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Details on Person Lysyl oxidase (LOX) is secreted to the extracellular space i...

Class:IdSummation:2022121
_displayNameLysyl oxidase (LOX) is secreted to the extracellular space i...
_timestamp2012-11-19 09:23:06
created[InstanceEdit:2022095] Jupe, S, 2011-11-25
literatureReference[LiteratureReference:2022102] The proteolytic processing site of the precursor of lysyl oxidase
[LiteratureReference:2022110] Metalloproteinase activity secreted by fibrogenic cells in the processing of prolysyl oxidase. Potential role of procollagen C-proteinase
[LiteratureReference:2022126] 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
modified[InstanceEdit:2422439] Jassal, B, 2012-07-19
[InstanceEdit:2588522] Jupe, S, 2012-11-19
textLysyl 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).
(summation)[Reaction:2022141] Prolysyl oxidase activation [Homo sapiens]
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