2014
DOI: 10.1016/j.bbrc.2014.09.058
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Structural insights into the histidine trimethylation activity of EgtD from Mycobacterium smegmatis

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Cited by 27 publications
(24 citation statements)
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“…EgtD catalyzes the initial step in the biosynthesis of ergothioneine by catalyzing the trimethylation of the α -amino acid moiety of l -histidine (Figure 6A). 26,36 Previously, determination of the affinity for l -histidine and AdoMet to Mycobacterium smegmatis EgtD using isothermal calorimetry showed K d values of 290 ± 14 and 270 ± 20 μ M, 36 respectively. Kinetic characterization of l -histidine by EgtD at nonsaturating AdoMet concentrations using the developed competitive FP assay demonstrated a K m app value of 330 ± 35 μ M (Figure 6B), which is within error of the previously determined K d value for the homologue.…”
Section: Resultsmentioning
confidence: 99%
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“…EgtD catalyzes the initial step in the biosynthesis of ergothioneine by catalyzing the trimethylation of the α -amino acid moiety of l -histidine (Figure 6A). 26,36 Previously, determination of the affinity for l -histidine and AdoMet to Mycobacterium smegmatis EgtD using isothermal calorimetry showed K d values of 290 ± 14 and 270 ± 20 μ M, 36 respectively. Kinetic characterization of l -histidine by EgtD at nonsaturating AdoMet concentrations using the developed competitive FP assay demonstrated a K m app value of 330 ± 35 μ M (Figure 6B), which is within error of the previously determined K d value for the homologue.…”
Section: Resultsmentioning
confidence: 99%
“…25,26 An in-depth protocol for cloning and purification for both enzymes can be found in the supplemental section of the manuscript.…”
Section: Methodsmentioning
confidence: 99%
“…First, it is well documented that methyltransferases undergo extensive conformational changes upon substrate and cofactor binding. The apo forms of SAM-dependent methyltransferases frequently exhibit an open conformation in which the N-terminal region and the lid domain are distant from the core domain36444546. Hence, active site residues are predominantly solvent-exposed and ready to interact with the incoming substrate and cofactor.…”
Section: Resultsmentioning
confidence: 99%
“…These results suggest that the SAM-mediated effect on (mt)pre-tRNA Leu(UUR) and (mt)pre-tRNA Val binding affinity and processing by mtRNase P is linked to cofactor binding to MRPP1/2 rather than pre-tRNA methylation. There are several examples in the literature in which SAM acts as an effector molecule affecting protein function and activity; SAM is an allosteric regulator of human cystathione-β-synthase and histidine trimethylase EgtD from Mycobacterium smegmatis (Lin et al 2012;Jeong et al 2014;McCorvie et al 2014). Furthermore, in the presence of SAM, a bifunctional restriction enzyme harboring a methyltransferase domain, RM.BpuSI, had increased processing activity without significant methylation activity (Sarrade-Loucheur et al 2013), similar to mtRNase P acting on (mt)pre-tRNA Val .…”
Section: Discussionmentioning
confidence: 99%