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Status table SHERPA RoMEO
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|Blue||can archive post-prints|
|Yellow||can archive pre-prints|
|White||can not archive any materials|
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- Gdańsk University of Technology
Papers published in magazine
Crystal structures of aminotransferases Aro8 and Aro9 from Candida albicans and structural insights into their propertiesPublication
Aminotransferases catalyze reversibly the transamination reaction by a ping-pong bi-bi mechanism with pyridoxal 5′-phosphate (PLP) as a cofactor. Various aminotransferases acting on a range of substrates have been reported. Aromatic transaminases are able to catalyze the transamination reaction with both aromatic and acidic substrates. Two aminotransferases from C. albicans, Aro8p and Aro9p, have been identified recently, exhibiting...
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