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Results 1 - 10 of 33 > >>
EC Number Natural Substrates Commentary (Nat. Sub.)
Show all pathways known for 2.5.1.47Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.47cysteine + CN- involved in cyanide metabolism during seed germination
Show all pathways known for 2.5.1.47Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.47L-Cys + acetate involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear
Show all pathways known for 2.5.1.47Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.47L-cysteine + dithiothreitol the side reaction of the enzyme seems to contribute massively to the total H2S release of higher plants at least at higher pH values
Show all pathways known for 2.5.1.47Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.47more enzyme is induced in leaves exposed to salt stress. The results suggest that the plant enzyme is responding to the salt stress by inducing cysteine biosynthesis as a protection against high ion concentrations
Show all pathways known for 2.5.1.47Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.47more model of a dynamic cysteine synthesis system with regulatory function
Show all pathways known for 2.5.1.47Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.47more the enzyme is induced by Al3+. Cysteine synthase may be a key player during Al response/adaptation in rice
Show all pathways known for 2.5.1.47Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.47more the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
Show all pathways known for 2.5.1.47Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.47more cysteine synthase CysB is the only isoform of physiological importance in Aspergillus nidulans. Starvation-induced cysteine synthase activity is under control of cross-pathway regulation
Show all pathways known for 2.5.1.47Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.47more stopped-flow fluorescence spectroscopy is used to characterize the interaction of serine acetyltransferase with OASS and in the presence of the physiological regulators cysteine and bisulfide. Cysteine synthase assembly occurs via a two-step mechanism involving rapid formation of an encounter complex between the two enzymes, followed by a slow conformational change. The conformational change likely results from the closure of the active site of OASS upon binding of the serine acetyltransferase C-terminal peptide. Bisulfide stabilizes the cysteine synthase complex mainly by decreasing the back rate of the isomerization step. Cysteine, the product of the OASS reaction and a SAT inhibitor, slightly affects the kinetics of cysteine synthase formation leading to destabilization of the complex
Show all pathways known for 2.5.1.47Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.47more the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
Results 1 - 10 of 33 > >>