TY - JOUR AU - Bootorabi, Fatemeh AU - Jänis, Janne AU - Valjakka, Jarkko AU - Isoniemi, Sari AU - Vainiotalo, Pirjo AU - Vullo, Daniela AU - Supuran, Claudiu T. AU - Waheed, Abdul AU - Sly, William S. AU - Niemelä, Onni AU - Parkkila, Seppo PY - 2008 DA - 2008/11/27 TI - Modification of carbonic anhydrase II with acetaldehyde, the first metabolite of ethanol, leads to decreased enzyme activity JO - BMC Biochemistry SP - 32 VL - 9 IS - 1 AB - Acetaldehyde, the first metabolite of ethanol, can generate covalent modifications of proteins and cellular constituents. However, functional consequences of such modification remain poorly defined. In the present study, we examined acetaldehyde reaction with human carbonic anhydrase (CA) isozyme II, which has several features that make it a suitable target protein: It is widely expressed, its enzymatic activity can be monitored, its structural and catalytic properties are known, and it contains 24 lysine residues, which are accessible sites for aldehyde reaction. SN - 1471-2091 UR - https://doi.org/10.1186/1471-2091-9-32 DO - 10.1186/1471-2091-9-32 ID - Bootorabi2008 ER -