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Results 1 - 10 of 15 > >>
EC Number General Information Commentary Reference
Display the reaction diagram Show all sequences 2.1.1.282malfunction in DELTATYW3 strain, tRNAPhe has two wybutosine intermediates, 7-(3-amino-3-carboxypropyl)-4-demethylwyosine37 (yW-86) and 4-demethylwyosine37 (yW-14). Recombinant TYW3 clearly methylated 7-(3-amino-3-carboxypropyl)-4-demethylwyosine37 in tRNA to yield 7-(3-amino-3-carboxypropyl)-4-methylwyosine37 in tRNA in S-adenosyl-L-methionine-dependent manner. 4-Demethylwyosine37 is not methylated by TYW3 722112
Display the reaction diagram Show all sequences 2.1.1.282physiological function the enzyme is involved in the biosynthesis of the tricyclic base wybutosine 722112
Display the reaction diagram Show all sequences 2.1.1.282evolution archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a ), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c/ family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview 758324
Display the reaction diagram Show all sequences 2.1.1.282evolution archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a ), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c/ family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview. Crenarcheota Saccharolobus solfataricus as well as in other Sulfalobales and Desulfurococcales, two different tRNAPhe methyltransferases are involved in the biosynthesis of mimG, catalyzing the formation of m1G (Trm5c, EC 2.1.1.228) and imG2 (Trm5a, EC 2.1.1.282) at position 37 in tRNAPhe, respectively -, 758324
Display the reaction diagram Show all sequences 2.1.1.282evolution archaeal Trm5a, a member of the archaeal Trm5a/b/c family of enzymes involved in the biosynthesis of the wyosine derivatives, division of the family aTrm5 into three subfamilies aTrm5a (further divided into Taw21 and Taw22 which are monofunctional and bifunctional aTrm5a), aTrm5b, and aTrm5c. While the enzymes belonging to these subfamilies do not significantly differ in their AdoMet-binding site, small differences have been observed within the NPPY motif, which, in certain amino-methyltransferases, is involved in the positioning of the target nitrogen atom. In contrast, the N-terminal sequences of the aforementioned enzymes differ substantially, e.g. a small conservative domain called D1 is present in aTrm5b and aTrm5c but absent in most of the aTrm5a proteins. Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis of wyosine derivatives in Archaea. Amino acid sequence alignment of Trm5a/b/c/ family of proteins. Monofunctional and bifunctional aTrm5a enzymes, overview 758324
Display the reaction diagram Show all sequences 2.1.1.282malfunction substitutions of individual conservative amino acids of Pyrococcus abyssi Taw22 (P260N, E173A, and R174A) have a differential effect on the formation of m1G/imG2, while replacement of R134, F165, E213, and P262 with alanine abolishes the formation of both derivatives of G37 -, 758324
Display the reaction diagram Show all sequences 2.1.1.282metabolism putative enzymatic pathway leading to the formation of wyosine derivatives in Archaea -, 758324
Display the reaction diagram Show all sequences 2.1.1.282physiological function tricyclic wyosine derivatives are found at position 37 of eukaryotic and archaeal tRNAPhe. In Archaea, the intermediate imG-14 is targeted by three different enzymes that catalyze the formation of yW-86, imG, and imG2. Methyltransferase aTrm5a/Taw22 likely catalyzes two distinct reactions: N1-methylation of guanosine to yield m1G (EC 2.1.1.228), and C7-methylation of imG-14 to yield imG2 (EC 2.1.1.282) -, 758324
Display the reaction diagram Show all sequences 2.1.1.282malfunction deletion of the D1 domain greatly reduces the affinity and activity of PaTrm5a toward its RNA substrate 758348
Display the reaction diagram Show all sequences 2.1.1.282more structure comparison of the Pyrococcus abyssii Trm5a enzyme structure (PDB ID 5WT1) with the structure of its orthologue Trm5b (MjTrm5b, PDB IDs 2YX1 and 3AY0) from Methanococcus jannaschii, overview 758348
Results 1 - 10 of 15 > >>