Prolysyl oxidase activation

Stable Identifier
Reaction [transition]
Homo sapiens
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Lysyl oxidase (LOX) is secreted to the extracellular space in an inactive, proenzyme form (proLOX). This is proteolytically cleaved between Gly168 and Asp169 generating the mature 32-kDa enzyme. The activating proteinase is Bone morphogenetic protein 1 (BMP1), also called Procollagen C-proteinase (Cronshaw et al. 1995, Panchenko et al. 1996). Other extracellular proteases, including the BMP1 variant mammalian tolloid, tolloid-like (TLL) 1 and TLL2 proteases cleave proLOX at the correct physiological site but with lower efficiency (Uzel et al. 2001).

Literature References
PubMed ID Title Journal Year
11313359 Multiple bone morphogenetic protein 1-related mammalian metalloproteinases process pro-lysyl oxidase at the correct physiological site and control lysyl oxidase activation in mouse embryo fibroblast cultures

Palamakumbura, AH, Scott, IC, Uzel, MI, Babakhanlou-Chase, H, Trackman, PC, Greenspan, DS, Hong, HH, Pappano, WN

J Biol Chem 2001
8636146 Metalloproteinase activity secreted by fibrogenic cells in the processing of prolysyl oxidase. Potential role of procollagen C-proteinase

Trubetskoy, OV, Stetler-Stevenson, WG, Kagan, HM, Gacheru, SN, Panchenko, MV

J Biol Chem 1996
Catalyst Activity

metalloendopeptidase activity of Procollagen C-proteinases [extracellular region]

Orthologous Events
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