Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.64 - 4.28
O-acetyl-L-Ser
0.46
O-acetyl-L-serine
-
-
0.31 - 10.2
O3-acetyl-L-serine
additional information
additional information
-
HPLC method for product quantification
-
0.37
H2S
-
pH 7.0, 25°C, recombinant free enzyme
0.55
H2S
-
pH 7.5, 25°C, recombinant complex-bound enzyme
3
hydrogen sulfide
-
isoform B, pH 7.5, 25°C, Michaelis-Menten kinetics
3.2
hydrogen sulfide
-
isoform B, pH 7.5, 25°C, Hill equation, Hill coefficient 0.75
4.6
hydrogen sulfide
-
isoform C, pH 7.5, 25°C, Hill equation, Hill coefficient 1.05
4.7
hydrogen sulfide
-
isoform C, pH 7.5, 25°C, Michaelis-Menten kinetics
5.6
hydrogen sulfide
-
isoform A, pH 7.5, 25°C, Michaelis-Menten kinetics
6.4
hydrogen sulfide
-
isoform A, pH 7.5, 25°C, Hill equation, Hill coefficient 0.81
0.64
O-acetyl-L-Ser
-
pH 7.5, 25°C, recombinant free enzyme
4.28
O-acetyl-L-Ser
-
pH 7.5, 25°C, recombinant complex-bound enzyme
0.31
O3-acetyl-L-serine
-
isoform B, pH 7.5, 25°C, Michaelis-Menten kinetics
0.32
O3-acetyl-L-serine
-
isoform B, pH 7.5, 25°C, Hill equation, Hill coefficient 1.03
0.43
O3-acetyl-L-serine
-
isoform C, pH 7.5, 25°C, Michaelis-Menten kinetics
0.51
O3-acetyl-L-serine
-
isoform C, pH 7.5, 25°C, Hill equation, Hill coefficient 0.86
0.57
O3-acetyl-L-serine
-
mutant S269A, pH 7.0, 25°C
0.66
O3-acetyl-L-serine
-
isoform A, pH 7.5, 25°C, Hill equation, Hill coefficient 1.05
0.68
O3-acetyl-L-serine
-
mutant T78A, pH 7.0, 25°C
0.69
O3-acetyl-L-serine
-
isoform A, pH 7.5, 25°C, Michaelis-Menten kinetics
0.82
O3-acetyl-L-serine
-
mutant T78S, pH 7.0, 25°C
0.91
O3-acetyl-L-serine
-
mutant H157Q, pH 7.0, 25°C
0.94
O3-acetyl-L-serine
-
mutant H157N, pH 7.0, 25°C
0.96
O3-acetyl-L-serine
-
mutant S269T, pH 7.0, 25°C
1.2
O3-acetyl-L-serine
-
mutant S75T, pH 7.0, 25°C
1.2
O3-acetyl-L-serine
-
mutant T182A, pH 7.0, 25°C
1.4
O3-acetyl-L-serine
-
wild-type, pH 7.0, 25°C
1.5
O3-acetyl-L-serine
-
mutant T185A, pH 7.0, 25°C
1.5
O3-acetyl-L-serine
-
mutant T74S, pH 7.0, 25°C
1.6
O3-acetyl-L-serine
-
mutant S75A, pH 7.0, 25°C
1.6
O3-acetyl-L-serine
-
mutant T182S, pH 7.0, 25°C
1.6
O3-acetyl-L-serine
-
mutant T185S, pH 7.0, 25°C
1.6
O3-acetyl-L-serine
-
mutant T74A, pH 7.0, 25°C
2
O3-acetyl-L-serine
-
mutant S75N, pH 7.0, 25°C
3.8
O3-acetyl-L-serine
-
mutant Q147S, pH 7.0, 25°C
4.4
O3-acetyl-L-serine
-
mutant Q147A, pH 7.0, 25°C
4.7
O3-acetyl-L-serine
-
mutant N77A, pH 7.0, 25°C
10.2
O3-acetyl-L-serine
-
mutant N77D, pH 7.0, 25°C
0.18
Sulfide
-
mutant N77D, pH 7.0, 25°C
0.21
Sulfide
-
mutant S75T, pH 7.0, 25°C
0.22
Sulfide
-
wild-type, pH 7.0, 25°C
0.22
Sulfide
-
mutant T182S, pH 7.0, 25°C
0.22
Sulfide
-
mutant T185A, pH 7.0, 25°C
0.23
Sulfide
-
mutant N77A, pH 7.0, 25°C
0.27
Sulfide
-
mutant Q147S, pH 7.0, 25°C
0.3
Sulfide
-
mutant H157Q, pH 7.0, 25°C
0.3
Sulfide
-
mutant T78S, pH 7.0, 25°C
0.36
Sulfide
-
mutant T185S, pH 7.0, 25°C
0.39
Sulfide
-
mutant T182A, pH 7.0, 25°C
0.4
Sulfide
-
mutant H157N, pH 7.0, 25°C
0.44
Sulfide
-
mutant T78A, pH 7.0, 25°C
0.54
Sulfide
-
mutant S269A, pH 7.0, 25°C
1.6
Sulfide
-
mutant S269T, pH 7.0, 25°C
1.7
Sulfide
-
mutant Q147A, pH 7.0, 25°C
3.2
Sulfide
-
mutant T74S, pH 7.0, 25°C
3.9
Sulfide
-
mutant T74A, pH 7.0, 25°C
4.6
Sulfide
-
mutant S75A, pH 7.0, 25°C
5.7
Sulfide
-
mutant S75N, pH 7.0, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.08 - 1780
O3-acetyl-L-serine
0.08
O3-acetyl-L-serine
-
mutant T74A, pH 7.0, 25°C
0.09
O3-acetyl-L-serine
-
mutant S75N, pH 7.0, 25°C
0.19
O3-acetyl-L-serine
-
mutant Q147S, pH 7.0, 25°C
0.34
O3-acetyl-L-serine
-
mutant N77D, pH 7.0, 25°C
1.07
O3-acetyl-L-serine
-
mutant T185A, pH 7.0, 25°C
3.11
O3-acetyl-L-serine
-
mutant T185S, pH 7.0, 25°C
4.02
O3-acetyl-L-serine
-
mutant Q147A, pH 7.0, 25°C
7.16
O3-acetyl-L-serine
-
mutant S75A, pH 7.0, 25°C
34.3
O3-acetyl-L-serine
-
mutant S269A, pH 7.0, 25°C
51.5
O3-acetyl-L-serine
-
mutant S75T, pH 7.0, 25°C
403
O3-acetyl-L-serine
-
mutant N77A, pH 7.0, 25°C
456
O3-acetyl-L-serine
-
mutant T74S, pH 7.0, 25°C
554
O3-acetyl-L-serine
-
mutant T78A, pH 7.0, 25°C
572
O3-acetyl-L-serine
-
mutant S269T, pH 7.0, 25°C
775
O3-acetyl-L-serine
-
mutant T78S, pH 7.0, 25°C
889
O3-acetyl-L-serine
-
mutant T182A, pH 7.0, 25°C
1055
O3-acetyl-L-serine
-
mutant H157Q, pH 7.0, 25°C
1520
O3-acetyl-L-serine
-
mutant H157N, pH 7.0, 25°C
1660
O3-acetyl-L-serine
-
mutant T182S, pH 7.0, 25°C
1780
O3-acetyl-L-serine
-
wild-type, pH 7.0, 25°C
0.22
Sulfide
-
mutant Q147S, pH 7.0, 25°C
0.42
Sulfide
-
mutant T74A, pH 7.0, 25°C
0.73
Sulfide
-
mutant N77D, pH 7.0, 25°C
1.44
Sulfide
-
mutant T185A, pH 7.0, 25°C
1.45
Sulfide
-
mutant S75N, pH 7.0, 25°C
5.57
Sulfide
-
mutant T185S, pH 7.0, 25°C
12.5
Sulfide
-
mutant Q147A, pH 7.0, 25°C
20.2
Sulfide
-
mutant S75A, pH 7.0, 25°C
29.5
Sulfide
-
mutant S269A, pH 7.0, 25°C
82.7
Sulfide
-
mutant S75T, pH 7.0, 25°C
155
Sulfide
-
mutant N77A, pH 7.0, 25°C
370
Sulfide
-
mutant T78S, pH 7.0, 25°C
537
Sulfide
-
mutant T78A, pH 7.0, 25°C
929
Sulfide
-
mutant S269T, pH 7.0, 25°C
1600
Sulfide
-
mutant T182A, pH 7.0, 25°C
1690
Sulfide
-
mutant T182S, pH 7.0, 25°C
1700
Sulfide
-
mutant T74S, pH 7.0, 25°C
1780
Sulfide
-
mutant H157Q, pH 7.0, 25°C
1990
Sulfide
-
mutant H157N, pH 7.0, 25°C
2170
Sulfide
-
wild-type, pH 7.0, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
brenda
-
root plasma membrane SO42- transporter SULTR1,2 physically interacts with the enzyme. The domain of SULTR1,2 important for association with enzyme is called the STAS domain, located at the C-terminus of the transporter and extending from the plasma membrane into the cytoplasm. The binding of enzyme to the STAS domain negatively impacts transporter activity. In contrast, the activity of purified enzyme measured in vitro is enhanced by co-incubation with the STAS domain of SULTR1,2 but not with the analogous domain of the SO42- transporter isoform SULTR1,1. The observations suggest a regulatory model in which interactions between SULTR1,2 and enzyme coordinate internalization of SO42- with the energetic/metabolic state of plant root cells
brenda
-
presence of an active CS26 enzyme exclusively in the thylakoid lumen
brenda
-
brenda
isozyme OAS-TL A
brenda
-
-
brenda
-
brenda
thylakoid lumen
brenda
-
bienzyme complex
brenda
isozyme OAS-TL B
brenda
-
-
brenda
-
isoform A
brenda
-
isoform OAS-TL A
brenda
isozyme OAS-TL A
brenda
-
-
brenda
-
isoform C
brenda
-
isoform OAS-TL C
brenda
-
serine O-acetyltransferase SAT3 and O-acetylserine sulfhydrolase can interact in plant mitochondria to form the cysteine synthase complex. Formation of the mitochondrial cysteine synthase complex might be promoted by the stabilizing effect of sulfide, by efficient export of O-acetylserine from mitochondria, or by a combination of both
brenda
isozyme OAS-TL C
brenda
isozyme OAS-TL C
brenda
-
isoform B
brenda
-
isoform OAS-TL B
brenda
additional information
the major isoforms, OAS-TL A, OAS-TL B, and OAS-TL C, catalyze the formation of Cys by combining O-acetylserine and sulfide in the cytosol, the plastids, and the mitochondria, respectively. Subcellular localization of OAS-TL proteins is more important for efficient Cys synthesis than total cellular OAS-TL activity in leaves
-
brenda
additional information
the major isoforms, OAS-TL A, OAS-TL B, and OAS-TL C, catalyze the formation of Cys by combining O-acetylserine and sulfide in the cytosol, the plastids, and the mitochondria, respectively. Subcellular localization of OAS-TL proteins is more important for efficient Cys synthesis than total cellular OAS-TL activity in leaves
-
brenda
additional information
the major isoforms, OAS-TL A, OAS-TL B, and OAS-TL C, catalyze the formation of Cys by combining O-acetylserine and sulfide in the cytosol, the plastids, and the mitochondria, respectively. Subcellular localization of OAS-TL proteins is more important for efficient Cys synthesis than total cellular OAS-TL activity in leaves
-
brenda
additional information
the major isoforms, OAS-TL A, OAS-TL B, and OAS-TL C, catalyze the formation of Cys by combining O-acetylserine and sulfide in the cytosol, the plastids, and the mitochondria, respectively. Subcellular localization of OAS-TL proteins is more important for efficient Cys synthesis than total cellular OAS-TL activity in leaves
-
brenda
additional information
the major isoforms, OAS-TL A, OAS-TL B, and OAS-TL C, catalyze the formation of Cys by combining O-acetylserine and sulfide in the cytosol, the plastids, and the mitochondria, respectively. Subcellular localization of OAS-TL proteins is more important for efficient Cys synthesis than total cellular OAS-TL activity in leaves
-
brenda
additional information
the major isoforms, OAS-TL A, OAS-TL B, and OAS-TL C, catalyze the formation of Cys by combining O-acetylserine and sulfide in the cytosol, the plastids, and the mitochondria, respectively. Subcellular localization of OAS-TL proteins is more important for efficient Cys synthesis than total cellular OAS-TL activity in leaves
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
malfunction
Cys can be supplied by the mother plant for the development of female gametophytes lacking OAS-TL activity. In contrast, the presence of at least one functional OAS-TL isoform is essential in the male gametophyte. Only the absence of both isozymes OAS-TL A and OAS-TL C results in a decreased incorporation of sulfur and the carbon/nitrogen backbone into thiols, which also causes lower thiol steady-state levels. A segregation pattern can only be explained by a gamete-lethal phenotype of the oastlABC triple mutant. Phenotypes of mutants in the generative phase of the life cycle, overview
malfunction
lack of a functional isozyme OASTL-A1 results in enhanced disease susceptibility against infection with virulent and non-virulent Pseudomonas syringae pv. tomato DC3000 strains. Reduction of the OASTL activity of the old3-1 protein in vitro causes autonecrosis in specific Arabidopsis accessions, association of an effector triggered-like immune response and metabolic disorder with with auto-necrosis in old3 mutants. A negative epistatic interaction with the old3-1 mutation is not linked to reduced cysteine biosynthesis. Mutations in O-acetylserine (thiol) lyase regulate innate immune responses and disease susceptibility
metabolism
the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview
metabolism
the subcellular compartmentation of Cys precursor formation is a remarkable feature of Cys synthesis in higher plants that implies a high degree of regulation between the participating compartments. Contribution of additional OAS-TL-like proteins to Cys synthesis, overview
physiological function
besides a role of OAST-A1 in cysteine biosynthesis, the enzyme is involved in regulation of plant immunity
physiological function
enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. Regulatory function of CysK/CysE interaction in plants, overview
physiological function
the major isoforms, OAS-TL A, OAS-TL B, and OAS-TL C, catalyze the formation of Cys by combining O-acetylserine and sulfide in the cytosol, the plastids, and the mitochondria, respectively. Subcellular localization of OAS-TL proteins is more important for efficient Cys synthesis than total cellular OAS-TL activity in leaves
malfunction
-
knockout mutants demonstrate a reduction in size and show paleness, but penetrance of the growth phenotype depend on the light regime. The cs26 mutant plants also show reductions in chlorophyll content and photosynthetic activity as well as elevated glutathione levels. cs26 mutant leaves are not able to properly detoxify reactive oxygen species, which accumulate to high levels under long-day growth conditions. The transcriptional profile of the cs26 mutant reveal that the mutation has a pleiotropic effect on many cellular and metabolic processes
malfunction
Cys can be supplied by the mother plant for the development of female gametophytes lacking OAS-TL activity. In contrast, the presence of at least one functional OAS-TL isoform is essential in the male gametophyte. Only the absence of both isozymes OAS-TL A and OAS-TL C results in a decreased incorporation of sulfur and the carbon/nitrogen backbone into thiols, which also causes lower thiol steady-state levels. A segregation pattern can only be explained by a gamete-lethal phenotype of the oastlABC triple mutant. Phenotypes of mutants in the generative phase of the life cycle, overview
malfunction
direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis. OAS-TL C loss-of-function mutant shows a retarded growth phenotype, conversely to the loss-of-function mutants for OAS-TL A and OAS-TL B
metabolism
biosynthesis of cysteine is one of the fundamental processes in plants providing the reduced sulfur for cell metabolism. It is accomplished by the sequential action of two enzymes, serine acetyltransferase and O-acetylserine (thiol) lyase (OAS-TL). Together they constitute the hetero-oligomeric cysteine synthase (CS) complex through specific protein-protein interactions influencing the rate of cysteine production. The enzyme activity and level of thiols are not influenced by PEP4 expression. Increased serine acetyltransferase activity, but not O-acetylserine (thiol) lyase activity is an efficient trigger for enhanced cysteine synthesis in planta
metabolism
the subcellular compartmentation of Cys precursor formation is a remarkable feature of Cys synthesis in higher plants that implies a high degree of regulation between the participating compartments. Contribution of additional OAS-TL-like proteins to Cys synthesis, overview
physiological function
-
loss of CS26 function results in dramatic phenotypic changes, which are dependent on the light treatment. Under long-day growth conditions, the photosynthetic characterization, based on substomatal CO2 concentrations and CO2 concentration in the chloroplast curves, reveals significant reductions in most of the photosynthetic parameters for cs26, which are unchanged under short-day growth conditions. These parameters include net CO2 assimilation rate, mesophyll conductance, and mitochondrial respiration at darkness. Mutant cs26 under long-day growth conditions requires more absorbed quanta per driven electron flux and fixed CO2. In cs26 plants, the excess electrons that are not used in photochemical reactions may form reactive oxygen species
physiological function
-
root plasma membrane SO42- transporter SULTR1,2 physically interacts with the enzyme. The domain of SULTR1,2 important for association with enzyme is called the STAS domain, located at the C-terminus of the transporter and extending from the plasma membrane into the cytoplasm. The binding of enzyme to the STAS domain negatively impacts transporter activity. In contrast, the activity of purified enzyme measured in vitro is enhanced by co-incubation with the STAS domain of SULTR1,2 but not with the analogous domain of the SO42- transporter isoform SULTR1,1. The observations suggest a regulatory model in which interactions between SULTR1,2 and enzyme coordinate internalization of SO42- with the energetic/metabolic state of plant root cells
physiological function
S-sulfocysteine activity of enzyme is essential for the proper photosynthetic performance of the chloroplast under long-day growth conditions. Results suggest that S-sulfocysteine synthase functions as a protein sensor to detect the accumulation of thiosulfate as a result of the inadequate detoxification of reactive oxygen species generated under conditions of excess light to produce the S-sulfocysteine molecule that triggers protection mechanisms of the photosynthetic apparatus
physiological function
-
the enzyme's active site has two access sites. Binding of the enzyme to the C-terminal tail of serine O-acetyltransferase leads to loss of activity due to reduction in ligand accessibility of the second, unoccupied active site. The observed dynamics of the gates show allosteric closure of the unoccupied active site of the enzyme in the cysteine synthase complex, which can hinder substrate binding, abolishing its turnover to cysteine
physiological function
-
the mitochondrial cysteine synthase complex CSC acts as a sensor that regulates the level of serine O-acetyltransferase activity in response to sulfur supply and cysteine demand
physiological function
biosynthesis of cysteine is one of the fundamental processes in plants providing the reduced sulfur for cell metabolism. It is accomplished by the sequential action of two enzymes, serine acetyltransferase (SAT) and O-acetylserine (thiol) lyase (OAS-TL). Together they constitute the hetero-oligomeric cysteine synthase (CS) complex through specific proteinprotein interactions influencing the rate of cysteine production. The function of the complex formation is not metabolic channeling, but sensing the sulfur status of the cell to properly adjust the sulfur homeostasis. Whereas OAS-TL is only active outside the CS complex, SAT is strongly activated by association with OAS-TL. Mitochondrial isozyme OAS-TL C has an additional function besides cysteine synthesis, regulatory function when complexed with serine acetyltransferase. The formation of the CS complex is also important because of the inhibition of the free serine acetyltransferase by cysteine
physiological function
the major isoforms, OAS-TL A, OAS-TL B, and OAS-TL C, catalyze the formation of Cys by combining O-acetylserine and sulfide in the cytosol, the plastids, and the mitochondria, respectively. Subcellular localization of OAS-TL proteins is more important for efficient Cys synthesis than total cellular OAS-TL activity in leaves
physiological function
cyclophilin 20-3, 2-cysteine peroxiredoxin and cysteine synthase form a redox-sensitive module. The interference of the module is accompanied with disturbance of carbohydrate, sulfur and nitrogen metabolism, and also citric acid cycle intermediates. Serine acetyltransferase2-1 and OASB appear to play antagonistic functions in sulfur metabolism, and also in nitrogen metabolism
additional information
auto-necrosis depends on recognition of peronospora parasitica 1 (RPP1)-like disease resistance R gene(s) from an evolutionarily divergent R gene cluster that is present in Ler-0 but not the reference accession Col-0
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific, interaction analysis and binding structure. Negative cooperativity with decapeptide binding to AtCysK
additional information
computational modeling is used to build a model of the Arabidopsis thaliana mitochondrial cysteine synthase complex, overview. Direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis, several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for SAT binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation
additional information
-
computational modeling is used to build a model of the Arabidopsis thaliana mitochondrial cysteine synthase complex, overview. Direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis, several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for SAT binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
G162E
naturally occuring mutation, the EMS-induced single nucleotide substitution in the cytosolic OASTL-A1 gene in the Ler-0 accession of Arabidopsis thaliana causes early senescence and death in plants, and is referred to as onset of leaf death3 (old3-1)
H157N
-
comparable to wild-type
H157Q
-
reduced kcat-value, reduced Km-value
K46A
-
no enzymic activity, crystallization data
N77A
-
reduced kcat-value
N77D
-
drastically reduced kcat-value
Q147E
-
drastically reduced kcat-value, increased Km-value
S269A
-
reduced kcat-value, reduced Km-value
S269T
-
reduced kcat-value, reduced Km-value
S75N
-
drastically reduced kcat-value
T182A
-
reduced kcat-value
T182S
-
comparable to wild-type
T185A
-
drastically reduced kcat-value
T185S
-
drastically reduced kcat-value
T74A
-
drastically reduced kcat-value
T78A
-
reduced kcat-value, reduced Km-value
T78S
-
reduced kcat-value, reduced Km-value
Y302A
-
loss of enzymic activity
Q147A
-
drastically reduced kcat-value, increased Km-value
Q147A
-
mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
S75A
-
drastically reduced kcat-value
S75A
-
mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
S75T
-
drastically reduced kcat-value
S75T
-
mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
T74S
-
reduced kcat-value
T74S
-
mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
additional information
upon expression of the enzymes of the cysteine synthase complex, serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL, cross-binding of Arabidopsis thaliana OAS-TL with Escherichia coli SAT may take place
additional information
-
upon expression of the enzymes of the cysteine synthase complex, serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL, cross-binding of Arabidopsis thaliana OAS-TL with Escherichia coli SAT may take place
additional information
generation of a OAS-TL A mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview. The incorporation of sulfur into thiols but not thiol steady-state levels is decreased in mutants lacking cytosolic OAS-TL A
additional information
generation of a OAS-TL A mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview. The incorporation of sulfur into thiols but not thiol steady-state levels is decreased in mutants lacking cytosolic OAS-TL A
additional information
generation of a OAS-TL A mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview. The incorporation of sulfur into thiols but not thiol steady-state levels is decreased in mutants lacking cytosolic OAS-TL A
additional information
-
knockout of the most abundant cytosolic OAS-TL isoforms oas-a1.1 and osa-a1.2. Total intracellular Cys and glutathione concentrations are reduced, and the glutathione redox state is shifted in favor of its oxidized form. The capability of the mutants to chelate heavy metals does not differ from that of the wild type, but the mutants have an enhanced sensitivity to cadmium. The oas-a1.1 mutant plants are oxidatively stressed, H2O2 production is localized in shoots and roots, spontaneous cell death lesions occur in the leaves, and lignification and guaiacol peroxidase activity are significantly increased
additional information
-
null alleles of cytosolic isoform oas-tl A or plastid isoform oas-tl B alone show that cytosolic OAS-TL A and plastid OAS-TL B are completely dispensable, although together they contribute 95% of total OAS-TL activity. An oas-tl AB double mutant, relying solely on mitochondrial OAS-TL C for Cys synthesis, shows 25% growth retardation. Although OAS-TL C alone is sufficient for full development, oas-tl C plants also show retarded growth
additional information
direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis and enhance cysteine rduction. Several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for serine acetyltransferase binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation. Transgenic Arabidopsis lines with PEP4 expression show moderate changes in SAT and OAS-TL activities
additional information
-
direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis and enhance cysteine rduction. Several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for serine acetyltransferase binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation. Transgenic Arabidopsis lines with PEP4 expression show moderate changes in SAT and OAS-TL activities
additional information
generation of a OAS-TL B mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview
additional information
generation of a OAS-TL B mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview
additional information
generation of a OAS-TL B mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview
additional information
generation of a OAS-TL C mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview. Lack of mitochondrial OAS-TL C diminishes the incorporation of OAS into thiols without affecting thiol steady-state levels
additional information
generation of a OAS-TL C mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview. Lack of mitochondrial OAS-TL C diminishes the incorporation of OAS into thiols without affecting thiol steady-state levels
additional information
generation of a OAS-TL C mutant by T-DNA insertion. Generation major isozyme OAS-TL double loss-of-function mutants oastlBC A+/+, oastlAC B+/+, and oastlAB C+/+, leaving only one major OAS-TL in the cytosol, in the plastids, and in the mitochondria, respectively. Extractable OAS-TL activity is not altered in the oastlBC A+/+ mutant compared with the wild-type, while OAS-TL activities are decreased to 30% and 3% in the oastlAC B+/+ and oastlAB C+/+ mutants, respectively. Phenotypes, overview. Lack of mitochondrial OAS-TL C diminishes the incorporation of OAS into thiols without affecting thiol steady-state levels
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Droux, M.; Ruffet, M.L.; Douce, R.; Job, D.
Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants. Structural and kinetic properties of the free and bound enzymes
Eur. J. Biochem.
255
235-245
1998
Arabidopsis thaliana
brenda
Noji, M.; Saito, K.
Molecular and biochemical analysis of serine acetyltransferase and cysteine synthase towards sulfur metabolic engineering in plants
Amino Acids
22
231-243
2002
Arabidopsis thaliana, Spinacia oleracea, Triticum aestivum, Zea mays
brenda
Hell, R.; Bork, C.; Bogdanova, N.; Frolov, I.; Hauschild, R.
Isolation and characterization of two cDNAs encoding for compartment specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis thaliana
FEBS Lett.
351
257-262
1994
Arabidopsis thaliana
brenda
Romero, L.C.; Dominguez-Solis, J.R.; Gutierrez-Alcala, G.; Gotor, C.
Salt regulation of O-acetylserine(thiol)lyase in Arabidopsis thaliana and increased tolerance in yeast
Plant Physiol. Biochem.
39
643-647
2001
Arabidopsis thaliana
-
brenda
Mino, K.; Ishikawa, K.
Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1
J. Bacteriol.
185
2277-2284
2003
Aeropyrum pernix, Arabidopsis thaliana
brenda
Bonner, E.R.; Cahoon, R.E.; Knapke, S.M.; Jez, J.M.
Molecular basis of cysteine biosynthesis in plants: Structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana
J. Biol. Chem.
280
38803-38813
2005
Arabidopsis thaliana
brenda
Wirtz, M.; Droux, M.; Hell, R.
O-acetylserine (thiol) lyase: an enigmatic enzyme of plant cysteine biosynthesis revisited in Arabidopsis thaliana
J. Exp. Bot.
55
1785-1798
2004
Arabidopsis thaliana
brenda
Kumaran, S.; Jez, J.M.
Thermodynamics of the interaction between O-acetylserine sulfhydrylase and the C-terminus of serine acetyltransferase
Biochemistry
46
5586-5594
2007
Arabidopsis thaliana
brenda
Francois, J.A.; Kumaran, S.; Jez, J.M.
Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex
Plant Cell
18
3647-3655
2006
Arabidopsis thaliana
brenda
Feldman-Salit, A.; Wirtz, M.; Hell, R.; Wade, R.C.
A mechanistic model of the cysteine synthase complex
J. Mol. Biol.
386
37-59
2009
Escherichia coli (P16703), Escherichia coli, Arabidopsis thaliana (P47998), Arabidopsis thaliana
brenda
Heeg, C.; Kruse, C.; Jost, R.; Gutensohn, M.; Ruppert, T.; Wirtz, M.; Hell, R.
Analysis of the Arabidopsis O-acetylserine(thiol)lyase gene family demonstrates compartment-specific differences in the regulation of cysteine synthesis
Plant Cell
20
168-185
2008
Arabidopsis thaliana
brenda
Lopez-Martin, M.C.; Becana, M.; Romero, L.C.; Gotor, C.
Knocking out cytosolic cysteine synthesis compromises the antioxidant capacity of the cytosol to maintain discrete concentrations of hydrogen peroxide in Arabidopsis
Plant Physiol.
147
562-572
2008
Arabidopsis thaliana
brenda
Bermudez, M.A.; Paez-Ochoa, M.A.; Gotor, C.; Romero, L.C.
Arabidopsis S-sulfocysteine synthase activity is essential for chloroplast function and long-day light-dependent redox control
Plant Cell
22
403-416
2010
Arabidopsis thaliana
brenda
Wirtz, M.; Heeg, C.; Samami, A.A.; Ruppert, T.; Hell, R.
Enzymes of cysteine synthesis show extensive and conserved modifications patterns that include Nalpha-terminal acetylation
Amino Acids
39
1077-1086
2010
Arabidopsis thaliana
brenda
Shibagaki, N.; Grossman, A.R.
Binding of cysteine synthase to the STAS domain of sulfate transporter and its regulatory consequences
J. Biol. Chem.
285
25094-25102
2010
Arabidopsis thaliana
brenda
Alvarez, C.; Lozano-Juste, J.; Romero, L.C.; Garcia, I.; Gotor, C.; Leon, J.
Inhibition of Arabidopsis O-acetylserine(thiol)lyase A1 by tyrosine nitration
J. Biol. Chem.
286
578-586
2011
Arabidopsis thaliana
brenda
Wirtz, M.; Beard, K.F.; Lee, C.P.; Boltz, A.; Schwarzlaender, M.; Fuchs, C.; Meyer, A.J.; Heeg, C.; Sweetlove, L.J.; Ratcliffe, R.G.; Hell, R.
Mitochondrial cysteine synthase complex regulates O-acetylserine biosynthesis in plants
J. Biol. Chem.
287
27941-27947
2012
Arabidopsis thaliana
brenda
Bermudez, M.A.; Galmes, J.; Moreno, I.; Mullineaux, P.M.; Gotor, C.; Romero, L.C.
Photosynthetic adaptation to length of day is dependent on S-sulfocysteine synthase activity in the thylakoid lumen
Plant Physiol.
160
274-288
2012
Arabidopsis thaliana
brenda
Gotor, C.; Romero, L.C.
S-sulfocysteine synthase function in sensing chloroplast redox status
Plant Signal. Behav.
8
e23313
2013
Arabidopsis thaliana (O22682), Arabidopsis thaliana
brenda
Feldman-Salit, A.; Wirtz, M.; Lenherr, E.D.; Throm, C.; Hothorn, M.; Scheffzek, K.; Hell, R.; Wade, R.C.
Allosterically gated enzyme dynamics in the cysteine synthase complex regulate cysteine biosynthesis in Arabidopsis thaliana
Structure
20
292-302
2012
Arabidopsis thaliana
brenda
Campanini, B.; Benoni, R.; Bettati, S.; Beck, C.M.; Hayes, C.S.; Mozzarelli, A.
Moonlighting O-acetylserine sulfhydrylase: new functions for an old protein
Biochim. Biophys. Acta
1854
1184-1193
2015
Arabidopsis thaliana (P47998), Bacillus subtilis (P37887), Caenorhabditis elegans (Q93244), Entamoeba histolytica (Q401L7), Escherichia coli (P0ABK5), Escherichia coli, Glycine max (A3RM03), Haemophilus influenzae (P45040), Mycobacterium tuberculosis (P9WP55), Salmonella enterica subsp. enterica serovar Typhimurium (P0A1E3), Staphylococcus aureus
brenda
Tahir, J.; Watanabe, M.; Jing, H.; Hunter, D.; Tohge, T.; Nunes-Nesi, A.; Brotman, Y.; Fernie, A.; Hoefgen, R.; Dijkwel, P.
Activation of R-mediated innate immunity and disease susceptibility is affected by mutations in a cytosolic O-acetylserine (thiol) lyase in Arabidopsis
Plant J.
73
118-130
2013
Arabidopsis thaliana (P47998)
brenda
Birke, H.; Heeg, C.; Wirtz, M.; Hell, R.
Successful fertilization requires the presence of at least one major O-acetylserine(thiol)lyase for cysteine synthesis in pollen of Arabidopsis
Plant Physiol.
163
959-972
2013
Arabidopsis thaliana (P47998), Arabidopsis thaliana (P47999), Arabidopsis thaliana (Q43725)
brenda
Wawrzynska, A.; Kurzyk, A.; Mierzwinska, M.; Plochocka, D.; Wieczorek, G.; Sirko, A.
Direct targeting of Arabidopsis cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis
Plant Sci.
207
148-157
2013
Arabidopsis thaliana (Q43725), Arabidopsis thaliana
brenda
Mueller, S.M.; Wang, S.; Telman, W.; Liebthal, M.; Schnitzer, H.; Viehhauser, A.; Sticht, C.; Delatorre, C.; Wirtz, M.; Hell, R.; Dietz, K.J.
The redox-sensitive module of cyclophilin 20-3, 2-cysteine peroxiredoxin and cysteine synthase integrates sulfur metabolism and oxylipin signaling in the high light acclimation response
Plant J.
91
995-1014
2017
Arabidopsis thaliana (P47999)
brenda