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UPP1 catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate which are used as carbon and energy sources or in the release of pyrimidine bases for nucleotide synthesis. UPP1 is part of the family of glycosyltransferases, specifically the pentosyltransferases. Pyrimidine nucleoside phosphorylases add ribose or deoxyribose to pyrimidine bases to form nucleosides that can be incorporated into RNA or DNA.

Ribophorin 2 (RPN2) is a dolichyl-diphosphooligosaccharide protein glycosyltransferase subunit 2. The Ribophorin 2 protein is part of an N-oligosaccharyl transferase complex which links high mannose oligosaccharides to asparagine residues found in the Asn-X-Ser/Thr consensus motif of nascent polypeptide chains. RPN2 is analogous in sequence to the yeast oligosaccharyl transferase subunit SWP1.

Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases that break down extracellular matrix proteins. The MMP9 is secreted as a 92kDa zymogen. Cleavage of ProMMP-9 results in the active enzyme, having a molecular weight of approximately 82kDa. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by the several cell types: monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells. MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. MMP9 cleaves type IV and type V collagens into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. MMP9 can also degrade fibronectin but not laminin or Pz-peptide.
MMP9 defects may be a cause of susceptibility to intervertebral disc disease (IDD), also known as lumbar disk herniation (LDH).

Matrix metalloproteinase-14 (MMP14), is a membrane-anchored zinc-binding endopeptidase which is expressed at the leading edge of different invasive carcinomas and also promotes tumor cell invasion through degradation of the extracellular matrix. MMP14 takes a vital part in extracellular matrix, ECM, remodeling by having the capability to degrade type I collagen, activate pro-MMP-2 and process cell adhesion molecules for instance CD44 and integrin alpha V. MMP14 is a key enzyme in many physiological as well as pathological processes for example angiogenesis & tumor invasion.

UBE2N belongs to the E2 ubiquitin-conjugating enzyme family. UBE2N catalyzes the ATP-dependent synthesis of non-canonical polyubiquitin chains, a process which doesn’t set in motion proteasomal degradation. UBE2N mediates the transcription of some target genes and is believed to have a role in cell cycle progression; cellular differentiation and DNA repair mechanisms which ensure cell survival after DNA damage.

GARS is an (alpha)2 dimer which is a member of the class II family of tRNA synthetases. GARS is a glycyl-tRNA synthetase, one of the aminoacyl-tRNA synthetases which charge tRNAs with their cognate amino acids. GARS catalyzes the attachment of glycine to tRNA(Gly). In addition, GARS is able to produce diadenosine tetraphosphate (Ap4A), which is a universal pleiotropic signaling molecule required for cell regulation pathways, by direct condensation of two ATPs. GARS has been demonstrated to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis.

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.

Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases that break down extracellular matrix proteins. The MMP9 is secreted as a 92kDa zymogen. Cleavage of ProMMP-9 results in the active enzyme, having a molecular weight of approximately 82kDa. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by the several cell types: monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells. MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. MMP9 cleaves type IV and type V collagens into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. MMP9 can also degrade fibronectin but not laminin or Pz-peptide.
MMP9 defects may be a cause of susceptibility to intervertebral disc disease (IDD), also known as lumbar disk herniation (LDH).

GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.

Matrix Metallopeptidase 23B (MMP23B) belongs to the matrix metalloproteinase (MMP) family, and it is section of a duplicated region of chromosome 1p36.3. MMP23B is a protease. MMP23B regulates the surface expression of some potassium channels by holding them in the endoplasmic reticulum. Members of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis.

Cyclophilin-E is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. Cyclophilin-E contains a highly conserved cyclophilin domain in addition to a RNA-binding domain. Cyclophilin-E exhibits PPIase activity, protein folding activities and possess RNA-binding activity. Cyclophilin-E contains 2 RNA binding domains at the N-terminal region and a PPIase domain at the C-terminal region.

UBE2E3 or Ubiquitin-conjugating enzyme E2 E3 is part of the E2 ubiquitinconjugating enzyme family. UBE2E3 is needed for the destruction of mitotic cyclins and for cell cycle progression. The ubiquitination process covalently attaches to a short protein of 76 amino acids called ubiquitin, to a lysine residue on the target protein. When a protein has been tagged with one ubiquitin molecule, other rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein which grants passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell.

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

ADH1C is a member of the zinc-containing alcohol dehydrogenase family which metabolizes a large assortment of substrates, such as ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH1 is a monomorphic and a key factor in fetal and infant livers, becoming less active in gestation and only weakly active during adulthood.

Porphobilinogen deaminase (HMBS) belongs to the hydroxymethylbilane synthase superfamily. HMBS is a cytoplasmic enzyme found in the heme synthesis pathway. HMBS is the 3rd enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of 4 porphobilinogen molecules into the linear hydroxymethylbilane. HMBS gene mutations cause errors in pyrrole metabolism which in turn lead to the autosomal dominant disease acute intermittent porphyria.

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.

Magnesium-dependent phosphatase 1 (MDP1) is a memeber of the HAD-like hydrolase superfamily. MDP1 is a magnesium-dependent phosphatase which may act as a tyrosine phosphatase. MDP1 is inhibited by vanadate and zinc, and slightly by calcium.

Isocitrate dehydrogenase [NAD] subunit gamma (IDH3G) mitochondrial is a member of the isocitrate and isopropylmalate dehydrogenases family. Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. The IDH3G is a gamma subunit of one isozyme of isocitrate dehydrogenase which belongs to a distinct subclass, which utilizes NAD(+) as the electron acceptor, and is restricted to the mitochondrial matrix.

LPL is a lipoprotein lipase, which is expressed in the heart, muscle, and adipose tissue. LPL acts as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Type I hyperlipoproteinemia is a result of severe mutations which cause LPL deficiency, whereas less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism. Lipoprotein lipase (LPL) is a fundamental enzyme in plasma triglyceride hydrolysis and is secreted by macrophages in the subendothelial space. LPL also promotes the development of atherosclerosis through facilitation of monocyte adhesion to endothelial cells, stimulation of tumor necrosis factor alpha (TNF) secretion and induction of vascular smooth muscle cell proliferation.

Phosphoglycolate phosphatase (PGP) is discovered in all tissues including red cells, lymphocytes and cultured fibroblasts (at protein level). PGP is most active in skeletal muscle and cardiac muscle. The catalytic activity of PGP is 2-phosphoglycolate + H2O = glycolate + phosphate. Diseases associated with PGP include tardive dyskinesia and polycystic kidney disease.

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.

Methionine sulfoxide reductase B (MsrB) from Escherichia coli is a member of the msrB Met sulfoxide reductase family. The E.coli msrB carries out the reduction of methionine-R-sulfoxide to methionine. msrB possess a metal binding site composed of 2 CXXC motifs. The bound metal (zinc or iron) may stabilize the conformation of the enzymes.

Enolase-phosphatase E1 (ENOPH1) belongs to the MasA family of the HAD (halo-acid dehalogenase)-like hydrolase superfamily. ENOPH1 is a bifunctional enzyme which demonstrates both phosphatase and atypical enolase activities. ENOPH1 has a significant role in the ubiquitous methionine salvage pathway which is a biochemical pathway found in all organisms that regulate methionine levels in the cell.

BPGM is found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. PGM deficiency increases the oxygen affinity of cells. BPGM is a multifunctional enzyme that catalyzes 2,3-DPG synthesis through its synthetase activity, and 2,3-DPG degradation using its phosphatase activity. BPGM has phosphoglycerate phosphomutase activity. Mutations in BPGM cause hemolytic anemia. BPGM catalyzes the reaction of EC 5.4.2.1 (mutase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.