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Lysyl oxidase (LOX), also known as protein-lysine 6-oxidase, is an enzyme that, in humans, is encoded by the LOX gene. It catalyzes the conversion of lysine residues into its aldehyde derivative allysine. Allysine form cross-links in extracellular matrix proteins. Inhibition of lysyl oxidase can cause osteolathyrism, but, at the same time, its upregulation by tumor cells may promote metastasis of the existing tumor, causing it to become malignant and cancerous.
Adamalysin is an enzyme. This enzyme catalyses the following chemical reaction
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Collagenase 3 is an enzyme that in humans is encoded by the MMP13 gene. It is a member of the matrix metalloproteinase (MMP) family. Like most MMPs, it is secreted as an inactive pro-form. MMP-13 has an predicted molecular weight around 54 kDa. It is activated once the pro-domain is cleaved, leaving an active enzyme composed of the catalytic domain and the hemopexin-like domain PDB: 1PEX. Although the actual mechanism has not been described, the hemopexin domain participates in collagen degradation, the catalytic domain alone being particularly inefficient in collagen degradation. During embryonic development, MMP-13 is expressed in the skeleton as required for restructuring the collagen matrix for bone mineralization. In pathological situations it is highly overexpressed; this occurs in human carcinomas, rheumatoid arthritis and osteoarthritis.
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Atrolysin A is an enzyme that is one of six hemorrhagic toxins found in the venom of western diamondback rattlesnake. This endopeptidase has a length of 419 amino acid residues. The metalloproteinase disintegrin-like domain and the cysteine-rich domain of the enzyme are responsible for the enzyme's hemorrhagic effects on organisms via inhibition of platelet aggregation.
Pseudolysin is an enzyme. This enzyme catalyses the following chemical reaction
Leishmanolysin is an enzyme. This enzyme catalyses the following chemical reaction
Atrolysin C is an enzyme. This enzyme catalyses the following chemical reaction
Ruberlysin is an enzyme. This enzyme catalyses the following chemical reaction
Trimerelysin I is an enzyme. This enzyme catalyses the following chemical reaction
Pitrilysin is an enzyme. This enzyme catalyses the following chemical reaction:
Meprin B is an enzyme. This enzyme catalyses the following chemical reaction
Jararhagin is an enzyme. This enzyme catalyses the following chemical reaction
References
- ↑ Banda MJ, Werb Z (February 1981). "Mouse macrophage elastase. Purification and characterization as a metalloproteinase". The Biochemical Journal. 193 (2): 589–605. PMID 7030312.
- ↑ Kettner C, Shaw E, White R, Janoff A (May 1981). "The specificity of macrophage elastase on the insulin B-chain". The Biochemical Journal. 195 (2): 369–72. PMID 7032505.
- ↑ Shapiro SD, Griffin GL, Gilbert DJ, Jenkins NA, Copeland NG, Welgus HG, Senior RM, Ley TJ (March 1992). "Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase". The Journal of Biological Chemistry. 267 (7): 4664–71. PMID 1537850.
- ↑ Shapiro SD, Kobayashi DK, Ley TJ (November 1993). "Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages". The Journal of Biological Chemistry. 268 (32): 23824–9. PMID 8226919.
