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Myeloperoxidase is an important enzyme used by granulocytes during phagocytic lysis of foreign particles engulfed. In normal tissues and in a variety of myeloproliferative disorders myeloid cells of both neutrophilic and eosinophilic types, at all stages of maturation, exhibit strong cytoplasmic reactivity for MPO. Erythroid precursors, megakaryocytes, lymphoid cells, mast cells, and plasma cells are nonreactive. MPO is not observed in the neoplastic cells of a wide variety of epithelial tumors and sarcomas. MPO is useful in differentiating between myeloid and lymphoid leukemias.

MMP9 is part of the matrix metalloproteinase family. MMP enzymes take part in the dismantle of extracellular matrix in different physiological pathways, for instance wound healing, bone development, reproduction etc. the enzyme is also involved in pathological pathways: metastasis, arthritis and intracerebral hemorrhage.

NT5M is a member of the 5'(3')-deoxyribonucleotidase family. NT5M localizes to the mitochondrial matrix. The NT5M enzyme dephosphorylates the 5'- and 2'(3')-phosphates of uracil and thymine deoxyribonucleotides. The NT5M gene is located on chromosome 17 p11.2 in the critical region deleted in the Smith-Magenis syndrome (SMS), a genetic disease of unidentified etiology.

OGG1 is a DNA glycosylase enzyme which takes part in base excision repair. OGG1 protein is the main enzyme accountable for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which arises as a result of exposure to reactive oxygen species (ROS). OGG1 shows beta lyase activity that nicks DNA 3'' to the lesion.

ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, also know as ST3GAL5 belongs to the glycosyltransferase family 29 and localized to the Golgi apparatus. ST3GAL5 is known to play a part in the induction of cell differentiation, modulation of cell proliferation, maintenance of fibroblast morphology, signal transduction, and integrin-mediated cell adhesion. ST3GAL5 is a type II membrane protein which catalyzes the formation of GM3 with lactosylceramide as the substrate. Mutation in this ST3GAL5 has been connected with Amish infantile epilepsy syndrome. Transcript variants encoding various isoforms have been found for this gene.

Lysyl-tRNA synthetase (KARS) is a member of the class-II aminoacyl-tRNA synthetase family. KARS exists as both mitochondrial and cytoplasmic isoforms produced by alternative splicing, and believed to have a role in autoimmune diseases, such as polymyositis or dermatomyositis. The KARS protein functions to catalyze the aminoacylation of tRNAs by their corresponding amino acids, so linking amino acids with tRNA-contained nucleotide triplets.

GlpK also known as glycerol kinase, is a member of the FGGY kinase family. GlpK catalyzes the transfer of a phosphate group from ATP to glycerol, thereby forming glycerol phosphate. Furthermore, this intermediate can then be converted to dihydroxyacetone phosphate (DHAP), which is utilized in either glycolysis or gluconeogenesis. The activity of GlpK is affected by numerous metabolites. The non-competitive allosteric inhibition by fructose 1,6-bisphosphate (FBP) triggers modifications in the quaternary structure of Glpk.

Protease Serine 7, also known as PRSS7, is in charge of initiating the activation of pancreatic proteolytic proenzymes such as trypsin, chymotrypsin and carboxypeptidase A. PRSS7 catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, as well as proelastases.

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.

MMP9 is part of the matrix metalloproteinase family. MMP enzymes take part in the dismantle of extracellular matrix in different physiological pathways, for instance wound healing, bone development, reproduction etc. the enzyme is also involved in pathological pathways: metastasis, arthritis and intracerebral hemorrhage.

CBR4 is a member of the short-chain dehydrogenase/reductase family. CBR4 has a role in biosynthesis of fatty acids in the mitochondria and a broad substrate specificity and reduces 9,10-phenanthrenequinone, 1,4-benzoquinone and a range of other o-quinones and p-quinones (in vitro). CBR4 formation of a heteroteramer with HSD17B8 has NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity for o- and p-quinones.

Alpha-galactosidase A (GLA) is a homodimeric glycoprotein which hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. GLA catalyzes the hydrolysis of melibiose into galactose and glucose. Various mutations in the GLA gene affect the synthesis, processing, and stability of this enzyme, which causes Fabry disease (a rare lysosomal storage disorder which results from a failure to catabolize alpha-D-galactosyl glycolipid moieties).

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).

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.

GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.

Deoxyribodipyrimidine photo-lyase (phrB) is a member of the DNA photolyase class-1 family. phrB takes part in repair of UV radiation-inducedDNA damage. phrB catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidinedimers (in cis-syn configuration), which are formed between closest bases on the same DNA strand uponexposure to ultraviolet radiation.

Acyl CoA dehydrogenase is the enzymeused to catalyzethe first step of ?-oxidationin Fatty acid metabolism.
Acyl-coenzyme A (CoA) dehydrogenases (ACADs) are a family of mitochondrial enzymes that catalyze the first dehydrogenation step in the bets-oxidation of fatty acyl-CoA derivatives. Several human ACADs exist and all ACADs catalyze the same initial dehydrogenation of the substrate at the beta-carbon atom and require electron transfer flavoprotein as an alectron acceptor. The predicted 415-amino acid ACAD8 protein contains many of the residues conserved in most other ACADs, including an active site glutamic acid residue and residues important for tetramer formation.

Acireductone dioxygenase 1 (ADI1) is a part of the acireductone dioxygenase family of metal-binding enzymes, which are involved in methionine salvage. ADI1 regulates mRNA processing in the nucleus, and carries out different functions depending on its localization. Related pseudogenes have been defined on chromosomes 8 and 20. ADI1 down-regulates cell migration arbitrated by MMP14.

DCXR catalyzes the NADPH-dependent reduction of numerous pentoses, tetroses, trioses, alpha-dicarbonyl molecules and L-xylulose. DCXR takes part in the uronate cycle of glucose metabolism. DCXR participates in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thus preventing osmolytic stress from occurring in the renal tubules.

ECH1 is a member of the hydratase/isomerase superfamily. ECH1 demonstrates high sequence similarity to enoyl-coenzyme A (CoA) hydratases of more than a few species, mostly within a conserved domain characteristic of these proteins. ECH1 contains a C-terminal peroxisomal targeting sequence, localizes to both the peroxisome and the mitochondria. peroxisomal takes part in the auxiliary step of the fatty acid beta-oxidation pathway specifically functioning to catalyze the isomerization of 3-trans, 5-cis-dienoyl-CoA to 2-trans, 4-transdienoyl-CoA.

FBP1 is a gluconeogenesis regulatory protein which catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBP1 deficiency is associated with hypoglycemia and metabolic acidosis. FBP1 regulates mouse endogenous glucose production. FBP1 coupled with phosphofructokinase (PFK) takes part in the metabolism of pancreatic islet cells.

GALM is a main enzyme of carbohydrate metabolism catalysing the translation of beta-D-galactose to alpha-D-galactose. GALM is needed for normal galactose metabolism by preserveing the equilibrium of alpha and beta anomers of galactose. GALM is required for the production of complex oligosaccharides.

Phosphopantothenate-cysteine ligase (PPCS) catalyzes the first step in the biosynthesis of coenzyme A (CoA) from pantothenic acid (vitamin B5), which is a vital universal pathway in prokaryotes and eukaryotes. PPCS, being one of the last enzymes in this pathway, converts phosphopantothenate to phosphopantothenoylcysteine.

DARS uses a 2 step reaction to catalyze the specific attachment of an amino acid to its cognate tRNA: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.