Prolysyl oxidase activation

Stable Identifier
R-HSA-2022141
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

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

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

J Biol Chem 1996
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

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

J Biol Chem 2001
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
metalloendopeptidase activity of Procollagen C-proteinases [extracellular region]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed