Summary
Lysyl oxidase is unusual amongst the copper-containing amine oxidases. It is much smaller (29kDa) and has a high cysteine content, with ten conserved cysteines. Quantitative NTSB assays show that lysyl oxidase contains five disulfide links and no free cysteines. Thus lysyl oxidase has six covalent cross-links (including one on the cofactor) that provide constraints for molecular modeling studies directed at elucidating the secondary structure of lysyl oxidase and clarifying the geometry of the active site. Computer modeling of a 34-residue, histidine-rich section of lysyl oxidase implicated as a copper-binding region indicates that this region alone does not account for the known properties of the copper-binding site, so we are now extending modeling to the 140-amino acid C-terminal region.
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Greenaway, F.T., Qiu, C., Ryvkin, F. (2000). Structural Aspects of Lysyl Oxidase. In: Iriarte, A., Martinez-Carrion, M., Kagan, H.M. (eds) Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8397-9_16
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DOI: https://doi.org/10.1007/978-3-0348-8397-9_16
Publisher Name: Birkhäuser, Basel
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