BMP1-3:Zn2+ cleaves pro-APOA1 to APOA1

Stable Identifier
Reaction [transition]
Homo sapiens
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The six aminoterminal residues of pro-apolipoprotein A-1 are removed to generate the mature, lipid-binding form of the protein (APOA1). Studies of tissue culture systems suggest that BMP1 catalyzes this reaction (Chau et al. 2006, 2007). While BMP1 is annotated here as a monomer, its subunit structure is not known, and its 1:1 association with Zn2+ is inferred from its sequence similarity to known metallopeptidases. Tetrameric alpha2-macroglobulin (A2M) at concentrations found in plasma in inflammatory responses inhibits this reaction in vitro, suggesting a possible link between inflammation and perturbation of HDL function (Zhang et al. 2006, Chau et al. 2007).
Literature References
PubMed ID Title Journal Year
17580958 Bone morphogenetic protein-1 (BMP-1) cleaves human proapolipoprotein A1 and regulates its activation for lipid binding

Chau, P, Fielding, PE, Fielding, CJ

Biochemistry 2007
17071617 Inhibition of bone morphogenetic protein 1 by native and altered forms of alpha2-macroglobulin

Zhang, Y, Ge, G, Greenspan, DS

J Biol Chem 2006
16548525 Mechanism of prebeta-HDL formation and activation

Chau, P, Fielding, PE, Nakamura, Y, Fielding, CJ

Biochemistry 2006
Catalyst Activity

metalloendopeptidase activity of BMP1-3:Zn2+ [extracellular region]

This event is regulated
Orthologous Events
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