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Results 1 - 10 of 15 > >>
EC Number General Information Commentary Reference
Display the reaction diagram Show all sequences 2.1.1.282evolution 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 2.1.1.282evolution during the evolutionary process, some euryarchaeota like Thermococcus and Pyrococcus preserved both the trm5 genes from the crenarchaeal origin as well as the native copy, but others apparently lost the latter. Phylogenetic distribution analyses of trm5 homologues in archaeal genomes allow the identification of three archaeal Trm5 (aTrm5) subfamilies: Trm5a, Trm5b, and Trm5c. Trm5b refers to the native form, while Trm5a refers to the crenarchaeal origin, and Trm5c to other members with divergent Trm5 sequences11. The three Trm5s differ substantially in primary sequences 758376
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 2.1.1.282malfunction 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 2.1.1.282malfunction 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 2.1.1.282metabolism the enzyme is part of the biosynthetic pathway of mimG in Pyrococcus abyssi, overview. In archaea, G37 hypermodification in tRNAPhe leads to wyosine derivatives. They are important in reading-frame maintenance during protein synthesis, while the absence of such modifications results in elevated error rates in +1 frame-shifting. Among the modification products, 7-methylwyosine (mimG) is perhaps the earliest and minimalist version of the wyosine derivatives unique to some archaea, and 4-demethylwyosine (imG-14), isowyosine (imG2) have also been identified as intermediates along the pathway. The first biosynthetic step of mimG is the formation of m1G37, catalysed by the S-adenosine-L-methionine (SAM)-dependent tRNA methyltransferase named Trm5, which belongs to class-I methyltransferases. The second step is the complex radical-mediated formation of imG-14, catalyzed by the radical SAM enzyme Taw1. The Trm5 enzyme from the archaeon Pyrococcus abyssi (PaTrm5a) also catalyzes the methylation of C7 on imG-14 to produce imG2 (EC 2.1.1.282), which is further methylated on the N4 position of the imidazo-purine ring by Taw3 to form mimG 758376
Display the reaction diagram Show all sequences 2.1.1.282more enzyme structure comparisons 758376
Results 1 - 10 of 15 > >>