The antiviral protein viperin is a radical SAM enzyme |
| |
Authors: | Kaitlin S Duschene |
| |
Institution: | Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA Astrobiology Biogeocatalysis Research Center, Montana State University, Bozeman, MT 59717, USA |
| |
Abstract: | Viperin, an interferon-inducible antiviral protein, is shown to bind an iron-sulfur cluster, based on iron analysis as well as UV-Vis and electron paramagnetic resonance spectroscopic data. The reduced protein contains a 4Fe-4S]1+ cluster whose g-values are altered upon addition of S-adenosylmethionine (SAM), consistent with SAM coordination to the cluster. Incubation of reduced viperin with SAM results in reductive cleavage of SAM to produce 5′-deoxyadenosine (5′-dAdo), a reaction characteristic of the radical SAM superfamily. The 5′-dAdo cleavage product was identified by a combination of HPLC and mass spectrometry analysis. |
| |
Keywords: | SAM S-adenosylmethionine EPR electron paramagnetic resonance 5&prime -dAdo 5&prime -deoxyadenosine SAH S-(5&prime l-homocysteine" target="_blank">-adenosyl)-l-homocysteine MTA methylthioadenosine DAF 5-deazariboflavin |
本文献已被 ScienceDirect 等数据库收录! |
|