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evolution
O-acetylserine sulfydrylase, a highly conserved pyridoxal 5'-phosphate-dependent enzyme, present in different isoforms in bacteria, plants, and nematodes, but absent in mammals
evolution
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the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
evolution
the enzyme belongs to the family of fold-type II PLP-dependent enzymes. The cyanobacterium Microcystis aeruginosa PCC 7806 encodes three putative OASSs: CAO86616, CAO86589 and CAO86970, sequence comparisons
evolution
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O-acetylserine sulfydrylase, a highly conserved pyridoxal 5'-phosphate-dependent enzyme, present in different isoforms in bacteria, plants, and nematodes, but absent in mammals
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malfunction
GmOASTL4 gene is overexpressed in tobacco. Transgenic plants show markedly increased accumulation of transcripts and higher cysteine content compared with the wild-type. Upon exposure to cadmium stress, OASTL activity and cysteine levels increase significantly in transgenic plants. Cadmium accumulation and the activity of both superoxide dismutase and catalase enzymes are enhanced in transformants
malfunction
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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
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transgenic Ipomoea aquatica plants, which simultaneously express two genes encoding serine acetyltransferase and cysteine synthase are created. Transgenic plants are shown to rapidly grow and to accumulate sulfate at a high level. Upon hydroponical cultivation in the presence of 200 mM cadmium for 7 days, two transgenic lines (SR1 and SR2) accumulate 2- to 4fold higher levels of cysteine and glutathione than the wild type control plants. When plantlets are exposed to 100 mM cadmium for 30 days, wild type and transgenic SR2 plantlets die, whereas transgenic SR1 exhibit a 1.7fold increase in total biomass in comparison with the initial weight at day-0 of cadmium treatment
malfunction
the inhibition of cysteine biosynthesis in prokaryotes and protozoa is proposed for the development of antibiotics
malfunction
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mutation of cysM causes increased sensitivity of Staphylococcus (S.) aureus to tellurite (15fold), hydrogen peroxide (45fold), acid (30fold after 4h at pH 2.0), and diamide (but not methyl viologen) and also significantly reduces the ability to recover from starvation in amino acid- or phosphate-limiting conditions. A cysM knockout mutant grows poorly in cysteine-limiting conditions
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
cysl-2 mutant phenotype, overview. The cysl-2 mutant has a reduced rate of enzymatic H2S synthesis from the added substrates L-cysteine and is marked by a decline in reproductive output compared to wild-type worms. Body area and length are significantly lower in cysl-2 compared to age-matched wild type worms, and GYY4137 treatment effectively rescues this phenotype. Lifespan is reduced in cysl-2 compared to wild-type and the addition of GYY4137 reverses this effect and increases the median survival of cysl-2
malfunction
deletion of the C-terminal Ile, or substitution with Ala or Glu, in CysE consistently impairs complex formation with CysK
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
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
malfunction
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mutation of cysM causes increased sensitivity of Staphylococcus (S.) aureus to tellurite (15fold), hydrogen peroxide (45fold), acid (30fold after 4h at pH 2.0), and diamide (but not methyl viologen) and also significantly reduces the ability to recover from starvation in amino acid- or phosphate-limiting conditions. A cysM knockout mutant grows poorly in cysteine-limiting conditions
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metabolism
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catalyzes the final step of the L-cysteine biosynthesis
metabolism
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key enzyme in the L-cysteine pathway
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
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key enzyme in the biosynthetic cysteine pathway
metabolism
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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 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 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 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 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 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 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 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 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 enzyme catalyzes the final reaction of cysteine biosynthesis. Biological roles of known CysK complexes in the context of cysteine metabolism, overview
metabolism
the enzyme catalyzes the last step of cysteine biosynthesis. Cysteine is a building block for several biomolecules that are crucial for living organisms
metabolism
the enzyme is part of the sulfur assimilatory de novo L-cysteine biosynthetic pathway, that is essential for various cellular activities, including the proliferation and anti-oxidative defense of Entamoeba histolytica
metabolism
the O-acetylserine sulfhydrylase catalyzes the final step of cysteine biosynthesis from O-acetylserine and inorganic sulfide, negative feedback regulation of the pathway. Autoinhibition by cystine might be a universal mechanism of cysteine biosynthesis pathway
metabolism
the O-acetylserine sulfhydrylase catalyzes the final step of cysteine biosynthesis from O-acetylserine and inorganic sulfide, negative feedback regulation of the pathway. Autoinhibition by cystine might be a universal mechanism of cysteine biosynthesis pathway, redox-dependent autoregulation
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
metabolism
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key enzyme in the biosynthetic cysteine pathway
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metabolism
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the enzyme catalyzes the last step of cysteine biosynthesis. Cysteine is a building block for several biomolecules that are crucial for living organisms
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metabolism
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catalyzes the final step of the L-cysteine biosynthesis
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physiological function
cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL1 grow in the M9 minimal medium in the absence of cysteine
physiological function
cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL2 does not grow in the M9 minimal medium in the absence of cysteine
physiological function
cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL3 grow in the M9 minimal medium in the absence of cysteine
physiological function
cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL4 grow in the M9 minimal medium in the absence of cysteine
physiological function
cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL6 grow in the M9 minimal medium in the absence of cysteine
physiological function
cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL7 does not grow in the M9 minimal medium in the absence of cysteine
physiological function
product cysteine plays an important role in the antioxidative defense mechanisms of the human parasite
physiological function
activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction
physiological function
activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction
physiological function
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cysteine synthase complex CSC is comprised of the two enzymes that catalyze the final steps in cysteine biosynthesis: serine O-acetyltransferase, EC 2.3.1.30, which produces O-acetyl-L-serine, and O-acetyl-L-serine sulfhydrylase, EC 2.5.1.47, which converts it to cysteine. The system exhibits a contact-induced inactivation of half of each biomolecule, and exhibits a mechanism in which serine O-acetyltransferase interacts with O-acetyl-L-serine sulfhydrylase in a nonallosteric interaction involving its C-terminus. This early docking event appears to fasten the proteins in close proximity. The complex passes through at least three stable conformations in achieving its most stable configuration. Binding of a serine O-acetyltransferase C-terminal peptide is monophasic, and binding at one O-acetyl-L-serine sulfhydrylase active site does not prevent, or otherwise influence, binding at the second. The rate constants governing the first phase of the serine O-acetyltransferase binding reaction are remarkably similar to those for the binding of peptide, suggesting that early docking of serine O-acetyltransferase occurs primarily through the its C-terminus. The inability of the peptide to either induce isomerization or close the distal site suggests that serine O-acetyltransferase structure beyond its C-terminus is required to engage in isomerization and that closure of the unoccupied O-acetyl-L-serine sulfhydrylase active site may be coupled to the one or more isomerizations
physiological function
enzyme is able to complement the cysteine auxotrophy of an Escherichia coli cysMK mutant
physiological function
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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
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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
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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
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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
beside the biosynthesis of cysteine, enzyme OASS exerts a series of moonlighting activities in bacteria, such as transcriptional regulation, contact-dependent growth inhibition, swarming motility, and induction of antibiotic resistance
physiological function
besides a role of OAST-A1 in cysteine biosynthesis, the enzyme is involved in regulation of plant immunity
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
CysK influences transcription in Caenorhabditis elegans. The enzyme from Caenorhabditis elegans interacts with EGL-9 in regulation of O2-dependent behavioral plasticity
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
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
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
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
physiological function
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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. CysK influences transcription in Gram-positive bacteria. The enzyme from Staphylococcus aureus interacts with CymR in transcription repression
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
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. Productive cysteine biosynthesis requires a high CysK to CysE ratio
physiological function
enzyme CysK is organized in a complex with serine acetyltransferase (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. CysK also activates an antibacterial nuclease toxin produced by uropathogenic Escherichia coli. Role for CysK during bacterial contact-dependent growth inhibition involving the CDI system from uropathogenic Escherichi coli, overview. CysK-binding provides a mechanism to protect the bacterial CysE from cold-inactivation and proteolysis. Escherichia coli CysK acts as a so-called permissive factor to activate an antibacterial contact-dependent growth inhibition (CDI) toxin, and interacts with CdiA-CTUPEC536 in toxin activation
physiological function
enzyme CysK is organized in a complex with serine acetyltransferase (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. CysK influences transcription in Gram-positive bacteria. In Bacillus subtilis, CysK modulates the affinity of an Rrf2-type transcription factor for its operator sequences, thereby regulating expression of the cysteine regulon. The enzyme from Bacillus subtilis interacts with CymR in transcription repression. CdiA-CT toxins are activated by CysK, also from other species
physiological function
O-acetylserine sulfhydrylase plays a key role in the adaptation of bacteria to the host environment, in the defense mechanisms to oxidative stress and in antibiotic resistance
physiological function
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occurrence of the regulatory cysteine synthase complex in microalgae. In plants and also in bacteria, enzyme OASTL is catalytically inactive in the cysteine synthase complex but becomes fully active upon dissociation from the complex realized by O-acetylserine
physiological function
the bifunctional enzyme, encoded by gene K10H10.2, or cysl-2, shows cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9. It has been described as a hypoxia inducible factor (HIF) target. The enzyme regulates the mRNA expression of aging-associated and stress-related genes in wild-type Caenorhabditis elegans. Enzyme treatment protects the wild-type nematodes against oxidative, endoplasmic reticulum stress, and thermal stressors but not cadmium-induced metallic stress. The enzyme is active in vitro and in vivo and protects against lipopolysaccharide-induced inflammation. GYY4137 induces longevity and stress resistance, mechanism of action via induction of T24B8.5 and altered transcriptional control of SKN-1
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
tree legume Leucaena contains a toxic, nonprotein amino acid, mimosine, which is not formed by the enzyme O-acetylserine (thiol) lyase, OAS-TL
physiological function
upregulation of cysteine synthase and cystathionine beta-synthase contributes to Leishmania braziliensis survival under oxidative stress. Ability of Leishmania braziliensis promastigotes and amastigotes overexpressing the enzyme to resist oxidative stress, which is significantly enhanced compared to that of nontransfected cells, resulting in a phenotype far more resistant to treatment with the pentavalent form of sodium stibogluconate in vitro
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
physiological function
knockout of OASTL-A1 leads to significantly lower levels of cysteine, glutathione, and phytochelatins in roots and increased sensitivity to arsenate stress. The knockout reduces As accumulation in the roots, but increases As accumulation in shoots. OASTL-A1 is able to complement an Escherichia coli cysteine synthase-deficient mutant
physiological function
over-expression of CS1 in Arabidopsis results in the enhanced biosynthesis of glutathione, which allows plants to tolerate cadmium stress
physiological function
overexpression of cysteine synthase in amphotericin B (Amp B) sensitive strain S1-OE modulates resistance towards oxidative stress and drug pressure. Antioxidant enzyme activities are upregulated in S1-OE parasites and these parasites alleviate intracellular reactive oxygen species efficiently by maintaining the reduced thiol pool. The Amp B sensitive strain shows higher levels of reactive oxygen species which is positively correlated with the protein carbonylation levels and negatively correlated with cell viability. Cysteine synthase overexpression also augments the ROS-primed induction of cysteine synthase-GFP as well as endogenous cysteine synthase and thiol pathway proteins in Leishmania donovani parasites. The expression of cysteine synthase is upregulated in Amp B resistant isolates and during infective stationary stages of growth. Cysteine synthase overexpression enhances the infectivity of Leishmania donovani parasites
physiological function
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overexpression of OASS does not affect the nodule number, but negatively impacts plant growth. Levels of cysteine, glutathione, and homoglutathione nearly double in OASS overexpressing nodules when compared to control nodules. Several metabolites related to serine, aspartate, glutamate, and branched-chain amino acid pathways are significantly elevated in OASS overexpressing nodules. Flavonoid levels of the OASS overexpressing nodules are mostly reduced
physiological function
parental infection by Pseudomonas vranovensis results in increased expression of the cysteine synthases CysL-1 and CysL-2 and the regulator of hypoxia inducible factor Rhy-1 in progeny, and these three genes are required for adaptation to Pseudomonas vranovensis
physiological function
serine acetyltransferase CysE is activated when bound to O-acetylserine sulfhydrylase CysK. CysE activation results from the release of substrate inhibition. Feedback inhibition of CysE by L-Cys is also relieved in the bacterial cysteine synthase complex
physiological function
the binding interaction of CdiA-CT toxin from uropathogenic Escherichia coli 536 with CysK mimics the cysteine synthase complex of CysK:CysE. The C-terminal tails of CysE and CdiA-CT each insert into the CysK active-site cleft to anchor the respective complexes. The dissociation constant for CysK:CdiA-CT is comparable to that of the Escherichia coli cysteine synthase complex, and both complexes bind through a two-step mechanism with a slow isomerization phase after the initial encounter. CdiA-CT can effectively displace CysE from pre-formed cysteine synthase complexes, enabling toxin activation even in the presence of excess competing CysE
physiological function
when expressed in tobacco plants, total O-acetylserine(thiol)lyase activity in tobacco leaves is reduced. Isoform CSaseLP binds to isoform CSaseA. The O-acetylserine(thiol)lyase activity of the copurified CSaseA is reduced compared with the activity of CSaseA that is purified on its own, CSaseLP negatively regulates cysteine biosynthesis in tobacco plants
physiological function
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upregulation of cysteine synthase and cystathionine beta-synthase contributes to Leishmania braziliensis survival under oxidative stress. Ability of Leishmania braziliensis promastigotes and amastigotes overexpressing the enzyme to resist oxidative stress, which is significantly enhanced compared to that of nontransfected cells, resulting in a phenotype far more resistant to treatment with the pentavalent form of sodium stibogluconate in vitro
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physiological function
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occurrence of the regulatory cysteine synthase complex in microalgae. In plants and also in bacteria, enzyme OASTL is catalytically inactive in the cysteine synthase complex but becomes fully active upon dissociation from the complex realized by O-acetylserine
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physiological function
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beside the biosynthesis of cysteine, enzyme OASS exerts a series of moonlighting activities in bacteria, such as transcriptional regulation, contact-dependent growth inhibition, swarming motility, and induction of antibiotic resistance
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physiological function
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serine acetyltransferase CysE is activated when bound to O-acetylserine sulfhydrylase CysK. CysE activation results from the release of substrate inhibition. Feedback inhibition of CysE by L-Cys is also relieved in the bacterial cysteine synthase complex
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physiological function
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the binding interaction of CdiA-CT toxin from uropathogenic Escherichia coli 536 with CysK mimics the cysteine synthase complex of CysK:CysE. The C-terminal tails of CysE and CdiA-CT each insert into the CysK active-site cleft to anchor the respective complexes. The dissociation constant for CysK:CdiA-CT is comparable to that of the Escherichia coli cysteine synthase complex, and both complexes bind through a two-step mechanism with a slow isomerization phase after the initial encounter. CdiA-CT can effectively displace CysE from pre-formed cysteine synthase complexes, enabling toxin activation even in the presence of excess competing CysE
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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
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
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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
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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
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
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
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
additional information
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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
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
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
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
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, the C-terminal Ile (residue P4) is fundamental for the CysE/CysK binding interaction
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. The P4 Ile residue accounts for about 80% of total binding energy. The P2 and P3 positions account for about 10% each, and the P1 residue negatively impacts binding, interaction analysis
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. The P4 Ile residue accounts for about 80% of total binding energy. The P2 and P3 positions account for about 10% each, and the P1 residue negatively impacts binding, interaction analysis. No negative cooperativity
additional information
enzyme structure homology modeling, three-dimensional structure, overview
additional information
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intramolecular electrostatic interaction of enzyme OASS-B, overview
additional information
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the enzyme has a CBS-ike structure and a Rhodanese homology domain in the C-terminus, structure homology modeling
additional information
three-dimensional structure comparisons of isozymes CysK1 and CysK2, overview
additional information
three-dimensional structure comparisons of isozymes CysK1 and CysK2, overview
additional information
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three-dimensional structure comparisons of isozymes CysK1 and CysK2, overview
additional information
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intramolecular electrostatic interaction of enzyme OASS-B, overview
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