MiaA from Escherichia coli - protein summary.
Position of modification - modification:
t:37 - i6A
Bacterial MiaA, initially called dimethylallyl diphosphate:tRNA dimethylallyltransferase, belongs to the IPP transferase superfamily including eukaryotic Mod5. It catalyzes the transfer of isopentenyl group on N6 of A37 in most A36A37-containing tRNA. Isopentenyl originates from ispentenyl-pyrophosphate (IPP). MiaA-like proteins are totally absent in Archaea.
Molecular cloning of the Escherichia coli miaA gene involved in the formation of delta 2-isopentenyl adenosine in tRNA.
Caillet J, Droogmans L
Structural bioinformatics analysis of enzymes involved in the biosynthesis pathway of the hypermodified nucleoside ms(2)io(6)A37 in tRNA.
Kaminska KH, Baraniak U, Boniecki M, Nowaczyk K, Czerwoniec A, Bujnicki JM
Snapshots of dynamics in synthesizing N(6)-isopentenyladenosine at the tRNA anticodon.
Chimnaronk S, Forouhar F, Sakai J, Yao M, Tron CM, Atta M, Fontecave M, Hunt JF, Tanaka I
RNA-protein mutually induced fit: structure of Escherichia coli isopentenyl-tRNA transferase in complex with tRNA(Phe).
Seif E, Hallberg BM
J Biol Chem
Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: a binding mechanism for recombinant enzyme.
Moore JA, Poulter CD
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