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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).

SURA is a PPIase enzyme and chaperone of Escherichia coli and other Gram-negative bacteria. SURA is a key player in the biogenesis of beta-barrel outer membrane proteins and is involved in cell envelope homeostasis and cell envelope functions. SURA is necessary for the survival of E.coli in stationary phase and needed for pilus biogenesis.

RNASE2, also known as EDN, is best-known as one of the 4 major proteins found in the large specific granules of human eosinophilic leukocytes. This protein is also expressed constitutively in human liver tissue and its expression can be induced in macrophages by proinflammatory stimuli. RNASE2 is a non-secretory ribonuclease which belongs to the pancreatic ribonuclease family, a subset of the ribonuclease A superfamily. Diseases associated with EDN include Dermatitis, Atopic, 8 and Pulmonary Eosinophilia.

Luciferase is a general term for the class of oxidative enzymes used in bioluminescence and is distinct from a photoprotein. Luciferase catalyzes a bioluminescent reaction which involves the substrate luciferin as well as Mg2+ and ATP, produces green light with a wavelength of 562 nm. Luciferase from firefly is broadly used as a reporter for studying gene regulation and function, and for pharmaceutical screening.

Chitinase is a digestive enzyme which breaks down glycosidic bonds in chitin. Due to chitin being a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods), chitinases are usually found in organisms that either need to remake their own chitin or to dissolve and digest the chitin of fungi or animals. Chitinivorous organisms include many bacteria genuses such as Aeromonas, Bacillus, Vibrio, among others, which may be pathogenic or detritivorous. Chitinase expression is mediated by the NPR1 gene and the salicylic acid pathway, both of which are involved in resisting fungal and insect attack. Human chitinases appear in gastric juices. They are likely to be digestive chitinases, for catabolic activity. Chitinase activity is identified systemically in humans, in the blood, and possibly cartilage. Chitinase has been related to allergies, asthma in particular has been linked to enhanced chitinase expression levels, also dust mites and mold spores which are both chitin covered.

Angiotensin converting enzyme 2 or ACE-2 is an enzyme that is located in the cell membranes in different organs such as kidney, intestines, lungs, heart & arteries. ACE2 acts as an entry receptor of SARS coronaviruses & SARS-CoV-2.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen bound to the external envelope of the virion that has a role in a crucial part in viral infection by identifying host cell receptors and starting fusion of the viral and cellular membranes. Couple of main domains in coronavirus S1 have been identified, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains acts as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 has a signal peptide, a transmembrane domain & a single metalloproteinase active site holds an HEXXH zinc-binding domain. ACE-2 takes part as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.

BAT1 belongs to the DEAD box family of RNA-dependent ATPases that mediate ATP hydrolysis during pre-mRNA splicing. UAP56 protein is a vital splicing factor which is needed for connecting U2 small nuclear ribonucleoprotein with pre-mRNA, as well as takes a key part in mRNA export from the nucleus to the cytoplasm. Mutations in this protein may be connected to rheumatoid arthritis.

melA is a member of the glycosyl hydrolase 4 family. melA catalyze the hydrolysis of saccharides containing o-1,6,-galactoside bonds. melA catalyze the same reaction in E.coli, human and yeast but is found in different cellular sections: The E.coli melA is a cytoplasmic protein and the human and yeast melA are secretory proteins. Thus, even though the active enzyme from all three species has almost an equal molecular weight, structural resemblances, as well as dissimilarities, are probable.

MMP-1 (interstitial collagenase) 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.

Phosphoglycerate mutase 2 (PGAM2) is a member of the phosphoglycerate mutase family. PGAM is a dimeric enzyme which contains in separate tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM (Phosphoglycerate mutase) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM2 gene mutations cause muscle phosphoglycerate mutase efficiency, otherwise known as glycogen storage disease X.

PHOSPHO1 is involved in mineralization process & plays a role in bone and cartilage matrix mineralization.
PHOSPHO1 is expressed at sites of mineralization in bone and cartilage. Highly expressed in osteoblast cell line SaOS-2 which produces a mineralized matrix.
Orphan-1 is collagen type -2 is specific for cartilaginous tissues. Orphan1 is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
Phosphoethanolamine (2-O3POCH2CH2NH3) is a key intermediate in the formation of cephalins, it is formed in liver and brain by phosphorylation of ethanolamine.
PHOSPHO2 and PHOSPHO1 suggest subtle differences in the charge distributions around the putative substrate entry site and in the location of potential H-bond donors.
PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities PHOSPHO1 is a phosphatase enzyme for which expression is upregulated in mineralizing cells. PHOSPHO1 has been implicated in the generation of Pi for matrix mineralization, a process central to skeletal development. PHOSPHO1 is a member of the haloacid dehalogenase (HAD) superfamily of Mg2+-dependent hydrolases. PHOSPHO1 exhibits high specific activities toward phosphoethanolamine (PEA) and phosphocholine (PCho).

Phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP) belongs to the HAD-like hydrolase superfamily. LHPP is an exceptional enzyme which hydrolyzes not only oxygen-phosphorus bonds in inorganic pyrophosphate but also nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate in vitro. LHPP is expressed in the liver, kidney and moderately in the brain.

AKR1B1 is part of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. AKR1B1 catalyzes the reduction several aldehydes, including the aldehyde form of glucose, and thus involved in the development of diabetic complications by catalyzing the reduction of glucose to sorbitol. AKR1B1 catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Transgenic mice over expressing human aldose reductase show that AKR1B1 is a key player in ischemic injury and impairment of functional and metabolic recovery after ischemia. Aldose Reductase is an obligatory mediator of TNF-alpha signaling leading to an increase in the expression of adhesion molecules and increased binding of monocytes to the endothelium. AKR1B1 is a critical regulator of TNF-alpha-induced apoptotic signaling in endothelial cells.

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.

PCBD1 enzyme takes part in phenylalanine hydroxylation. PCBD1 deficiency results in hyperphenylalaninemia. PCBD1 enzyme controls the homodimerization of HNF1. PCBD1 takes part in tetrahydrobiopterin biosynthesis. PCBD1 prevents the formation of 7-pterins and accelerate the formation of quinonoid-BH2. PCBD1 is a coactivator for HNF1A-dependent transcription.

Thymine-DNA glycosylase (TDG) is a member of the TDG/mug DNA glycosylase family.
TDG is a nuclear protein that fixes G/T mismatches to G/C pairs by hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired thymin. In addition, TDG removes uracil and 5-bromouracil from mispairings with guanine. The TDG enzyme has an essential role in cellular defense against genetic mutation triggered by the spontaneous deamination of 5-methylcytosine and cytosine.

Inositol monophosphatase1 (IMPA1) is responsible for the provision of inositol essential for synthesis of phosphatidylinositol and polyphosphoinositides. IMPA1 has a central role in the phosphatidylinositol signaling pathway by catalyzing the hydrolysis of inositol monophosphates. IMPA1 has been recognized as the pharmacological target for lithium action in the brain. The IMPA1 enzyme has a magnesium-dependent phosphatase activity and is inhibited by therapeutic concentrations of lithium. Inhibition of inositol monophosphate hydroylosis and ensuing depletion of inositol for phosphatidylinositol synthesis may perhaps explain the anti-manic and anti-depressive effects of lithium administered to treat bipolar disorder.

Core 1 Beta3-Gal-T1 also known as,C1GALT1 creates the common core 1 O-glycan structure, Gal-beta-1-3GalNAc-R, by the transfer of Gal from UDP-Gal to GalNAc-alpha-1-R. Core 1 is a precursor for lots of extended mucin-type O-glycans on cell surface and secreted glycoproteins. Studies in mice have shown that this gene takes a main role in angiogenesis, thrombopoiesis and kidney homeostasis.

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.

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.

Matrix metalloproteinase-2 (MMP-2) is involved in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. MMP-2 contains a number of distinct domains: a prodomain that is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin like domain believed to have a role in substrate targeting; and a carboxyl terminal (hemopexin like) domain containing 2 N-linked glycosylation. The MMP-2 can degrade an extensive array of substrates including type IV, V, VII and X collagens as well as gelatin type I. In addition, MMP-2 interacts with THBS2, TIMP2, Thrombospondin 1, CCL7 and TIMP4. MMP-2 autocatalytic cleavage in the C-terminal generates the anti-angiogenic peptide, PEX. This process seems to be made possible by binding integrinv/beta3. Defects in the MMP-2 are the cause of Torg-Winchester syndrome (TWS), aka multicentric osteolysis nodulosis and arthropathy (MONA).

Dimethylglycine oxidase (DMGO) is a covalent flavoenzyme from Arthrobacter globiformis that catalyzes the oxidative demethylation of dimethylglycine to yield sarcosine, formaldehyde, and hydrogen peroxide. The N-terminal region binds FAD covalently so it is yellowish.

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.