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2 L-cysteine
(2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) + H2S
-
-
-
?
3-chloro-L-alanine + NaHS
L-cysteine + ?
-
beta-replacement reaction, enzyme can be induced by 3-chloro-L-alanine
-
?
5-thio-2-nitrobenzoate + O-acetyl-L-serine
acetate + ?
-
-
-
-
?
beta-chloro-L-alanine + 2-nitro-5-thiobenzoate
?
-
-
-
-
?
chloroalanine + sulfide
cysteine + chloride
cyanide + cysteine
beta-cyanoalanine + sulfide
-
-
-
?
cysteine + CN-
cyanoalanine + H2S
L-Cys + acetate
?
-
involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear
-
-
?
L-Cys + acetate
O-acetyl-L-Ser + H2S
L-Cys + dithiothreitol
beta-cyanoalanine + H2S
-
-
-
?
L-cysteine + cyanide
cyanoalanine + H2S
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
L-cysteine + H2O
L-serine + H2S
A0A1J9VES8
-
-
-
?
L-cysteine + L-cysteine
L-lanthionine + H2S
L-cysteine + L-homocysteine
L-cystathionine + H2S
L-homocysteine + L-serine
L-cystathionine + H2O
-
-
-
?
L-homoserine + sulfide
?
-
1.6% of the activity with O-acetyl-L-serine
-
-
?
monofluoralanine + H2S
?
-
-
-
?
NaN3 + O-acetyl-Ser
beta-azidoalanine + sodium acetate
O-acetyl-L-Ser + 1,2,3,4-tetrazole
?
-
-
-
-
?
O-acetyl-L-Ser + 1,2,3-benzotriazole
?
-
weak activity
-
-
?
O-acetyl-L-Ser + 1,2,4-triazole
?
-
-
-
-
?
O-acetyl-L-Ser + 1-propanethiol
?
-
-
-
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
O-acetyl-L-Ser + 3-mercapto-1,2,4-triazole
?
-
-
-
-
?
O-acetyl-L-Ser + 5-mercapto-2-nitrobenzoate
S-(3-carboxy-4-nitrophenyl)-L-cysteine + ?
-
-
-
?
O-acetyl-L-Ser + benzenethiol
L-cys + benzylacetate
-
-
-
-
?
O-acetyl-L-Ser + cysteamine
?
-
weak activity
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
O-acetyl-L-Ser + hydrogen sulfide
L-Cys + acetate
O-acetyl-L-Ser + isoxazolin-5-one
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
O-acetyl-L-Ser + pyrazole
?
-
weak activity
-
-
?
O-acetyl-L-Ser + S2O32-
S-sulfocysteine + ?
O-acetyl-L-Ser + sodium azide
?
-
weak activity
-
-
?
O-acetyl-L-Ser + sodium thiosulfate
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
O-acetyl-L-Ser + thiosulfate
S-sulfocysteine + sodium acetate
O-acetyl-L-serine
L-cysteine + acetate
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
O-acetyl-L-serine + H2O
pyruvate + acetate + NH3
-
-
-
?
O-acetyl-L-serine + H2S
L-cysteine + acetic acid
A0A1J9VES8
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
O-acetyl-L-serine + sulfide
L-Cys + acetate
-
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate + H+
-
-
-
-
?
O-acetyl-Ser + selenide
selenocysteine + acetate
-
maximal 40% rate of cysteine synthesis
-
?
O-acetylhomoserine + H2S
homocysteine + ?
O-diazoacetyl-L-serine + sulfide
?
O-phosphoserine + H2S
L-Cys + phosphate
-
-
-
-
?
O-succinyl-L-homoserine + sulfide
?
O3-acetyl-L-serine
alpha-aminoacrylate
-
-
in absence of S2- and at 50°C, not below
-
?
O3-acetyl-L-serine + 2-nitro-5-thiobenzoate
?
O3-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
O3-acetyl-L-serine + benzylmercaptan
S-benzyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + cyanide
beta-cyano-L-alanine + acetate
-
-
-
?
O3-acetyl-L-serine + ethylmercaptan
S-ethyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
O3-acetyl-L-serine + hydrogensulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + methylmercaptan
S-methyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + phenol
O-phenyl-L-serine + acetate
-
-
-
?
O3-acetyl-L-serine + phenylmercaptan
S-phenyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + propylmercaptan
S-propyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + sulfide
L-cysteine + acetate
-
-
-
-
?
Ser + sulfide
?
-
1.8% of the activity with O-acetyl-L-serine
-
-
?
additional information
?
-
chloroalanine + sulfide
cysteine + chloride
-
3-6% of the activity of the cysteine synthase reaction
-
r
chloroalanine + sulfide
cysteine + chloride
-
beta-chloroalanine, 6% of the activity with O-acetyl-L-Ser
-
-
r
chloroalanine + sulfide
cysteine + chloride
-
beta-chloroalanine, 6% of the activity with O-acetyl-L-Ser
-
-
r
cysteine + CN-
cyanoalanine + H2S
-
-
H2S i.e. bisulfide
?
cysteine + CN-
cyanoalanine + H2S
Xanthium pennsylvanicum
-
-
-
?
cysteine + CN-
cyanoalanine + H2S
Xanthium pennsylvanicum
-
involved in cyanide metabolism during seed germination
-
-
?
L-Cys + acetate
O-acetyl-L-Ser + H2S
-
-
-
r
L-Cys + acetate
O-acetyl-L-Ser + H2S
-
-
-
r
L-Cys + acetate
O-acetyl-L-Ser + H2S
-
-
-
r
L-Cys + acetate
O-acetyl-L-Ser + H2S
-
equilibrium constant
-
r
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
the side reaction of the enzyme seems to contribute massively to the total H2S release of higher plants at least at higher pH values
-
-
?
L-cysteine + L-cysteine
L-lanthionine + H2S
-
preferred reaction
-
-
?
L-cysteine + L-cysteine
L-lanthionine + H2S
-
preferred reaction
-
-
?
L-cysteine + L-homocysteine
L-cystathionine + H2S
A0A1J9VES8
-
-
-
?
L-cysteine + L-homocysteine
L-cystathionine + H2S
-
-
-
?
NaN3 + O-acetyl-Ser
beta-azidoalanine + sodium acetate
-
-
mutagenic
?
NaN3 + O-acetyl-Ser
beta-azidoalanine + sodium acetate
-
-
mutagenic in Salmonella typhimurium
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
18% of activity with sulfide
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
6.2% of the activity with sulfide, isoenzyme 2
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
2.6% and 6.8% of the activity with sulfide, isoenzyme 1 and 2, respectively
-
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
18% of activity with sulfide
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
enzyme that catalyzes the final step in cysteine biosynthesis. Cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
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
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
yeast two-hybrid system for screening of a cDNA library of Nicotiana plumbaginifolia for clones encoding plant proteins interacting with two proteins of Escherichia coli: serine acetyltransferase (SAT, the product of cysE gene) and O-acetylserine (thiol) lyase A, also termed cysteine synthase (OASTL-A, the product of cysK gene). Two plant cDNA clones are identified when using the cysE gene as a bait
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
equilibrium constant
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
the second half of the OASS-A reaction is limited by the conformational change needed to open the active site and release the amino acid product. No quinonoid or geminal-diamine intermediates are detected. The amino acid external Schiff base of the enzyme is found to be very stable when the reaction is run in D2O
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
OASTL activity regulates not only Cys de novo synthesis but also its homeostasis
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
r
O-acetyl-L-Ser + hydrogen sulfide
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + hydrogen sulfide
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + hydrogen sulfide
L-Cys + acetate
-
-
-
?
O-acetyl-L-Ser + isoxazolin-5-one
?
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
?
O-acetyl-L-Ser + isoxazolin-5-one
?
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
6.1% of activity with sulfide
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
2.2% of activity with sulfide, isoenzyme 1 and 2
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
2.3% and 1.6% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
2.5% of activity with sulfide
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
-
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
21.5% and 77% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
-
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
4% and 1% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
-
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
product identification uncertain
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
32% of activity with sulfide
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
6.84% and 7.64% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
12.3% of activity with sulfide
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
-
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
-
-
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
-
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
-
-
-
?
O-acetyl-L-Ser + S2O32-
S-sulfocysteine + ?
-
-
-
-
?
O-acetyl-L-Ser + S2O32-
S-sulfocysteine + ?
-
-
-
-
?
O-acetyl-L-Ser + sodium thiosulfate
?
-
-
-
-
?
O-acetyl-L-Ser + sodium thiosulfate
?
-
-
-
-
?
O-acetyl-L-Ser + sodium thiosulfate
?
-
-
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
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
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in synthesis of antioxidants such as glutathione during fruit development
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in glutathione formation
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
controlled by feedback inhibition, adaptively significant as sulfide removal mechanism
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
repressed during growth with sulfide or thiosulfide as sulfur source
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
key role in metabolism of S-containing amino acids
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
functions as a Cys synthase rather than as a homocysteine synthase in vivo
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
enzyme transcription repressed by L-cystine, derepressed by limiting sulfide concentrations
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in thiosulfate assimilation
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
activity varies between sulfur sources, enzyme formation regulated by L-Cys concentration
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + thiosulfate
S-sulfocysteine + sodium acetate
-
-
-
-
?
O-acetyl-L-Ser + thiosulfate
S-sulfocysteine + sodium acetate
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
A0A1J9VES8
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
ir
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
ir
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine
L-cysteine + acetate
Xanthium pennsylvanicum
-
-
-
-
?
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
residue Arg210 near the entrance of the active site and is important for O-acetyl-L-serine substrate recognition
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
residue Arg210 near the entrance of the active site and is important for O-acetyl-L-serine substrate recognition
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate. The enzyme catalyzes the reaction with O-acetyl-L-serine and hydroxyurea with 80fold lower catalytic efficiency
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate. The enzyme catalyzes the reaction with O-acetyl-L-serine and hydroxyurea with 80fold lower catalytic efficiency
-
-
?
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
-
-
-
?
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetylhomoserine + H2S
homocysteine + ?
-
-
-
?
O-acetylhomoserine + H2S
homocysteine + ?
-
not, low molecular weight enzyme
-
-
?
O-acetylhomoserine + H2S
homocysteine + ?
-
2.4% of the activity with O-acetyl-L-Ser
-
-
?
O-acetylhomoserine + H2S
homocysteine + ?
-
2.4% of the activity with O-acetyl-L-Ser
-
-
?
O-diazoacetyl-L-serine + sulfide
?
-
44% of the activity with O-acetyl-Ser
-
-
?
O-diazoacetyl-L-serine + sulfide
?
-
44% of the activity with O-acetyl-Ser
-
-
?
O-succinyl-L-homoserine + sulfide
?
-
3.6% of the activity with O-acetyl-L-serine
-
-
?
O-succinyl-L-homoserine + sulfide
?
-
3.6% of the activity with O-acetyl-L-serine
-
-
?
O3-acetyl-L-serine + 2-nitro-5-thiobenzoate
?
-
-
-
-
?
O3-acetyl-L-serine + 2-nitro-5-thiobenzoate
?
-
-
-
-
?
O3-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O3-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
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
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
970% of the activity with cyanide
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.5.1.65, O-phosphoserine hydrolase
-
-
?
additional information
?
-
-
isoenzyme 1 and 2 have different substrate specificities towards various beta-substituted L-Cys
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
model of a dynamic cysteine synthesis system with regulatory function
-
-
?
additional information
?
-
-
preferred state of sulfide is hydrogen sulfide
-
-
?
additional information
?
-
the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity
-
-
?
additional information
?
-
-
the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
A0A1J9VES8
no substrate: L-serine
-
-
?
additional information
?
-
-
no substrate: L-serine
-
-
?
additional information
?
-
-
beta-substituted alanines, low activity
-
-
?
additional information
?
-
the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
-
-
?
additional information
?
-
-
the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
-
-
?
additional information
?
-
-
beta-substituted alanines, low activity
-
-
?
additional information
?
-
-
several nucleophiles may stimulate sulfide formation
-
-
?
additional information
?
-
-
activity of the enzyme bound to serine acetyltransferase is lower than that of the free enzyme
-
-
?
additional information
?
-
no substrate: L-serine, L-homoserine, O-acetyl-L-homoserine, L-alanine, L-homocysteine
-
-
?
additional information
?
-
-
no substrate: L-serine, O-propionyl-L-serine, L-alanine, glycine
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the binding free energy of 400 pentapeptides, MNXXI, interacting with the HiOASS-A active site using a combined docking-scoring procedure based on GOLD and HINTare examined. The free energy prediction is verified by the experimental determination of the binding affinity of 14 of these pentapeptides, selected for spanning a large range of predicted binding affinity and presenting charged, polar, or apolar residues at mutation sites
-
-
?
additional information
?
-
the binding free energy of 400 pentapeptides, MNXXI, interacting with the HiOASS-A active site using a combined docking-scoring procedure based on GOLD and HINTare examined. The free energy prediction is verified by the experimental determination of the binding affinity of 14 of these pentapeptides, selected for spanning a large range of predicted binding affinity and presenting charged, polar, or apolar residues at mutation sites
-
-
?
additional information
?
-
no substrates: serine, phosphoserine, O-succinylhomoserine, thiosulfate
-
-
?
additional information
?
-
-
no substrates: serine, phosphoserine, O-succinylhomoserine, thiosulfate
-
-
?
additional information
?
-
no synthesis of mimosine. The enzyme is specific for cysteine synthesis. The recombinant enzyme is active with or without the leader peptide
-
-
?
additional information
?
-
-
no synthesis of mimosine. The enzyme is specific for cysteine synthesis. The recombinant enzyme is active with or without the leader peptide
-
-
?
additional information
?
-
-
enzyme additionally catalyzes synthesis of mimosine, reaction of EC 2.5.1.52. The apparent kcat for Cys production is over sixfold higher than mimosine synthesis and the apparent Km is 3.7 times lower
-
-
-
additional information
?
-
enzyme additionally catalyzes synthesis of mimosine, reaction of EC 2.5.1.52. The apparent kcat for Cys production is over sixfold higher than mimosine synthesis and the apparent Km is 3.7 times lower
-
-
-
additional information
?
-
-
enzyme is unable to synthesize mimosine, reaction of EC 2.5.1.52
-
-
-
additional information
?
-
enzyme is unable to synthesize mimosine, reaction of EC 2.5.1.52
-
-
-
additional information
?
-
enzyme is specific for synthesis of cysteine, no synthesis of mimosine
-
-
-
additional information
?
-
-
enzyme is specific for synthesis of cysteine, no synthesis of mimosine
-
-
-
additional information
?
-
-
the enzyme is induced by Al3+. Cysteine synthase may be a key player during Al response/adaptation in rice
-
-
?
additional information
?
-
protein predominately catalyzes the synthesis but not the degradation of cysteine. The L-cysteine desulfhydrase reaction may be a side reaction
-
-
-
additional information
?
-
-
beta-substituted alanines, low activity
-
-
?
additional information
?
-
enzyme additionally catalyzes the formation of O-ureido-L-serine from O-acetyl-L-serine and hydroxyurea, reaction of EC 2.6.99.3. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
-
-
?
additional information
?
-
-
enzyme additionally catalyzes the formation of O-ureido-L-serine from O-acetyl-L-serine and hydroxyurea, reaction of EC 2.6.99.3. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
-
-
?
additional information
?
-
enzyme additionally catalyzes the formation of O-ureido-L-serine from O-acetyl-L-serine and hydroxyurea, reaction of EC 2.6.99.3. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
-
-
?