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cysteine + CN-
cyanoalanine + H2S
Xanthium pennsylvanicum
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involved in cyanide metabolism during seed germination
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L-Cys + acetate
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involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear
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L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
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the side reaction of the enzyme seems to contribute massively to the total H2S release of higher plants at least at higher pH values
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O-acetyl-L-Ser + H2S
L-Cys + acetate
O-acetyl-L-Ser + isoxazolin-5-one
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O-acetyl-L-Ser + S2O32-
S-sulfocysteine + ?
O-acetyl-L-Ser + sodium thiosulfate
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
additional information
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O-acetyl-L-Ser + H2S
L-Cys + acetate
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enzyme that catalyzes the final step in cysteine biosynthesis. Cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation
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O-acetyl-L-Ser + H2S
L-Cys + acetate
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Entamoeba histolytica, the causative agent of human amoebiasis, is essentially anaerobic, requiring a small amount of oxygen for growth. It cannot tolerate the higher concentration of oxygen present in human tissues or blood. However, during tissue invasion it is exposed to a higher level of oxygen, leading to oxygen stress. Cysteine, which is a vital thiol in Entamoeba histolytica, plays an essential role in its oxygen-defence mechanisms. The major route of cysteine biosynthesis in this parasite is the condensation of O-acetylserine with sulfide by the de novo cysteine-biosynthetic pathway, which involves cysteine synthase (EhCS) as a key enzyme
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O-acetyl-L-Ser + H2S
L-Cys + acetate
OASTL activity regulates not only Cys de novo synthesis but also its homeostasis
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O-acetyl-L-Ser + isoxazolin-5-one
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synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
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O-acetyl-L-Ser + isoxazolin-5-one
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synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
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O-acetyl-L-Ser + S2O32-
S-sulfocysteine + ?
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O-acetyl-L-Ser + S2O32-
S-sulfocysteine + ?
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?
O-acetyl-L-Ser + sodium thiosulfate
?
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O-acetyl-L-Ser + sodium thiosulfate
?
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
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the cysteine synthase complex functions as a molecular sensor system that monitors the sulfur status of the cell and controls sulfate assimilation and cysteine synthesis according to the availability of sulfate
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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last step of assimilatory sulfate reduction
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
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involved in synthesis of antioxidants such as glutathione during fruit development
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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involved in glutathione formation
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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final step in Cys synthesis
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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final step in Cys synthesis
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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controlled by feedback inhibition, adaptively significant as sulfide removal mechanism
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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final step in Cys synthesis
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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repressed during growth with sulfide or thiosulfide as sulfur source
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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key role in metabolism of S-containing amino acids
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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functions as a Cys synthase rather than as a homocysteine synthase in vivo
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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enzyme transcription repressed by L-cystine, derepressed by limiting sulfide concentrations
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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involved in thiosulfate assimilation
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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final step in Cys synthesis
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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final step in Cys synthesis
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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last step of assimilatory sulfate reduction
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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last step of assimilatory sulfate reduction
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?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
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last step of assimilatory sulfate reduction
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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activity varies between sulfur sources, enzyme formation regulated by L-Cys concentration
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O-acetyl-L-Ser + sulfide
L-Cys + acetate
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last step of assimilatory sulfate reduction
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
in the absence of sulfide O3-acetyl-L-serine reacts with the cofactor pyridoxal 5'-phosphate to alpha-aminoacrylate intermediate
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O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
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additional information
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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
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additional information
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model of a dynamic cysteine synthesis system with regulatory function
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additional information
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the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity
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additional information
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the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity
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additional information
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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
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additional information
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the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
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additional information
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the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
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additional information
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the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
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additional information
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the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
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additional information
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the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
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additional information
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the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
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additional information
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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
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additional information
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the enzyme is induced by Al3+. Cysteine synthase may be a key player during Al response/adaptation in rice
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