2.5.1.47: cysteine synthase
This is an abbreviated version!
For detailed information about cysteine synthase, go to the full flat file.
Word Map on EC 2.5.1.47
-
2.5.1.47
-
h2s
-
sulfur
-
l-cysteine
-
gsh
-
gamma-glutamyl
-
acetyltransferase
-
pyridoxal
-
slow-releasing
-
typhimurium
-
5'-phosphate
-
gasotransmitter
-
o-acetylserinethiollyase
-
nahs
-
sulfite
-
gaseous
-
schiff
-
buthionine
-
sulfoximine
-
phytochelatins
-
assimilatory
-
plp-dependent
-
desulfhydrase
-
h2s-releasing
-
alpha-aminoacrylate
-
thiosulfate
-
oxygenase-1
-
gamma-gcs
-
sulphide
-
dl-propargylglycine
-
transsulfuration
-
bienzyme
-
3-mercaptopyruvate
-
5'-phosphate-dependent
-
beta-synthase
-
h2s-producing
-
sulfurylase
-
aldimine
-
beta-replacement
-
gamma-lyase
-
sulfurtransferase
-
cysb
-
hydrosulfide
-
biotechnology
-
agriculture
-
synthesis
-
pharmacology
-
medicine
-
environmental protection
-
drug development
-
analysis
- 2.5.1.47
- h2s
- sulfur
- l-cysteine
- gsh
-
gamma-glutamyl
- acetyltransferase
- pyridoxal
-
slow-releasing
- typhimurium
- 5'-phosphate
-
gasotransmitter
-
o-acetylserinethiollyase
- nahs
- sulfite
-
gaseous
-
schiff
-
buthionine
- sulfoximine
- phytochelatins
-
assimilatory
-
plp-dependent
- desulfhydrase
-
h2s-releasing
- alpha-aminoacrylate
- thiosulfate
- oxygenase-1
- gamma-gcs
- sulphide
- dl-propargylglycine
-
transsulfuration
-
bienzyme
- 3-mercaptopyruvate
-
5'-phosphate-dependent
- beta-synthase
-
h2s-producing
-
sulfurylase
-
aldimine
-
beta-replacement
-
gamma-lyase
- sulfurtransferase
- cysb
- hydrosulfide
- biotechnology
- agriculture
- synthesis
- pharmacology
- medicine
- environmental protection
- drug development
- analysis
Reaction
Synonyms
(OAS-TL)-like protein, acetylserine sulfhydrylase, At-OASS, ATCC 23270 protein, BAbS19_I09950, beta-cyano-alanine synthase, beta-cyano-L-alanine synthase, CS-A, CS-B, CS1, CS26, CS3, CSase, CSase A, CSase B, CSaseLP, CSC, Cys synthase complex, cysK, CysK1, CysK2, CYSL, CysL-1, cysl-2, CysM, Cysteine synthase, cysteine synthase 1, cysteine synthase A, cysteine synthase B, cysteine synthase, chloroplastic/chromoplastic, cysteine synthase, mitochondrial, cysteine synthetase, DcsD, EC 4.2.99.8, EhCS, EhCS1, EhCS3, EhOASS, Fn1220, GmOAS-TL1, GmOAS-TL2, GmOAS-TL3, GmOAS-TL4, GmOAS-TL6, GmOAS-TL7, GmOASTL4, GsOAS-TL1, GYY4137, HiOASS, HiOASS-A, lanthionine synthase, LbrCS, MCSA1, Nt-OAS-TL, O -acetylserine (thiol)-lyase, O-acetyl-L-serine (thiol) lyase, O-acetyl-L-serine acetate-lyase (adding hydrogen sulfide), O-acetyl-L-serine sulfhydrylase, O-acetyl-L-serine sulfhydrylase B, O-acetyl-L-serine sulfohydrolase, O-acetyl-L-serine(thiol)lyase, O-acetyl-serine (thiol) lyase, O-acetylserine (thiol) lyase, O-acetylserine (Thiol)-lyase, O-acetylserine (thiol)-lyase A, O-acetylserine (thiol)-lyase B, O-acetylserine (thiol)lyase, O-acetylserine sulfhydrylase, O-acetylserine sulfhydrylase A, O-acetylserine sulfhydrylase B, O-acetylserine sulfhydrylase isoenzyme B, O-acetylserine sulfhydrylase-A, O-acetylserine sulfhydrylase-B, O-acetylserine thiol lyase, O-acetylserine(thiol)lyase, O-acetylserine-(thiol)lyase, O-acetylserine-O-acetylhomoserine sulfhydro-lyase, O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase, OAS Shase, OAS thiol-lyases, OAS-TL, OAS-TL A, OAS-TL B, OAS-TL C, OASA1, OASB, OASS, OASS-A, OASS-B, OASTL, OASTL-A, OASTL-A1, old3-1, OPSS, Os01g0290600, Os03g53650, protein ONSET OF LEAF DEATH 3, RCS3, S-sulfocysteine synthase, SSC synthase, StOASTL A, StOASTL B, sulfhydrylase/cysteine synthase, synthase, cysteine, TvCS1
ECTree
2.5.1.47 cysteine synthaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.5.1.47 - cysteine synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H150A
-
in contrast to the wild-type protein the mutant protein is colorless after purification, and UV-Vis scanning of the mutant proteins show that there are no absorptions between 300 and 500 nm, mutant protein does not show a comparable activity to the wild-type protein. This suggests that the mutated residue is crucial or pyridoxal 5'-phosphate binding and stabilization
H168A
-
in contrast to the wild-type protein the mutant protein is colorless after purification, and UV-Vis scanning of the mutant proteins show that there are no absorptions between 300 and 500 nm, mutant protein does not show a comparable activity to the wild-type protein. This suggests that the mutated residue is crucial or pyridoxal 5'-phosphate binding and stabilization
K30A
-
in contrast to the wild-type protein the mutant protein is colorless after purification, and UV-Vis scanning of the mutant proteins show that there are no absorptions between 300 and 500 nm, mutant protein does not show a comparable activity to the wild-type protein. This suggests that the mutated residue is crucial or pyridoxal 5'-phosphate binding and stabilization
K41A
-
mutant protein is also colourful as the wild-type protein, mutant protein does not show the same activity as the wild-type protein
K127A
mutant is inactive for cysteine synthesis and does not form the alpha-aminoacrylate intermediate
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)
Q147A
S75A
S75T
T74S
Q96A/Y125A
F143A
-
mutant retains one molecule of pyridoxal 5'-phosphate per subunit, mutant reacts with O-acetylserine but the rate is significantly smaller, kcat/KM (O-acetylserine): 950/Msec
F143D
-
mutant retains one molecule of pyridoxal 5'-phosphate per subunit, mutant reacts with O-acetylserine but the rate is significantly smaller, kcat/KM (O-acetylserine): 150/Msec
F143S
-
mutant retains one molecule of pyridoxal 5'-phosphate per subunit, mutant reacts with O-acetylserine but the rate is significantly smaller, kcat/KM (O-acetylserine): 380/Msec
F143Y
-
mutant retains one molecule of pyridoxal 5'-phosphate per subunit, reaction with O-acetylserine is inhibited
Q142A
-
ability of pyridoxal 5'-phosphate binding is not altered, mutant does not react with O-acetylserine
Q240A
-
ratio kcat to Km value is 0.4% of wild-type, increase in temperature dependence factors, corresponding to an appreciable increase in the activation energy
T68A
-
ratio kcat to Km value is 0.1% of wild-type, increase in temperature dependence factors, corresponding to an appreciable increase in the activation energy
A70S
residue at the substrate binding pocket, important for the H2S-generating activity
E223G
residue at the substrate binding pocket, important for the H2S-generating activity
A70S
Lactiplantibacillus plantarum ATCC BAA-793
-
residue at the substrate binding pocket, important for the H2S-generating activity
-
E223G
Lactiplantibacillus plantarum ATCC BAA-793
-
residue at the substrate binding pocket, important for the H2S-generating activity
-
DELTAE115-K118
-
mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
K118A
-
mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
K221A/P222E/G223E/P224E
-
mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
W162A
-
mutation increases the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
Y188A
-
mutation increases the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
DELTAE115-K118
-
mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
-
K118A
-
mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
-
K221A/P222E/G223E/P224E
-
mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
-
W162A
-
mutation increases the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
-
Y188A
-
mutation increases the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
-
N71A
mutant exhibits formation of the alpha-aminoacrylate intermediate, but the rate constant for its formation from the external Schiff base is decreased by 1 order of magnitude compared to that of the wild type
Q142A
mutant is unable to form the alpha-aminoacrylate intermediate but produces pyruvate at a rate much greater than that of the wild-type enzyme
S69A
mutant exhibits formation of the alpha-aminoacrylate intermediate, but the rate constant for its formation from the external Schiff base is decreased by 1 order of magnitude compared to that of the wild type
T68A
mutant is unable to form the alpha-aminoacrylate intermediate but produces pyruvate at a rate much greater than that of the wild-type enzyme
H152A
K120Q
R186L
-
retains one cofactor per subunit, accelerates the reaction with substrate O3-acetyl-L-serine 1.8fold, intermediates are formed faster by 1.5 and 1.3fold, respectively, with azide or thiosulfate than in the wild type
R186P
-
loss of cofactor leads to enzyme inactivation
S272A
-
mutant enzyme catalyzes the overall reaction, first half-reaction is decreased by factor 3, the decrease in rate of elimination is compensated by an increase in affinity for O-acetyl-L-Ser
S272D
-
mutant enzyme catalyzes the overall reaction
W161Y
-
2fold increase in Vmax and Km-value of O3-acetyl-L-serine
W50Y
-
no effect on catalytic rate or affinity of enzyme to first substrate, Km-value for 5-thio-2-nitrobenzoate decrease by 2.7fold
H152A
K120Q
K43A
mutation in invariant Lys43 residue, inactive. Mutant forms an external aldimine adduct upon addition of L-methionine or O-ureido-L-serine
S121A
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
S121M
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
V74T
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
Y97F
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
Y97M
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
K43A
-
mutation in invariant Lys43 residue, inactive. Mutant forms an external aldimine adduct upon addition of L-methionine or O-ureido-L-serine
-
S121A
-
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
-
V74T
-
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
-
Y97F
-
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
-
Y97M
-
decreased activity for synthesis of ureido-L-serine, increased activity for synthesis of L-cysteine
-
K214A
-
mutant retains high activity with O-acetylserine and sulfide (40% of the activity of the wild type enzyme), but its activity with O-phosphoserine and sulfide is reduced by more than 100fold. The ability to use thiosulfate as an alternative nucleophile in the sulfhydrylase reaction is greatly reduced, but the mutant shows no change in cysteine desulfurase activity
K43A
-
protein is yellow, indicating that it binds pyridoxal 5'-phosphate but has no detectable activity as a cysteine synthase with O-acetylserine or O-phosphoserine and no detectable cysteine desulfurase activity
additional information
Q147A
-
mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
S75A
-
mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
S75T
-
mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
T74S
-
mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
Q96A/Y125A
mutant shows relatively strong binding to serine acetyltransferase C-terminal peptides in comparison with native OASS. The mutant structure looks similar except that the active-site pocket has enough space to bind the serine acetyltransferase C-terminal end
Q96A/Y125A
-
mutant shows relatively strong binding to serine acetyltransferase C-terminal peptides in comparison with native OASS. The mutant structure looks similar except that the active-site pocket has enough space to bind the serine acetyltransferase C-terminal end
-
H152A
-
shift in the ketoenamine to enolimine tautomeric equilibrium toward the neutral enolimineine, the internal Schiff base of the free enzyme, the amino acid external Schiff base, and the alpha-aminoacrylate intermediate. The decreased rate of the mutant likely reflects a decrease in the amount of active enzyme as a result of an increased flexibility of the cofactor , which leads to increased rates of interconversion of the open and closed forms of the enzyme and additional interactions between the cofactor and enzyme in the closed form of the enzyme. Analysis of spectral properties
H152A
-
shift in the ketoeneamine to enolimine tautomeric equilibrium towards neutral enolimine in the internal Shiff base of the free enzyme, the amino acid external Schiff base, and the alpha-aminoacrylate intermediate, 2 enzyme conformers are present, decreased rate of the enzyme likely reflects a decrease in the amount of active enzyme as result of the increased cofactor flexibility which stabilizes the nonproductive binding of O3-acetyl-L-serine in the external Schiff base
K120Q
-
mutation results in a shift in the tautomeric equilibrium toward the neutral enolimine and an increase in the rate of interconversion of the open and closed forms of the enzyme. A decrease in the rate of both half reactions reflects the stabilization of the external Schiff base. Role of K120 in helping to stabilize the closed conformation of the enzyme by participating in a new bond to the backbone carbonyl of A231
K120Q
-
shift in the tautomeric equilibrium toward the neutral enolimine and an increase of the rate of interconversion of the open and closed forms of the enzyme, probably reflecting the stabilization of the external Schiff base
H152A
-
shift in the ketoenamine to enolimine tautomeric equilibrium toward the neutral enolimineine, the internal Schiff base of the free enzyme, the amino acid external Schiff base, and the alpha-aminoacrylate intermediate. The decreased rate of the mutant likely reflects a decrease in the amount of active enzyme as a result of an increased flexibility of the cofactor , which leads to increased rates of interconversion of the open and closed forms of the enzyme and additional interactions between the cofactor and enzyme in the closed form of the enzyme. Analysis of spectral properties
-
H152A
-
shift in the ketoeneamine to enolimine tautomeric equilibrium towards neutral enolimine in the internal Shiff base of the free enzyme, the amino acid external Schiff base, and the alpha-aminoacrylate intermediate, 2 enzyme conformers are present, decreased rate of the enzyme likely reflects a decrease in the amount of active enzyme as result of the increased cofactor flexibility which stabilizes the nonproductive binding of O3-acetyl-L-serine in the external Schiff base
-
K120Q
-
mutation results in a shift in the tautomeric equilibrium toward the neutral enolimine and an increase in the rate of interconversion of the open and closed forms of the enzyme. A decrease in the rate of both half reactions reflects the stabilization of the external Schiff base. Role of K120 in helping to stabilize the closed conformation of the enzyme by participating in a new bond to the backbone carbonyl of A231
-
K120Q
-
shift in the tautomeric equilibrium toward the neutral enolimine and an increase of the rate of interconversion of the open and closed forms of the enzyme, probably reflecting the stabilization of the external Schiff base
-
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
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
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 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
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
additional information
upon expression of the Arabidopsis thaliana 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 Arabidopsis thaliana 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
recombinant enzyme expressed in Escherichia coli does not show catalytic activity
additional information
-
recombinant enzyme expressed in Escherichia coli does not show catalytic activity
additional information
-
enzyme knockout mutant, grows poorly in cysteine-limiting conditions and produces significantly less cysteine than wild-type. Mutant shows increased sensitivity to tellurite, hydrogen peroxide, acid, and diamide. Mutant cells have a significantly reduced ability to recover from starvation in amino acid- or phosphate-limiting conditions
additional information
-
enzyme knockout mutant, grows poorly in cysteine-limiting conditions and produces significantly less cysteine than wild-type. Mutant shows increased sensitivity to tellurite, hydrogen peroxide, acid, and diamide. Mutant cells have a significantly reduced ability to recover from starvation in amino acid- or phosphate-limiting conditions
-
