IMP). Defects in this gene are a cause of retinitis pigmentosa type 10 (RP10).

STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.

Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.

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.

Cysteine-Rich Secretory Protein 2 (CRISP2) regulates some ion channels activity and thereby regulates calcium fluxes during sperm capacitation. Amongst its related pathways are p53 signaling. Diseases related with CRISP2 include epididymitis and orchitis.

ALDOB is a tetrameric glycolytic enzyme which catalyzes the reversible cleavage of fructose 1-phosphate into dihydroxyacetone phosphate and glyceraldehyde. Fructose-bisphosphate aldolase B (ALDOB) is one of 3 known aldolase isoenzymes, and is located in the kidney and the small adult intestine where it is linked with aldolases A or C. ALDOB is regulated by Insulin and glucagon and is implicated in hereditary fructose intolerance disease.

Serine/threonine-protein kinase 16 (STK16) is a membrane-associated protein kinase which phosphorylates on serine and threonine residues. STK16 is involved in secretory vesicle trafficking or intracellular signaling. Furthermore, the STK16 protein may have a role in regulating stromal-epithelial interactions which occur during ductal morphogenesis in the mammary gland. STK16 can autophosphorylate on Tyr residue; it is however unclear whether STK16 has tyrosine-protein kinase toward other proteins. STK16 may also be involved in TGF-beta signaling.

CDK16 is a member of the CDK family of serine/threonine protein kinases which are known to regulate the cell cycle. These proteins have a core kinase domain flanked by unique amino- and carboxy- terminal domains. CDK16, which is expressed mainly in mammalian brain, cooperates with an assortment of proteins, and is a part of a multiple signal transduction cascade.

Glucose-6-phosphate isomerase (GPI) is a part of the GPI family whose members encode multifunctional phosphoglucose isomerase proteins involved in energy pathways. GPI is a dimeric enzyme which catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. Mammalian GPI also functions as a tumor-secreted cytokine and an angiogenic factor (AMF) which stimulates endothelial cell motility. In addition, GPI is a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. GPI performs in different capacities inside and outside the cell. In the cytoplasm, GPI is involved in glycolysis and gluconeogenesis, while outside the cell it acts as a neurotrophic factor for spinal and sensory neurons.
Defects in the GPI gene cause the nonspherocytic hemolytic anemia and a severe enzyme deficiency can be linked to hydrops fetalis, immediate neonatal death and neurological impairment.

LYPLA1 is lysophospholipase which performs on biological membranes to regulate the multifunctional lysophospholipids. LYPLA1 protein hydrolyzes fatty acids from S-acylated cysteine residues in proteins like trimeric G alpha proteins or HRAS and in addition has depalmitoylating activity.

PTX3 is part of the pentraxin family sharing the C-terminal domain with short pentraxins and containing a unique N-terminal domain. PTX3 is produced and released at inflammatory sites by various cell types including monocytes/macrophages, endothelial cells, vascular smooth muscle cells, fibroblasts, and adipocytes. PTX3 is involved in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. PTX3 is used as a marker for disease activity of psoriasis. High serum PTX3 levels are associated with the disease severity of systemic sclerosis. Elevated serum PTX3 is associated with pulmonary fungal infections.

Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor (PCSK1N) takes part in the control of the neuroendocrine secretory pathway. PCSK1N inhibits prohormone convertase 1, which regulates the proteolytic cleavage of neuroendocrine peptide precursors. PCSK1Nslows down convertase-mediated processing of proopiomelanocortin and proenkephalin and also monitors the intracellular timing of PCSK1.