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TRNA wybutosine-synthesizing protein 3

Enzyme From Wikipedia, the free encyclopedia

TRNA wybutosine-synthesizing protein 3
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tRNA wybutosine-synthesizing protein 3, known also as tRNAPhe 7-[(3-amino-3-carboxypropyl)-4-demethylwyosine37-N4]-methyltransferase, abbreviated to TYW3 is an S-adenosyl-L-methionine-dependent methyltransferase that is involved in the biosynthetic pathway of wybutosine, a hyper-modified guanosine possessing tricyclic base found at the 3'-position which is close to the anticodon of eukaryotic phenylalanine tRNA.[1] TYW3 is believed to also methylate the carboxyl group of leucine to form α-leucine esters.[2] The enzyme catalyzes the following reaction,

4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) + S-adenosyl-L-methionine = 7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) + S-adenosyl-L-homocysteine + H+
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The modifications this enzyme makes are important for translational reading-frame maintenance. TYW3 is found in all eukaryotes and in some archaea, but not in bacteria.[3][4]

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