TI - 1-meG and 3-meT do not stimulate AlkB -mediated decarboxylation of 2-oxoglutarate . AB - Many members of the superfamily of iron - and 2-oxoglutarate -dependent oxygenases are able to catalyse the decarboxylation of 2-oxoglutarate to succinate at a low rate even in the absence of their primary SUBstrate ( 'uncoupled reaction' ) , and this is also the case for AlkB ( 6,7 ) . Moreover , the uncoupled AlkB reaction can be stimulated by various nucleosides and bases representing the AlkB relevant lesions , i.e.the nucleosides 1-methyladenosine , 1-methyl-2'-deoxyadenosine , 3-methylcytidine , 3-methyl-2'-deoxycytidine and the free base 1-meA ( 12 ) . Therefore , we also tested the ability of 1-meG and 3-meT , as well as corresponding nucleosides , to stimulate the uncoupled AlkB reaction . However , while 1-methyladenosine , as previously reported , caused a substantial increase in the decarboxylation of 2-oxoglutarate , no such effect was observed with 1-meG , 3-meT , 3-methyl-2'-deoxythymidine or 1-methylguanosine ( Figure 5 ) .