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Results 1 - 10 of 23 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.50evolution EgtB contains a strongly conserved HX3HXE motif, implying that it is a member of the facial triad enzyme family with the Fe(II) site ligated by 2-His-1-Glu 745390
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.50evolution enzyme EgtB belongs to the mononuclear nonheme iron dioxygenase family -, 745070
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.50evolution enzyme EgtB represents a distinct enzyme class (sulfoxide synthases) with no relation to sulfur oxidizing or C-S bond-forming iron enzymes such as cysteine dioxygenase or isopenicillin synthase 733092
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.50evolution OvoA, EC 1.14.99.52, and EgtB are related in sequence, while they are biochemically distinct -, 743388
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.50evolution Some cyanobacteria recruited and adapted a sulfoxide synthase from a different biosynthetic pathway to make ergothioneine. Evolutionary malleability of the thiohistidine biosynthetic machinery. The sulfoxide synthase EgtB catalyzes the sulfurization of N-alpha-trimethylhistidine at the imidazole 2-position and subsequent oxidation to the S-sulfoxide. The homologous sulfoxide synthases OvoA, EC 1.14.99.52, catalyze the formation of 5-histidylcysteine sulfoxide. The stereochemistry of this sulfoxide is unknown, and cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution. Prokaryotic EgtBs are usually monofunctional, fungal EgtBs are fused to EgtD 744709
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.50evolution the two known sulfoxide synthases EgtB and OvoA distinguish themselves from each other by their substrate preferences and product C-S bond regioselectivity -, 734829
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.50malfunction a single point mutation Y377F converts this enzyme into a gamma-glutamyl cysteine dioxygenase with an efficiency that rivals naturally evolved thiol dioxygenases 744679
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.50metabolism biosynthesis of N-alpha-trimethyl-2-thiohistidine (ergothioneine) is a frequent trait in cyanobacteria. This sulfur compound may provide essential relief from oxidative stress related to oxygenic photosynthesis. The central steps in ergothioneine biosynthesis are catalyzed by a histidine methyltransferase and the iron-dependent sulfoxide synthase. Ergothioneine biosynthesis starts by trimethylation of the alpha-amino group of histidine. The resulting N-alpha-trimethylhistidine (TMH) is fused to either gamma-glutamylcysteine (in actinomycetes, EC 1.14.99.50) or cysteine (in fungi, EC 1.14.99.51). The sulfoxide product is converted into ergothoneine by removal of the glutamyl and cysteinyl moieties 744709
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.50metabolism EgtB is a nonheme iron enzyme catalyzing the C-S bond formation between gamma-glutamyl cysteine and N-alpha-trimethyl histidine in the ergothioneine biosynthesis -, 745070
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.50metabolism enzyme EgtB catalyzes O2-dependent C-S bond formation between gamma-glutamyl cysteine and N-alpha-trimethyl histidine as the central step in ergothioneine biosynthesis 733092
Results 1 - 10 of 23 > >>