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Enzyme Nomenclature
Information on EC 2.5.1.47 - cysteine synthase
for references in articles please use BRENDA:EC2.5.1.47
Word Map on EC 2.5.1.47
- 2.5.1.47
- sulfur
- h2s
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gamma-glutamyl
- thiols
- gsh
- l-cysteine
- pyridoxal
- typhimurium
- cystathionine
- 5'-phosphate
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slow-releasing
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buthionine
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schiff
- sulfoximine
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o-acetylserinethiollyase
- alpha-aminoacrylate
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gasotransmitter
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glutamyl
- nahs
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plp-dependent
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assimilatory
- phytochelatins
- gamma-gcs
- desulfhydrase
- sulphide
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beta-synthase
- hydrosulfide
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transsulfuration
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h2s-releasing
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aldimine
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5'-phosphate-dependent
- drug development
- dl-propargylglycine
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gamma-lyase
- synthesis
- medicine
- biotechnology
- pharmacology
- environmental protection
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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EC NUMBER 
COMMENTARY 
2.5.1.47
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RECOMMENDED NAME
GeneOntology No.
cysteine synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
mechanism of reverse reaction
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O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
mechanism similar to those of other pyridoxal enzymes
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O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
model of reaction mechanism
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O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
mechanism interpreted in structural context, conformational changes during catalysis
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O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
mechanism
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O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
identification and spectral characterization of the external aldimine of the reaction, mechanism
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O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
geometric model of reaction, comparison isoenzyme CysK
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
ping-pong bi-bi mechanism
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O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
ping-pong bi-bi mechanism
Escherichia coli W3110 / ATCC 27325
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O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
model of reaction mechanism
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O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-O bond cleavage
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elimination
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. Not identical with EC 2.5.1.51 (beta-pyrazolylalanine synthase), EC 2.5.1.52 (L-mimosine synthase) and EC 2.5.1.53 (uracilylalanine synthase).
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CAS REGISTRY NUMBER
COMMENTARY
37290-89-4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two isoenzymes, one with additional S-sulfocysteine synthase activity
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arginine, histidine or proline starvation leads to derepression of cysteine synthase activity. In addition to CysB, the activity is shared by homocysteine synthase CysD and at least one more enzyme, possibly CysF. Starvation-induced cysteine synthase activity is under control of cross-pathway regulation
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486766, 486775, 637364, 637385, 662427, 672256, 676429, 689472, 689625, 706226, 721262, 722680, 722737, 722770, 723475, 723782
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3 isoforms, recombinant enzymes, fast increase in enzyme product in response to sulfate deprivation
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aerobic form of enzyme forms a tight bienzyme complex in vivo with serine acetyltransferase
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low molecular weight enzyme is the same protein as serine sulfhydrylase
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637328, 637336, 637351, 637369, 637374, 637375, 637381, 637390, 637391, 637392, 672024, 701920, 707328
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; S-sulfocysteine synthase is identical with cysteine synthase B
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one enzyme free, one associated with serine transacetylase in cysteine synthase
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isozyme OASS-A
SwissProt
isozyme OASS-B
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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; 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
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
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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
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the CysK/CysE binding interaction is conserved in most bacterial and plant systems
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
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the CysK/CysE binding interaction is conserved in most bacterial and plant systems
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; 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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O-acetylserine sulfydrylase, a highly conserved pyridoxal 5'-phosphate-dependent enzyme, present in different isoforms in bacteria, plants, and nematodes, but absent in mammals; 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
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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
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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
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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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the inhibition of cysteine biosynthesis in prokaryotes and protozoa is proposed for the development of antibiotics
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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deletion of the C-terminal Ile, or substitution with Ala or Glu, in CysE consistently impairs complex formation with CysK
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
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; 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; 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
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
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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
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; 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 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
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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
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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
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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
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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 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; 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 enzyme catalyzes the last step of cysteine biosynthesis. Cysteine is a building block for several biomolecules that are crucial for living organisms; 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 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; 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; 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
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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the enzyme catalyzes the last step of cysteine biosynthesis. Cysteine is a building block for several biomolecules that are crucial for living organisms; 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
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product cysteine plays an important role in the antioxidative defense mechanisms of the human parasite
physiological function
cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL1 grow in the M9 minimal medium in the absence of cysteine; cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL2 does not grow in the M9 minimal medium in the absence of cysteine; cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL3 grow in the M9 minimal medium in the absence of cysteine; cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL4 grow in the M9 minimal medium in the absence of cysteine; cysteine auxotrophic mutant Escherichia coli NK3 transformed with GmOAS-TL6 grow in the M9 minimal medium in the absence of cysteine; 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
enzyme is able to complement the cysteine auxotrophy of an Escherichia coli cysMK mutant
physiological function
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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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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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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
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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
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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
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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
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
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
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
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), 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
CysK influences transcription in Caenorhabditis elegans. The enzyme from Caenorhabditis elegans interacts with EGL-9 in regulation of O2-dependent behavioral plasticity
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
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) 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
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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
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
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
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; 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
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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
besides a role of OAST-A1 in cysteine biosynthesis, the enzyme is involved in regulation of plant immunity
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; 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; 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
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 protein–protein 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
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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; 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
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
-
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
-
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
-
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; 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
-
additional information
-
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; three-dimensional structure comparisons of isozymes CysK1 and CysK2, overview
additional information
three-dimensional structure comparisons of isozymes CysK1 and CysK2, overview; three-dimensional structure comparisons of isozymes CysK1 and CysK2, overview
additional information
-
three-dimensional structure comparisons of isozymes CysK1 and CysK2, overview; three-dimensional structure comparisons of isozymes CysK1 and CysK2, overview
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
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. 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
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. 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
-
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
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
enzyme structure homology modeling, three-dimensional structure, overview
additional information
-
intramolecular electrostatic interaction of enzyme OASS-B, overview
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
Escherichia coli W3110 / ATCC 27325
-
intramolecular electrostatic interaction of enzyme OASS-B, overview
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-chloro-L-alanine + NaHS
L-cysteine + ?
-
beta-replacement reaction, enzyme can be induced by 3-chloro-L-alanine
-
?
5-thio-2-nitrobenzoate + O-acetyl-L-serine
acetate + ?
-
-
-
-
?
L-Cys + acetate
?
-
involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear
-
-
-
L-homoserine + sulfide
?
-
1.6% of the activity with O-acetyl-L-serine
-
-
?
O-acetyl-L-Ser + 5-mercapto-2-nitrobenzoate
S-(3-carboxy-4-nitrophenyl)-L-cysteine + ?
-
-
-
?
O-acetyl-L-serine + sulfide
L-Cys + acetate
-
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate + H+
-
-
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + sodium acetate
-
-
-
-
?
O-acetyl-Ser + selenide
selenocysteine + acetate
-
maximal 40% rate of cysteine synthesis
-
?
O3-acetyl-L-serine
alpha-aminoacrylate
-
-
in absence of S2- and at 50°C, not below
-
?
O3-acetyl-L-serine + benzylmercaptan
S-benzyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + cyanide
beta-cyano-L-alanine + acetate
-
-
-
?
O3-acetyl-L-serine + ethylmercaptan
S-ethyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + methylmercaptan
S-methyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + phenol
O-phenyl-L-serine + acetate
-
-
-
?
O3-acetyl-L-serine + phenylmercaptan
S-phenyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + propylmercaptan
S-propyl-L-cysteine + acetate
-
-
-
?
chloroalanine + sulfide
cysteine + chloride
-
3-6% of the activity of the cysteine synthase reaction
-
r
chloroalanine + sulfide
cysteine + chloride
-
beta-chloroalanine, 6% of the activity with O-acetyl-L-Ser
-
-
r
chloroalanine + sulfide
cysteine + chloride
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
beta-chloroalanine, 6% of the activity with O-acetyl-L-Ser
-
-
r
cysteine + CN-
cyanoalanine + H2S
Xanthium pennsylvanicum
-
involved in cyanide metabolism during seed germination
-
-
-
L-Cys + acetate
O-acetyl-L-Ser + H2S
-
-
-
r
L-Cys + acetate
O-acetyl-L-Ser + H2S
-
equilibrium constant
-
r
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
the side reaction of the enzyme seems to contribute massively to the total H2S release of higher plants at least at higher pH values
-
-
-
NaN3 + O-acetyl-Ser
beta-azidoalanine + sodium acetate
-
-
mutagenic
?
NaN3 + O-acetyl-Ser
beta-azidoalanine + sodium acetate
-
-
mutagenic in Salmonella typhimurium
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
18% of activity with sulfide
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
6.2% of the activity with sulfide, isoenzyme 2
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
2.6% and 6.8% of the activity with sulfide, isoenzyme 1 and 2, respectively
-
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
18% of activity with sulfide
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
enzyme that catalyzes the final step in cysteine biosynthesis. Cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
Entamoeba histolytica, the causative agent of human amoebiasis, is essentially anaerobic, requiring a small amount of oxygen for growth. It cannot tolerate the higher concentration of oxygen present in human tissues or blood. However, during tissue invasion it is exposed to a higher level of oxygen, leading to oxygen stress. Cysteine, which is a vital thiol in Entamoeba histolytica, plays an essential role in its oxygen-defence mechanisms. The major route of cysteine biosynthesis in this parasite is the condensation of O-acetylserine with sulfide by the de novo cysteine-biosynthetic pathway, which involves cysteine synthase (EhCS) as a key enzyme
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
yeast two-hybrid system for screening of a cDNA library of Nicotiana plumbaginifolia for clones encoding plant proteins interacting with two proteins of Escherichia coli: serine acetyltransferase (SAT, the product of cysE gene) and O-acetylserine (thiol) lyase A, also termed cysteine synthase (OASTL-A, the product of cysK gene). Two plant cDNA clones are identified when using the cysE gene as a bait
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
equilibrium constant
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
the second half of the OASS-A reaction is limited by the conformational change needed to open the active site and release the amino acid product. No quinonoid or geminal-diamine intermediates are detected. The amino acid external Schiff base of the enzyme is found to be very stable when the reaction is run in D2O
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
OASTL activity regulates not only Cys de novo synthesis but also its homeostasis
-
-
?
O-acetyl-L-Ser + isoxazylin-5-one
?
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
-
O-acetyl-L-Ser + isoxazylin-5-one
?
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
-
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
6.1% of activity with sulfide
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
2.2% of activity with sulfide, isoenzyme 1 and 2
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
2.3% and 1.6% of activity with sulfide, isoenzymes 1 and 2, respectively
-
-
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
2.5% of activity with sulfide
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
21.5% and 77% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
-
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
4% and 1% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
-
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
product identification uncertain
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
32% of activity with sulfide
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
6.84% and 7.64% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
12.3% of activity with sulfide
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
the cysteine synthase complex functions as a molecular sensor system that monitors the sulfur status of the cell and controls sulfate assimilation and cysteine synthesis according to the availability of sulfate
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in synthesis of antioxidants such as glutathione during fruit development
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
activity varies between sulfur sources, enzyme formation regulated by L-Cys concentration
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in glutathione formation
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
controlled by feedback inhibition, adaptively significant as sulfide removal mechanism
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
repressed during growth with sulfide or thiosulfide as sulfur source
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
key role in metabolism of S-containing amino acids
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
functions as a Cys synthase rather than as a homocysteine synthase in vivo
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
enzyme transcription repressed by L-cystine, derepressed by limiting sulfide concentrations
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in thiosulfate assimilation
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + thiosulfate
S-sulfocysteine + sodium acetate
-
-
-
?
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
residue Arg210 near the entrance of the active site and is important for O-acetyl-L-serine substrate recognition
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
Escherichia coli W3110 / ATCC 27325
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
Escherichia coli W3110 / ATCC 27325
-
residue Arg210 near the entrance of the active site and is important for O-acetyl-L-serine substrate recognition
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate. The enzyme catalyzes the reaction with O-acetyl-L-serine and hydroxyurea with 80fold lower catalytic efficiency
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate. The enzyme catalyzes the reaction with O-acetyl-L-serine and hydroxyurea with 80fold lower catalytic efficiency
-
-
?
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetylhomoserine + H2S
homocysteine + ?
-
not, low molecular weight enzyme
-
-
-
O-acetylhomoserine + H2S
homocysteine + ?
-
2.4% of the activity with O-acetyl-L-Ser
-
-
?
O-acetylhomoserine + H2S
homocysteine + ?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
2.4% of the activity with O-acetyl-L-Ser
-
-
?
O-diazoacetyl-L-serine + sulfide
?
-
44% of the activity with O-acetyl-Ser
-
-
?
O-diazoacetyl-L-serine + sulfide
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
44% of the activity with O-acetyl-Ser
-
-
?
O-succinyl-L-homoserine + sulfide
?
-
3.6% of the activity with O-acetyl-L-serine
-
-
?
O-succinyl-L-homoserine + sulfide
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
3.6% of the activity with O-acetyl-L-serine
-
-
?
O3-acetyl-L-serine + 2-nitro-5-thiobenzoate
?
-
-
-
-
?
O3-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O3-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
in the absence of sulfide O3-acetyl-L-serine reacts with the cofactor pyridoxal 5'-phosphate to alpha-aminoacrylate intermediate
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
970% of the activity with cyanide
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.5.1.65, O-phosphoserine hydrolase
-
-
-
additional information
?
-
-
isoenzyme 1 and 2 have different substrate specificities towards various beta-substituted L-Cys
-
-
-
additional information
?
-
-
enzyme is induced in leaves exposed to salt stress. The results suggest that the plant enzyme is responding to the salt stress by inducing cysteine biosynthesis as a protection against high ion concentrations
-
-
-
additional information
?
-
-
model of a dynamic cysteine synthesis system with regulatory function
-
-
-
additional information
?
-
-
preferred state of sulfide is hydrogen sulfide
-
-
-
additional information
?
-
the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity
-
-
-
additional information
?
-
-
cysteine synthase CysB is the only isoform of physiological importance in Aspergillus nidulans. Starvation-induced cysteine synthase activity is under control of cross-pathway regulation
-
-
-
additional information
?
-
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
-
additional information
?
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
-
additional information
?
-
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
-
additional information
?
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
-
additional information
?
-
-
the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
-
-
-
additional information
?
-
the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
-
-
-
additional information
?
-
-
beta-substituted alanines, low activity
-
-
-
additional information
?
-
-
several nucleophiles may stimulate sulfide formation
-
-
-
additional information
?
-
-
activity of the enzyme bound to serine acetyltransferase is lower than that of the free enzyme
-
-
-
additional information
?
-
no substrate: L-serine, L-homoserine, O-acetyl-L-homoserine, L-alanine, L-homocysteine
-
-
-
additional information
?
-
-
no substrate: L-serine, O-propionyl-L-serine, L-alanine, glycine
-
-
-
additional information
?
-
-
stopped-flow fluorescence spectroscopy is used to characterize the interaction of serine acetyltransferase with OASS and in the presence of the physiological regulators cysteine and bisulfide. Cysteine synthase assembly occurs via a two-step mechanism involving rapid formation of an encounter complex between the two enzymes, followed by a slow conformational change. The conformational change likely results from the closure of the active site of OASS upon binding of the serine acetyltransferase C-terminal peptide. Bisulfide stabilizes the cysteine synthase complex mainly by decreasing the back rate of the isomerization step. Cysteine, the product of the OASS reaction and a SAT inhibitor, slightly affects the kinetics of cysteine synthase formation leading to destabilization of the complex
-
-
-
additional information
?
-
-
the binding free energy of 400 pentapeptides, MNXXI, interacting with the HiOASS-A active site using a combined docking-scoring procedure based on GOLD and HINTare examined. The free energy prediction is verified by the experimental determination of the binding affinity of 14 of these pentapeptides, selected for spanning a large range of predicted binding affinity and presenting charged, polar, or apolar residues at mutation sites
-
-
-
additional information
?
-
the binding free energy of 400 pentapeptides, MNXXI, interacting with the HiOASS-A active site using a combined docking-scoring procedure based on GOLD and HINTare examined. The free energy prediction is verified by the experimental determination of the binding affinity of 14 of these pentapeptides, selected for spanning a large range of predicted binding affinity and presenting charged, polar, or apolar residues at mutation sites
-
-
-
additional information
?
-
no substrates: serine, phosphoserine, O-succinylhomoserine, thiosulfate
-
-
-
additional information
?
-
-
no substrates: serine, phosphoserine, O-succinylhomoserine, thiosulfate
-
-
-
additional information
?
-
-
no synthesis of mimosine. The enzyme is specific for cysteine synthesis. The recombinant enzyme is active with or without the leader peptide
-
-
-
additional information
?
-
no synthesis of mimosine. The enzyme is specific for cysteine synthesis. The recombinant enzyme is active with or without the leader peptide
-
-
-
additional information
?
-
-
the enzyme is induced by Al3+. Cysteine synthase may be a key player during Al response/adaptation in rice
-
-
-
additional information
?
-
-
enzyme additionally catalyzes the formation of O-ureido-L-serine from O-acetyl-L-serine and hydroxyurea, reaction of EC 2.6.99.3. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
-
-
-
additional information
?
-
-
enzyme additionally catalyzes the formation of O-ureido-L-serine from O-acetyl-L-serine and hydroxyurea, reaction of EC 2.6.99.3. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cysteine + CN-
cyanoalanine + H2S
Xanthium pennsylvanicum
-
involved in cyanide metabolism during seed germination
-
-
-
L-Cys + acetate
?
-
involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear
-
-
-
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
the side reaction of the enzyme seems to contribute massively to the total H2S release of higher plants at least at higher pH values
-
-
-
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
enzyme that catalyzes the final step in cysteine biosynthesis. Cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
Entamoeba histolytica, the causative agent of human amoebiasis, is essentially anaerobic, requiring a small amount of oxygen for growth. It cannot tolerate the higher concentration of oxygen present in human tissues or blood. However, during tissue invasion it is exposed to a higher level of oxygen, leading to oxygen stress. Cysteine, which is a vital thiol in Entamoeba histolytica, plays an essential role in its oxygen-defence mechanisms. The major route of cysteine biosynthesis in this parasite is the condensation of O-acetylserine with sulfide by the de novo cysteine-biosynthetic pathway, which involves cysteine synthase (EhCS) as a key enzyme
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
O81154, O81155
OASTL activity regulates not only Cys de novo synthesis but also its homeostasis
-
-
?
O-acetyl-L-Ser + isoxazylin-5-one
?
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
-
O-acetyl-L-Ser + isoxazylin-5-one
?
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
the cysteine synthase complex functions as a molecular sensor system that monitors the sulfur status of the cell and controls sulfate assimilation and cysteine synthesis according to the availability of sulfate
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in synthesis of antioxidants such as glutathione during fruit development
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
activity varies between sulfur sources, enzyme formation regulated by L-Cys concentration
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in glutathione formation
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
controlled by feedback inhibition, adaptively significant as sulfide removal mechanism
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
repressed during growth with sulfide or thiosulfide as sulfur source
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
key role in metabolism of S-containing amino acids
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
functions as a Cys synthase rather than as a homocysteine synthase in vivo
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
enzyme transcription repressed by L-cystine, derepressed by limiting sulfide concentrations
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in thiosulfate assimilation
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
P47998
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
P47999, Q43725
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
Q43725
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
O45679
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
Q93244
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
Q401L7
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
O15635
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
Escherichia coli W3110 / ATCC 27325
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
P45040
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
A4HPM6
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
A4HPM6
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
W5S3I4
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
A8YBP8, A8YBS4
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
P0A1E3
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
P29848
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
P0A1E3, P29848
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
P0A1E3, P29848
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
O15570
in the absence of sulfide O3-acetyl-L-serine reacts with the cofactor pyridoxal 5'-phosphate to alpha-aminoacrylate intermediate
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
P45040
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
additional information
?
-
-
enzyme is induced in leaves exposed to salt stress. The results suggest that the plant enzyme is responding to the salt stress by inducing cysteine biosynthesis as a protection against high ion concentrations
-
-
-
additional information
?
-
-
model of a dynamic cysteine synthesis system with regulatory function
-
-
-
additional information
?
-
Q43725
the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity
-
-
-
additional information
?
-
-
cysteine synthase CysB is the only isoform of physiological importance in Aspergillus nidulans. Starvation-induced cysteine synthase activity is under control of cross-pathway regulation
-
-
-
additional information
?
-
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
-
additional information
?
-
Q2PZM5
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
-
additional information
?
-
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
-
additional information
?
-
Q2PZM5
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
-
additional information
?
-
-
the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
-
-
-
additional information
?
-
O45679
the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
-
-
-
additional information
?
-
-
stopped-flow fluorescence spectroscopy is used to characterize the interaction of serine acetyltransferase with OASS and in the presence of the physiological regulators cysteine and bisulfide. Cysteine synthase assembly occurs via a two-step mechanism involving rapid formation of an encounter complex between the two enzymes, followed by a slow conformational change. The conformational change likely results from the closure of the active site of OASS upon binding of the serine acetyltransferase C-terminal peptide. Bisulfide stabilizes the cysteine synthase complex mainly by decreasing the back rate of the isomerization step. Cysteine, the product of the OASS reaction and a SAT inhibitor, slightly affects the kinetics of cysteine synthase formation leading to destabilization of the complex
-
-
-
additional information
?
-
-
the enzyme is induced by Al3+. Cysteine synthase may be a key player during Al response/adaptation in rice
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
1 per subunit of free enzyme, 4 per of cysteine synthase complex
pyridoxal 5'-phosphate
-
2.1 mol per mol of dimeric enzyme
pyridoxal 5'-phosphate
-
stoichiometry, binds to Lys, protects against inactivation by heat, urea, and trypsin, four binding sites per mol apoenzyme, association constant
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate containing catalytic sites are not equivalent
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate-binding site covalently bound, buried deeply within protein
pyridoxal 5'-phosphate
-
enzyme contains 1.2 pyridoxal phosphate per subunit
pyridoxal 5'-phosphate
-
enzyme contains pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
the 5'-phosphate is tightly bound to the enzyme via a hydrogen bond to His152, one to the residues responsible for positioning of the cofactor
pyridoxal 5'-phosphate
-
gives the crystals a yellow color, covalently linked to Lys58, interaction with Gly236, Ser280, Pro307, cofactor orientation at the active site and absorbance maximum change upon binding of cysteine or methionine
pyridoxal 5'-phosphate
-
the 31P chemical shift of the internal and external Schiff bases of pyridoxal 5'-phosphate in OASS-B are further downfield compared to OASS-A, suggesting a tighter binding of the cofactor in the B-isozyme. The chemical shift of the internal Schiff base (ISB) of OASS-B is 6.2 ppm, the highest value reported for the ISB of a PLP-dependent enzyme. Considering the similarity in the binding sites of the pyridoxal 5'-phosphate cofactor for both isozymes, torsional strain of the C5-C5' bond (O4'-C5'-C5-C4) of the Schiff base is proposed to contribute to the further downfield shift; tighter binding than in OASS-A, treatment with 1 mM hydroxylamine in 500 mM phosphate, pH 7.6, with 0.2 mM dithiothreitol, followed by dialysis against 100 mM phosphate, pH 7.0, with 0.2 mM dithiothreitol gerates apo-enzyme without the cofactor
pyridoxal 5'-phosphate
-
sequence alignment and site-directed mutation of the enzyme reveal that the cofactor PLP is covalently bound in Schiff base linkage with K30, as well as the two residues H150 and H168 are the crucial residues for PLP binding and stabilization
pyridoxal 5'-phosphate
-
enzyme sites K30, H150, and H168 are crucial for cofactor binding and stabilization
pyridoxal 5'-phosphate
-
R186 interacts with the cofactor
pyridoxal 5'-phosphate
-
residue K51 forms a Schiff base with pyridoxal 5'-phosphate, with conserved residues N82 and S274 forming hydrogen bonds to the cofactor. Further residues predicted to orient and hold the pyridoxal 5'-phosphate in position are G186, T182, G183 and T185
pyridoxal 5'-phosphate
dependent on, binding site structure analysis in a cleft between the N- and C-terminal domains, the phosphate group of PLP interacts with the highly conserved Gly/Thr-rich loop (G181TGGT185) and a water molecule, overview
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on; dependent on
pyridoxal 5'-phosphate
-
cofactor pyridoxal 5'-phosphate is linked covalently to Lys58, which is conserved in all OASS structures and is positioned in between these two domains, and highly conserved residues, such as Gly236, Ser280 and Pro307, interact with the aromatic ring of pyridoxal 5'-phosphate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2R)-1-(4-chlorobenzyl)-2-phenylcyclopropanecarboxylic acid
;
(1R,2R)-1-(4-methylbenzyl)-2-phenylcyclopropanecarboxylic acid
;
(1R,2R)-1-benzyl-2-phenylcyclopropanecarboxylic acid
;
(1R,2S)-1-ethyl-2-phenylcyclopropanecarboxylic acid
;
(1S,2R)-1-ethyl-2-phenylcyclopropanecarboxylic acid
;
(1S,2S)-1-(4-chlorobenzyl)-2-phenylcyclopropanecarboxylic acid
;
(1S,2S)-1-(4-methylbenzyl)-2-phenylcyclopropanecarboxylic acid
;
(1S,2S)-1-benzyl-2-phenylcyclopropanecarboxylic acid
;
(2E)-3-chloropent-2-enedioic acid
-
;
1,1'-(1,3-propanediyl)bis(5-benzyl-6-methylsulfanyl-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one)
-
-
1,1'-(1,3-propanediyl)bis(5-ethyl-6-methylthio-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one)
-
-
1,1'-(1,3-propanediyl)bis(5-methyl-6-methylthio-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one)
-
-
1,3-bis(4-ethoxy-6-methyl-sulfanyl-1H-pyrazolo[3,4-d]pyrimidin-1-yl)propane
-
-
1-(2-naphthylsulfonyl)-3-phenyl-1H-pyrazolo[3,4-d]pyrimidin-4-amine
-
-
1-(4,6-dimethylsulfanyl-1H-pyrazolo[3,4-d]pyrimidin-1-yl)-3-(5-methyl-6-methylsulfanyl-4-oxo-1,5-dihydropyrazolo[3,4-d]pyrimidin-1-yl)propane
-
-
1-ethyl-4-nitro-1H-pyrazole-5-carboxylic acid
-
;
1-N,4-N-bis[3-(1Hbenzimidazol-2-yl) phenyl]benzene-1,4-dicarboxamide
determined as potential inhibitor via computational inhibitor screening, molecular dynamics simulation and homology modeling
1-[(2,5-dichlorophenyl)sulfonyl]-3-phenyl-1Hpyrazolo[3,4-d]pyrimidine-4-amine
-
-
1-[(4-chlorophenyl)sulfonyl]-3-phenyl-1H-pyrazolo[3,4-d]pyrimidine-4-amine
-
-
1-[(4-nitrophenyl)sulfonyl]-3-phenyl-1H-pyrazolo[3,4-d]pyrimidine-4-amine
-
-
2,2'-(1,2,4-thiadiazole-3,5-diyldisulfanediyl)diacetic acid
-
;
2,2'-(5-ethyl-5-nitrodihydropyrimidine-1,3(2H,4H)-diyl)diacetic acid
-
;
2-[(1-methyl-1H-tetrazol-5-yl)sulfanyl]pyridine-3-carboxylic acid
-
;
2-[(5-methyl-1,3,4-thiadiazol-2-yl)carbamoyl]-3-nitrobenzoic acid
-
;
3,3'-[(phenylsulfonyl)imino]dipropanoic acid (non-preferred name)
-
;
3-(morpholin-4-ylmethyl)furan-2-carboxylic acid
-
;
4,6-bis(methylsulfanyl)-1-phthalimidopropyl-1H-pyrazolo[3,4-d]-pyrimidine
-
-
4-(2-methylphenyl)-8-nitro-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one
-
minimum inhibitory concentration against Mycobacterium tuberculosis 0.0335 mM, cytotoxicity against HEK 293T cell 3.6% at 0.025 mM
4-(4-methoxyphenyl)-8-nitro-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one
-
minimum inhibitory concentration against Mycobacterium tuberculosis 0.0321 mM, cytotoxicity against HEK 293T cell 0.2% at 0.025 mM
4-(methylsulfinyl)-2-[(phenylsulfonyl)amino]butanoic acid
-
;
4-hydroxy-2-[2-(1H-indol-3-yl)-2-oxoethyl]sulfanyl-1H-pyrimidin-6-one
-
inhibitor identified by molecular docking. Conserved residues involved in hydrogen bonding interaction include T85, S86, Q159, G87, R116, and G236. The compound displays a binding affinity of 8.05 microM and inhibits about 73% activity at 0.1 mM
6-(1,3,4-thiadiazol-2-ylcarbamoyl)cyclohex-3-ene-1-carboxylic acid
-
;
6-methyl-4,5,6,7-tetrahydro-1,2-benzoxazole-5,6-dicarboxylic acid
-
;
6-methyl-7-oxo-6-azabicyclo[3.2.1]oct-2-ene-2,8-dicarboxylic acid
-
;
6-methylsulfanyl-1-(3-phenylpropyl)-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one
-
-
6-methylsulfanyl-1-phthalimidopropyl-4(pyrrolidin-1-yl)-1H-pyrazolo[3,4-d]pyrimidine
-
-
6-[(pyridin-4-ylmethyl)carbamoyl]cyclohex-3-ene-1-carboxylic acid
-
;
8-nitro-4-(2-nitrophenyl)-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one
-
minimum inhibitory concentration against Mycobacterium tuberculosis 0.0309 mM, cytotoxicity against HEK 293T cell 1% at 0.025 mM
8-nitro-4-[2-(trifluoromethyl)phenyl]-4,4a-dihydro-2H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidine-2,5(3H)-dione
-
minimum inhibitory concentration against Mycobacterium tuberculosis 0.0076 mM, cytotoxicity against HEK 293T cell 5.7% at 0.025 mM
cystine
competitive versus O-acetyl-L-serine, the cystine-binding residues are highly conserved in all OASS proteins; competitive versus O-acetyl-L-serine, the cystine-binding residues are highly conserved in all OASS proteins. Active site of CysK2–cystine binding structure, overview. Cystine occupies the substrate/product binding site of the enzyme
D-cycloserine
-
82% loss of activity at 5 mM
DYVI
-
a peptide based on the C-terminus of the partner serine acetyltransferase with which the enzyme forms a complex, competitive inhibition
exophillic acid
from Exophiala sp.FKI-7082 , specific for isozyme CS1
MNDGI
-
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNEGI
-
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNENI
-
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNETI
-
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNKGI
-
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNKVI
-
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNLGI
-
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNLNI
-
pentapeptide inhibitor; wild type pentapeptide of serine acetyltransferase
MNPHI
-
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNVPI
-
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNWNI
-
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNYFI
-
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNYSI
-
pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
N-(furan-2-ylcarbonyl)phenylalanine
-
;
N-[(2,2-dimethyl-4,6-dioxo-1,3-dioxan-5-ylidene)methyl]glutamic acid
-
;
N-[(2,2-dimethyl-4,6-dioxo-1,3-dioxan-5-ylidene)methyl]leucine
-
;
N-[(3-carboxybicyclo[2.2.1]hept-5-en-2-yl)carbonyl]glycylglycine
-
;
N-{4-[(4-amino-3-phenyl-1H-pyrazolo[3,4-d]pyrimidin-1-yl)sulfonyl]phenyl}acetamide
-
-
NH2OH
-
97% loss of activity at 10 mM
peroxynitrite
-
nitrating conditions after exposure to peroxynitrite strongly inhibit enzyme activity. Among the isoforms, cytosolic OASA1 is markedly sensitive to nitration. Nitration assays on purified recombinant OASA1 protein lead to 90% reduction of the activity due to inhibition of the enzyme. Inhibition of OASA1 activity upon nitration correlates with the identification of a modified OASA1 protein containing a 3-nitroTyr302 residue. Inhibition caused by Tyr302 nitration on OASA1 activity seems to be due to a drastically reduced O-acetylserine substrate binding to the nitrated protein, and also to reduced stabilization of the pyridoxal-5-phosphate cofactor through hydrogen bonds
serine acetyltransferase
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serine acetyltransferase (EC 2.3.1.30) can inhibit O-acetylserine sulfhydrylase catalytic activity with a double mechanism, the competition with O-acetylserine for binding to the enzyme active site and the stabilization of a closed conformation that is less accessible to the natural substrate
-
trans-1-(4-chlorobenzyl)-2-phenylcyclopropanecarboxylic acid
;
trans-1-(4-methylbenzyl)-2-phenylcyclopropanecarboxylic acid
;
trans-1-benzyl-2-phenylcyclopropanecarboxylic acid
;
trans-1-ethyl-2-phenylcyclopropanecarboxylic acid
;
trans-1-phenethyl-2-phenylcyclopropanecarboxylic acid
;
trans-2-phenylcyclopropanecarboxylic acid
;
trichloroacetic acid
inactivation at 16.6% v/v; inactivation at 16.6% v/v
xanthofulvin
from Penicillium sp. if08054; from Penicillium sp. if08054 , inhibits isozymes CS1 and CS3
[2-[3-acetyl-1-(2,2-dihydroxyethyl)-4-hydroxy-5-oxo-2,5-dihydro-1H-pyrrol-2-yl]phenyl](hydroxy)oxoammonium
-
;
[3-[(2-carboxy-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-en-7-yl)carbamoyl]-1-methyl-1H-pyrazol-4-yl](hydroxy)oxoammonium
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;
[3-[(2-carboxypiperidin-1-yl)sulfonyl]phenyl](hydroxy)oxoammonium
-
;
Aminooxyacetate
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57% and 64% inhibition at 1 mM, isoenzymes 1 and 2, respectively
cadmium chloride
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plants grown in the presence of 0.0178 mM cadmium chloride show 141% increase in activity in leaves, and 189% increase in activity in root, respectively
cadmium chloride
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plants grown in the presence of 0.0178 mM cadmium chloride show 150% increase in activity in leaves; plants grown in the presence of 0.0178 mM cadmium chloride show 260% increase in activity in leaves, and 222% increase in activity in root, respectively
copper sulfate
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plants grown in the presence of 0.78 mM copper sulfate show 102% increase in activity in leaves, and 98% increase in activity in root, respectively
copper sulfate
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plants grown in the presence of 0.78 mM copper sulfate show 20% increase in activity in leaves, and 110% increase in activity in root, respectively; plants grown in the presence of 0.78 mM copper sulfate show 56% increase in activity in leaves
hydroxylamine
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35% and 48% inhibition at 5 mM, isoenzymes 1 and 2, respectively
hydroxylamine
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complete inhibition at 10 mM, isoenzymes 1 and 2, 90% inhibition at 10 mM, isoenzyme 3
L-cysteine
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not inhibitory up to 3.7 mM
lead nitrate
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plants grown in the presence of 2.4 mM lead nitrate plus 5 mM EDTA show 197% increase in activity in leaves, and 201% increase in activity in root, respectively
lead nitrate
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plants grown in the presence of 2.4 mM lead nitrate plus 5 mM EDTA show 176% increase in activity in leaves; plants grown in the presence of 2.4 mM lead nitrate plus 5 mM EDTA show 302% increase in activity in leaves, and 300% increase in activity in root, respectively
methionine
-
46% and 37% inhibition at 1 mM, isoenzymes 1 and 2, respectively
MNYDI
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pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action
MNYDI
interaction of the inhibitory pentapeptide MNYDI with CysK OASS isozyme from Salmonella typhimurium, the MNYDI peptide interacts with the HiCysK active site mainly through H-bonds involving its C-terminal carboxylate and hydrophobic interactions involving the side chains of Ile5 and Tyr3, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview
MNYDI
interaction of the inhibitory pentapeptide MNYDI with CysK OASS isozyme from Salmonella typhimurium, the MNYDI peptide interacts with the HiCysK active site mainly through H-bonds involving its C-terminal carboxylate and hydrophobic interactions involving the side chains of Ile5 and Tyr3, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview; interaction of the inhibitory pentapeptide MNYDI with CysM OASS isozyme from Salmonella typhimurium, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview. In isozyme CysM multiple H-bond interactions are made by Asn2 side chain with S205 side chain and I206 and I209 backbone carbonyl groups
p-chloromercuribenzoate
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14% and 4% inhibition at 1 mM, isoenzymes 1 and 2, respectively
p-chloromercuribenzoate