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EnglishAmine oxidases are a family of dimeric enzymes that contain one copper(II) ion and one 2,4,5-trihydroxyphenyalanine quinone per subunit. Here, the low-resolution structures of two Cu/TPQ amine oxidases from lentil (Lens esculenta) seedlings and from Euphorbia characias latex have been determined in solution by small-angle X-ray scattering. The active site of these enzymes is highly buried and requires a conformational change to allow substrate access. The study suggests that the funnel-shaped cavity located between the D3 and D4 domains is narrower within the crystal structure, whereas in solution the D3 domain could undergo movement resulting in a protein conformational change that is likely to lead to easier substrate access.
| Titolo: | Domain mobility as probed by small angle X-ray scattering may account for substrate access to the active site of two copper-dependent amine oxidases | |
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| Data di pubblicazione: | 2014 | |
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| Handle: | http://hdl.handle.net/11697/155942 | |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
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http://hdl.handle.net/11697/155942
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