Information on EC 2.5.1.47 - cysteine synthase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
2.5.1.47
-
RECOMMENDED NAME
GeneOntology No.
cysteine synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
show the reaction diagram
mechanism of reverse reaction
-
O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
show the reaction diagram
mechanism similar to those of other pyridoxal enzymes
-
O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
show the reaction diagram
model of reaction mechanism
-
O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
show the reaction diagram
mechanism
-
O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
show the reaction diagram
mechanism interpreted in structural context, conformational changes during catalysis
-
O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
show the reaction diagram
mechanism
-
O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
show the reaction diagram
identification and spectral characterization of the external aldimine of the reaction, mechanism
-
O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
show the reaction diagram
geometric model of reaction, comparison isoenzyme CysK
P16703
O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
show the reaction diagram
model of reaction mechanism
Synechococcus sp. 6301
-
-
O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C-O bond cleavage
-
-
-
-
elimination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Cysteine and methionine metabolism
-
cysteine biosynthesis I
-
Metabolic pathways
-
seleno-amino acid biosynthesis
-
Sulfur metabolism
-
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).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acetylserine sulfhydrylase
-
-
-
-
beta-cyano-L-alanine synthase
Q845F9
-
CS-A
O81154
-
CS-B
O81155
-
CSase
-
-
-
-
CSase A
O81154
-
CSase B
O81155
-
Cys synthase complex
-
serine acetyltransferase (EC 2.3.1.30) and O-acetylserine thiol lyase reversibly form the heterooligomeric Cys synthase complex
cysK
E5LPF4
-
CysM
P16703
-
CysM
Staphylococcus aureus SH1000
-
-
-
Cysteine synthase
Q8W1A0
-
Cysteine synthase
-
-
cysteine synthetase
-
-
-
-
DcsD
Streptomyces lavendulae ATCC 11924
D2Z027
-
-
EC 4.2.99.8
-
-
formerly
-
EhOASS
O15570
-
GmOAS-TL1
A3RM03
-
GmOAS-TL2
A3RM04
-
GmOAS-TL3
A5YT86
-
GmOAS-TL4
A5YT88
-
GmOAS-TL6
A3RM05
-
GmOAS-TL7
A3RM06
-
GmOASTL4
-
-
GsOAS-TL1
-
-
HiOASS-A
P45040
-
Nt-OAS-TL
-
-
O -acetylserine (thiol)-lyase
Q2PZM5
-
O -acetylserine (thiol)-lyase
Azospirillum brasilense Sp7
Q2PZM5
-
-
O-acetyl-L-serine (thiol) lyase
-
-
O-acetyl-L-serine acetate-lyase (adding hydrogen sulfide)
-
-
-
-
O-acetyl-L-serine sulfhydrylase
-
-
-
-
O-acetyl-L-serine sulfohydrolase
-
-
-
-
O-acetyl-L-serine(thiol)lyase
-
-
-
-
O-acetylserine (thiol) lyase
-
-
O-acetylserine (thiol) lyase
Q6STL6
-
O-acetylserine (thiol) lyase
-
-
O-acetylserine (thiol) lyase
Saccharomyces cerevisiae P169-4A
-
-
-
O-acetylserine (Thiol)-lyase
-
-
-
-
O-acetylserine (thiol)-lyase A
P0A1E3
-
O-acetylserine (thiol)-lyase B
P29848
-
O-acetylserine (thiol)lyase
-
-
-
-
O-acetylserine sulfhydrylase
-
-
-
-
O-acetylserine sulfhydrylase
O15570
-
O-acetylserine sulfhydrylase
-
-
O-acetylserine sulfhydrylase
Q8W1A0
-
O-acetylserine sulfhydrylase
-
-
O-acetylserine sulfhydrylase
-
cysteine synthase is a multiprotein assembly formed by the pyridoxal 5'-phosphate-dependent enzyme O-acetylserine sulfhydrylase and serine acetyltransferase
O-acetylserine sulfhydrylase
P45040
-
O-acetylserine sulfhydrylase
-
-
O-acetylserine sulfhydrylase
P0A1E3, P29848
-
O-acetylserine sulfhydrylase
Salmonella enterica subsp. enterica serovar Typhimurium DW378
-
-
-
O-acetylserine sulfhydrylase A
-
-
-
-
O-acetylserine sulfhydrylase A
P0A1E3
-
O-acetylserine sulfhydrylase B
P29848
-
O-acetylserine sulfhydrylase isoenzyme B
P16703
-
O-acetylserine sulfhydrylase-A
Salmonella enterica subsp. enterica serovar Typhimurium DW378
-
-
-
O-acetylserine sulfhydrylase-B
-
-
O-acetylserine thiol lyase
-
-
O-acetylserine(thiol)lyase
-
-
-
-
O-acetylserine(thiol)lyase
-
-
O-acetylserine-(thiol)lyase
-
-
O-acetylserine-O-acetylhomoserine sulfhydro-lyase
-
-
-
-
OAS Shase
-
-
-
-
OAS thiol-lyases
-
-
OAS-TL
-
-
-
-
OAS-TL
-
-
OAS-TL A
O81154
-
OAS-TL B
O81155
-
OASS
-
-
-
-
OASS
Azospirillum brasilense Sp7
Q2PZM5
-
-
OASS
Q8W1A0
-
OASS
P0A1E3
-
OASS-A
Salmonella enterica subsp. enterica serovar Typhimurium DW378
-
;
-
OASS-B
-
produced under unaerobic grwoth conditions in contrast to OASS-A
OASTL
-
-
-
-
OASTL
-
-
OASTL-A
Saccharomyces cerevisiae P169-4A
-
-
-
OPSS
Q9YBL2
-
S-sulfocysteine synthase
-
-
-
-
SSC synthase
-
-
SSC synthase
-
-
-
StOASTL A
O81154
-
StOASTL B
O81155
-
synthase, cysteine
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37290-89-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain K1
-
-
Manually annotated by BRENDA team
two isoforms, immunologically distinct
-
-
Manually annotated by BRENDA team
two isoenzymes, one with additional S-sulfocysteine synthase activity
-
-
Manually annotated by BRENDA team
3 isoforms, recombinant enzymes, fast increase in enzyme product in response to sulfate deprivation
-
-
Manually annotated by BRENDA team
ecotype Columbia
-
-
Manually annotated by BRENDA team
strain Sp7
Q2PZM5
SwissProt
Manually annotated by BRENDA team
Azospirillum brasilense Sp7
strain Sp7
Q2PZM5
SwissProt
Manually annotated by BRENDA team
two isoenzymes
-
-
Manually annotated by BRENDA team
three isoenzymes
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
strain 10-1
-
-
Manually annotated by BRENDA team
; isoenzyme CysM
Uniprot
Manually annotated by BRENDA team
overexpression in Escherichia coli
-
-
Manually annotated by BRENDA team
-
Swissprot
Manually annotated by BRENDA team
cytosolic isoform
Swissprot
Manually annotated by BRENDA team
aerobic form of enzyme forms a tight bienzyme complex in vivo with serine acetyltransferase
-
-
Manually annotated by BRENDA team
L. cultivar Xiangnuo 1
-
-
Manually annotated by BRENDA team
three isoforms
-
-
Manually annotated by BRENDA team
two isoenzymes, one with additional S-sulfocysteine synthase activity
-
-
Manually annotated by BRENDA team
low molecular weight enzyme is the same protein as serine sulfhydrylase
-
-
Manually annotated by BRENDA team
low molecular weight enzyme, wild type and Cys auxotroph strain
-
-
Manually annotated by BRENDA team
strain P169-4A
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae P169-4A
strain P169-4A
-
-
Manually annotated by BRENDA team
subsp. enterica serovar Typhimurium
UniProt
Manually annotated by BRENDA team
one enzyme free, one associated with serine transacetylase in cysteine synthase
-
-
Manually annotated by BRENDA team
S-sulfocysteine synthase is identical with cysteine synthase B
-
-
Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium DW378
DW378
-
-
Manually annotated by BRENDA team
cv. Danshaku
-
-
Manually annotated by BRENDA team
isoenzyme 1'
-
-
Manually annotated by BRENDA team
L. cv. Medina
-
-
Manually annotated by BRENDA team
overexpression in Nicotiana tabacum
-
-
Manually annotated by BRENDA team
three isoenzymes
-
-
Manually annotated by BRENDA team
Staphylococcus aureus SH1000
-
-
-
Manually annotated by BRENDA team
Streptomyces lavendulae ATCC 11924
-
UniProt
Manually annotated by BRENDA team
strain 6301, two isoenzymes
-
-
Manually annotated by BRENDA team
Synechococcus sp. 6301
strain 6301, two isoenzymes
-
-
Manually annotated by BRENDA team
Xanthium pennsylvanicum
three isoforms
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
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
-
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
-
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
-
the inhibition of cysteine biosynthesis in prokaryotes and protozoa is proposed for the development of antibiotics
malfunction
-
knockout mutants demonstrate a reduction in size and show paleness, but penetrance of the growth phenotype depend on the light regime. The cs26 mutant plants also show reductions in chlorophyll content and photosynthetic activity as well as elevated glutathione levels. cs26 mutant leaves are not able to properly detoxify reactive oxygen species, which accumulate to high levels under long-day growth conditions. The transcriptional profile of the cs26 mutant reveal that the mutation has a pleiotropic effect on many cellular and metabolic processes
malfunction
Staphylococcus aureus SH1000
-
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
-
metabolism
-
catalyzes the final step of the L-cysteine biosynthesis
metabolism
-
key enzyme in the L-cysteine pathway
metabolism
Salmonella enterica subsp. enterica serovar Typhimurium DW378
-
catalyzes the final step of the L-cysteine biosynthesis
-
physiological function
-
product cysteine plays an important role in the antioxidative defense mechanisms of the human parasite
physiological function
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
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
E5LPF4, -
enzyme is able to complement the cysteine auxotrophy of an Escherichia coli cysMK mutant
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
-
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
-
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
-
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
-
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
O22682
S-sulfocysteine activity of enzyme is essential for the proper photosynthetic performance of the chloroplast under long-day growth conditions. Results suggest that S-sulfocysteine synthase functions as a protein sensor to detect the accumulation of thiosulfate as a result of the inadequate detoxification of reactive oxygen species generated under conditions of excess light to produce the S-sulfocysteine molecule that triggers protection mechanisms of the photosynthetic apparatus
physiological function
-
the enzyme's active site has two access sites. Binding of the enzyme to the C-terminal tail of serine O-acetyltransferase leads to loss of activity due to reduction in ligand accessibility of the second, unoccupied active site. The observed dynamics of the gates show allosteric closure of the unoccupied active site of the enzyme in the cysteine synthase complex, which can hinder substrate binding, abolishing its turnover to cysteine
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-chloro-L-alanine + NaHS
L-cysteine + ?
show the reaction diagram
-
beta-replacement reaction, enzyme can be induced by 3-chloro-L-alanine
-
?
5-thio-2-nitrobenzoate + O-acetyl-L-serine
acetate + ?
show the reaction diagram
-
-
-
-
?
beta-chloro-L-alanine + 2-nitro-5-thiobenzoate
?
show the reaction diagram
-
-
-
-
?
chloroalanine + sulfide
cysteine + chloride
show the reaction diagram
-
beta-chloroalanine, 6% of the activity with O-acetyl-L-Ser
-
-
r
chloroalanine + sulfide
cysteine + chloride
show the reaction diagram
-
3-6% of the activity of the cysteine synthase reaction
-
r
cyanide + cysteine
beta-cyanoalanine + sulfide
show the reaction diagram
-
-
-
?
cysteine + CN-
cyanoalanine + H2S
show the reaction diagram
Xanthium pennsylvanicum
-
-
-
?
cysteine + CN-
cyanoalanine + H2S
show the reaction diagram
-
-
H2S i.e. bisulfide
?
cysteine + CN-
cyanoalanine + H2S
show the reaction diagram
Xanthium pennsylvanicum
-
involved in cyanide metabolism during seed germination
-
-
-
L-Cys + acetate
O-acetyl-L-Ser + H2S
show the reaction diagram
-
-
-
r
L-Cys + acetate
O-acetyl-L-Ser + H2S
show the reaction diagram
-
-
-
r
L-Cys + acetate
O-acetyl-L-Ser + H2S
show the reaction diagram
-
-
-
r
L-Cys + acetate
O-acetyl-L-Ser + H2S
show the reaction diagram
-
equilibrium constant
-
r
L-Cys + acetate
?
show the reaction diagram
-
involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear
-
-
-
L-Cys + dithiothreitol
beta-cyanoalanine + H2S
show the reaction diagram
E5LPF4, -
-
-
-
?
L-cysteine + cyanide
cyanoalanine + H2S
show the reaction diagram
Q845F9
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
show the reaction diagram
-
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
show the reaction diagram
-
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
show the reaction diagram
-
the side reaction of the enzyme seems to contribute massively to the total H2S release of higher plants at least at higher pH values
-
-
-
L-homocysteine + L-serine
L-cystathionine + H2O
show the reaction diagram
-
-
-
?
NaN3 + O-acetyl-Ser
beta-azidoalanine + sodium acetate
show the reaction diagram
-
-
mutagenic
?
NaN3 + O-acetyl-Ser
beta-azidoalanine + sodium acetate
show the reaction diagram
-
-
mutagenic in Salmonella typhimurium
?
O-acetyl-L-Ser + 1,2,3,4-tetrazole
?
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + 1,2,3-benzotriazole
?
show the reaction diagram
-
weak activity
-
-
?
O-acetyl-L-Ser + 1,2,4-triazole
?
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + 1-propanethiol
?
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
show the reaction diagram
-
6.2% of the activity with sulfide, isoenzyme 2
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
show the reaction diagram
-
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 + ?
show the reaction diagram
-
18% of activity with sulfide
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
show the reaction diagram
-
18% of activity with sulfide
-
?
O-acetyl-L-Ser + 3-mercapto-1,2,4-triazole
?
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + 5-mercapto-2-nitrobenzoate
S-(3-carboxy-4-nitrophenyl)-L-cysteine + ?
show the reaction diagram
-
-
-
?
O-acetyl-L-Ser + benzenethiol
L-cys + benzylacetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + cysteamine
?
show the reaction diagram
-
weak activity
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
-
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
E5LPF4, -
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
equilibrium constant
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
O81154, O81155, -
OASTL activity regulates not only Cys de novo synthesis but also its homeostasis
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
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
show the reaction diagram
-, Q6STL6
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
show the reaction diagram
-
-
-
?
O-acetyl-L-Ser + isoxazylin-5-one
?
show the reaction diagram
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
-
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
show the reaction diagram
-
2.2% of activity with sulfide, isoenzyme 1 and 2
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
show the reaction diagram
-
2.3% and 1.6% of activity with sulfide, isoenzymes 1 and 2, respectively
-
-
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
show the reaction diagram
-
6.1% of activity with sulfide
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
show the reaction diagram
-
2.5% of activity with sulfide
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
show the reaction diagram
-
-
-
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
show the reaction diagram
-
-
product identification uncertain
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
show the reaction diagram
-
4% and 1% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
show the reaction diagram
-
21.5% and 77% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
show the reaction diagram
-
32% of activity with sulfide
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
show the reaction diagram
-
-
-
-
-
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
show the reaction diagram
-
6.84% and 7.64% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
show the reaction diagram
-
12.3% of activity with sulfide
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
show the reaction diagram
-
-
-
-
-
O-acetyl-L-Ser + pyrazole
?
show the reaction diagram
-
weak activity
-
-
?
O-acetyl-L-Ser + S2O32-
S-sulfocysteine + ?
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + sodium azide
?
show the reaction diagram
-
weak activity
-
-
?
O-acetyl-L-Ser + sodium thiosulfate
?
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + sodium thiosulfate
?
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + sodium thiosulfate
?
show the reaction diagram
Staphylococcus aureus SH1000
-
-
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
-
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
-
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
-
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
-
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
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
show the reaction diagram
-
key role in metabolism of S-containing amino acids
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
activity varies between sulfur sources, enzyme formation regulated by L-Cys concentration
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
involved in synthesis of antioxidants such as glutathione during fruit development
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
involved in glutathione formation
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
enzyme transcription repressed by L-cystine, derepressed by limiting sulfide concentrations
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
functions as a Cys synthase rather than as a homocysteine synthase in vivo
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
controlled by feedback inhibition, adaptively significant as sulfide removal mechanism
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
repressed during growth with sulfide or thiosulfide as sulfur source
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
involved in thiosulfate assimilation
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
Synechococcus sp., Synechococcus sp. 6301
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + thiosulfate
S-sulfocysteine + sodium acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-Ser + thiosulfate
S-sulfocysteine + sodium acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium DW378
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
P16703
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
Streptomyces lavendulae, Streptomyces lavendulae ATCC 11924
D2Z027
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
show the reaction diagram
Streptomyces lavendulae, Streptomyces lavendulae ATCC 11924
D2Z027
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetyl-L-serine + sulfide
L-Cys + acetate
show the reaction diagram
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
-
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + sodium acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate
show the reaction diagram
Streptomyces lavendulae, Streptomyces lavendulae ATCC 11924
D2Z027
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 + H+
show the reaction diagram
-
-
-
-
?
O-acetyl-Ser + selenide
selenocysteine + acetate
show the reaction diagram
-
maximal 40% rate of cysteine synthesis
-
?
O-acetylhomoserine + H2S
homocysteine + ?
show the reaction diagram
-
-
-
?
O-acetylhomoserine + H2S
homocysteine + ?
show the reaction diagram
-
not, low molecular weight enzyme
-
-
-
O-acetylhomoserine + H2S
homocysteine + ?
show the reaction diagram
-
2.4% of the activity with O-acetyl-L-Ser
-
-
?
O-diazoacetyl-L-serine + sulfide
?
show the reaction diagram
-
44% of the activity with O-acetyl-Ser
-
-
?
O-phosphoserine + H2S
L-Cys + phosphate
show the reaction diagram
-
-
-
-
?
O-succinyl-L-homoserine + sulfide
?
show the reaction diagram
-
3.6% of the activity with O-acetyl-L-serine
-
-
?
O3-acetyl-L-serine
alpha-aminoacrylate
show the reaction diagram
-
-
in absence of S2- and at 50C, not below
-
?
O3-acetyl-L-serine + 2-nitro-5-thiobenzoate
?
show the reaction diagram
-
-
-
-
?
O3-acetyl-L-serine + 2-nitro-5-thiobenzoate
?
show the reaction diagram
-
-
-
-
?
O3-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
show the reaction diagram
-
-
-
-
?
O3-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium DW378
-
-
-
-
?
O3-acetyl-L-serine + benzylmercaptan
S-benzyl-L-cysteine + acetate
show the reaction diagram
Q845F9
-
-
-
?
O3-acetyl-L-serine + cyanide
beta-cyano-L-alanine + acetate
show the reaction diagram
Q845F9
-
-
-
?
O3-acetyl-L-serine + ethylmercaptan
S-ethyl-L-cysteine + acetate
show the reaction diagram
Q845F9
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-, P45040
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-, Q9YBL2
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
Q845F9
970% of the activity with cyanide
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-, 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
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium DW378
-
-
-
-
?
O3-acetyl-L-serine + hydrogensulfide
L-cysteine + acetate
show the reaction diagram
-
-
-
-
?
O3-acetyl-L-serine + methylmercaptan
S-methyl-L-cysteine + acetate
show the reaction diagram
Q845F9
-
-
-
?
O3-acetyl-L-serine + phenol
O-phenyl-L-serine + acetate
show the reaction diagram
Q845F9
-
-
-
?
O3-acetyl-L-serine + phenylmercaptan
S-phenyl-L-cysteine + acetate
show the reaction diagram
Q845F9
-
-
-
?
O3-acetyl-L-serine + propylmercaptan
S-propyl-L-cysteine + acetate
show the reaction diagram
Q845F9
-
-
-
?
O3-acetyl-L-serine + sulfide
L-cysteine + acetate
show the reaction diagram
-
-
-
-
?
Ser + sulfide
?
show the reaction diagram
-
1.8% of the activity with O-acetyl-L-serine
-
-
?
L-homoserine + sulfide
?
show the reaction diagram
-
1.6% of the activity with O-acetyl-L-serine
-
-
?
additional information
?
-
-
isoenzyme 1 and 2 have different substrate specificities towards various beta-substituted L-Cys
-
-
-
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
?
-
-
beta-substituted alanines, low activity
-
-
-
additional information
?
-
-
beta-substituted alanines, low activity
-
-
-
additional information
?
-
-
beta-substituted alanines, low activity
-
-
-
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
?
-
Q845F9
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
?
-
-
preferred state of sulfide is hydrogen sulfide
-
-
-
additional information
?
-
-
the enzyme is induced by Al3+. Cysteine synthase may be a key player during Al response/adaptation in rice
-
-
-
additional information
?
-
-, Q2PZM5
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
-
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
?
-
-
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
?
-
-, P45040
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
?
-
E5LPF4, -
no substrates: serine, phosphoserine, O-succinylhomoserine, thiosulfate
-
-
-
additional information
?
-
-, Q9YBL2
the enzyme also catalyzes the reaction of EC 2.5.1.65, O-phosphoserine hydrolase
-
-
-
additional information
?
-
Azospirillum brasilense Sp7
Q2PZM5
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cysteine + CN-
cyanoalanine + H2S
show the reaction diagram
Xanthium pennsylvanicum
-
involved in cyanide metabolism during seed germination
-
-
-
L-Cys + acetate
?
show the reaction diagram
-
involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear
-
-
-
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
O81154, O81155, -
OASTL activity regulates not only Cys de novo synthesis but also its homeostasis
-
-
?
O-acetyl-L-Ser + isoxazylin-5-one
?
show the reaction diagram
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
-
O-acetyl-L-Ser + S2O32-
S-sulfocysteine + ?
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + sodium thiosulfate
?
show the reaction diagram
Staphylococcus aureus, Staphylococcus aureus SH1000
-
-
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
-
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
-
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
-
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
-
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
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
show the reaction diagram
-
key role in metabolism of S-containing amino acids
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
activity varies between sulfur sources, enzyme formation regulated by L-Cys concentration
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
involved in synthesis of antioxidants such as glutathione during fruit development
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
involved in glutathione formation
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
enzyme transcription repressed by L-cystine, derepressed by limiting sulfide concentrations
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
functions as a Cys synthase rather than as a homocysteine synthase in vivo
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
controlled by feedback inhibition, adaptively significant as sulfide removal mechanism
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
repressed during growth with sulfide or thiosulfide as sulfur source
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
involved in thiosulfate assimilation
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
final step in Cys synthesis
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
Synechococcus sp., Synechococcus sp. 6301
-
last step of assimilatory sulfate reduction
-
-
-
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
P16703
-
-
-
?
O3-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
show the reaction diagram
-
-
-
-
?
O3-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium DW378
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-, P45040
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-, 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
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium DW378
-
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
show the reaction diagram
-
the side reaction of the enzyme seems to contribute massively to the total H2S release of higher plants at least at higher pH values
-
-
-
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
?
-
-
the enzyme is induced by Al3+. Cysteine synthase may be a key player during Al response/adaptation in rice
-
-
-
additional information
?
-
-, Q2PZM5
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
-
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
?
-
-
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
?
-
Azospirillum brasilense Sp7
Q2PZM5
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
4 per cysteine synthase complex
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
-
-
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
-
restores activity after dialysis against cysteine
pyridoxal 5'-phosphate
-
0.75 mol per mol subunit
pyridoxal 5'-phosphate
-
one per subunit
pyridoxal 5'-phosphate
-
one per subunit
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
protects against inactivation
pyridoxal 5'-phosphate
-
one per subunit
pyridoxal 5'-phosphate
-
responsible for O-acetylserine binding
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
-
1.1 mol per mol subunit
pyridoxal 5'-phosphate
-
Lys involved in cofactor binding
pyridoxal 5'-phosphate
-
Km of the cofactor at pH 8.0: 0.029 mM
pyridoxal 5'-phosphate
-
enzyme contains 1.2 pyridoxal phosphate per subunit
pyridoxal 5'-phosphate
-
enzyme contains pyridoxal phosphate
pyridoxal 5'-phosphate
-
enzyme contains pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
dependent on
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
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
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
-, Q9YBL2
crystallization data
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
slight activation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(NH4)6Mo7O24
-
1 mM, 97% inhibition
(NH4)6Mo7O24
-
1 mM, 61% loss of activity
1,10-phenanthroline
-
14% inhibition at 1 mM
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
-, P0A534
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
-, P0A534
minimum inhibitory concentration against Mycobacterium tuberculosis 0.0321 mM, cytotoxicity against HEK 293T cell 0.2% at 0.025 mM
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
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
non-competitive
5,5'-dithiobis(2-nitrobenzoic acid)
-
1 mM, 92% inactivation
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
-, P0A534
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
-, P0A534
minimum inhibitory concentration against Mycobacterium tuberculosis 0.0076 mM, cytotoxicity against HEK 293T cell 5.7% at 0.025 mM
AgNO3
-
1 mM, 22% inhibition
AgNO3
-
1 mM, complete loss of activity
Aminooxyacetate
-
57% and 64% inhibition at 1 mM, isoenzymes 1 and 2, respectively
Aminooxyacetate
-
10 mM, 76% inhibition
cadmium chloride
-
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
-
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
-
Cd2+
-
55% inhibition at 1 mM
chloroalanine
-
substrate inhibition
Co2+
-
complete inhibition at 1 mM
copper sulfate
-
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
-
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
-
CuSO4
-
1 mM, 99% loss of activity
cystathionine
-
competitive to sulfide
cystathionine
-
-
cystathionine
-
91% inhibition at 10 mM
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
-
EDTA
-
1 mM, 16% inhibition
FeSO4
-
1 mM, 96% inhibition
FeSO4
-
1 mM, 99% loss of activity
hydroxylamine
-
-
hydroxylamine
-
31% inhibition at 1 mM
hydroxylamine
-
complete inhibition at 10 mM, isoenzymes 1 and 2, 90% inhibition at 10 mM, isoenzyme 3
hydroxylamine
-
35% and 48% inhibition at 5 mM, isoenzymes 1 and 2, respectively
hydroxylamine
-
57% loss of activity at 10 mM, isoenzyme 1'
hydroxylamine
-
10 mM, 71.2% inhibition
iodoacetamide
-
1 mM, 48% loss of activity
KCN
-
15.6% inhibition by 1 mM
L-cysteine
-
non-competitive
L-cysteine
-
-
L-cysteine
-
66% inhibition at 10 mM
L-cysteine
-
35% inhibition at 4.5 mM
L-cysteine
-
28-41% inhibition at 4.5 mM, isoenzyme-dependent
L-cysteine
-
50% inhibition at 5 mM, only isoenzyme 1
L-cysteine
-
substrate inhibition
L-homocysteine
-
competitive to sulfide
L-homoserine
-
-
L-homoserine
-
non-competitive
lead nitrate
-
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
-
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
-
competitive to sulfide
methionine
-
slight inhibition
methionine
-
competitive to sulfide
methionine
-
46% and 37% inhibition at 1 mM, isoenzymes 1 and 2, respectively
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
MNYDI
-
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
NEM
-
non-competitive
Ni2+
-
complete inhibition at 1 mM
O-acetylserine
-
above 72 mM
O-acetylserine
-
at 150 mM
O-acetylserine
-
substrate inhibition
O-acetylserine
-
-
O-acetylserine
-
substrate inhibition
p-chloromercuribenzoate
-
non-competitive
p-chloromercuribenzoate
-
40% inhibition at 1 mM
p-chloromercuribenzoate
-
14% and 4% inhibition at 1 mM, isoenzymes 1 and 2, respectively
p-chloromercuribenzoate
-
1 mM, 59% inhibition
p-Chloromercuriphenylsulfonic acid
-
46% inhibition at 1 mM
p-hydroxymercuribenzoate
-
-
PCMB
-
1 mM, 97% loss of activity
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
phenylhydrazine
-
73% inhibition by 1 mM, 97.4% inhibition by 10 mM
pyridoxal hydrochloride
-
54% inhibition at 1 mM
S-methylcysteine
-
slight inhibition
S-sulfocysteine
-
52% inhibition at 4.5 mM
S-sulfocysteine
-
24% inhibition at 4.5 mM, isoenzyme 1
S-sulfocysteine
-
26% loss of activity at 5 mM
Semicarbazide
-
60% loss of activity at 1 mM
Semicarbazide
-
13% inhibition by 1 mM, 38.6% inhibition by 10 mM
serine
-
competitive to O-acetylserine
serine acetyltransferase
-
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
-
SO32-
-
competitive to sulfide
Sodium arsenite
-
plants grown in the presence of 0.0267 mM sodium arsenite show 109% increase in activity in leaves, and 238% increase in activity in root, respectively
Sodium arsenite
-
plants grown in the presence of 0.0267 mM sodium arsenite show 108% increase in activity in leaves, and 250% increase in activity in root, respectively; plants grown in the presence of 0.0267 mM sodium arsenite show 120% increase in activity in leaves
Sodium borohydride
-
59% inhibition at 1 mM
Sulfide
-
above 107 mM
-
Sulfide
-
-
-
Sulfide
-
above 200 mM
-
Sulfide
-
substrate inhibition
-
Sulfide
-
-
-
Thiourea
-
34% inhibition at 1 mM
Zn2+
-
95% inhibition at 1 mM
Zn2+
-
1 mM, 94% inhibition
ZnCl2
-
1 mM, 88% loss of activity
Monoiodoacetic acid
-
1 mM, complete inactivation
additional information
-
partial inhibition of enzyme upon complex formation with serine acetyltransferase
-
additional information
E5LPF4, -
presence of 4% NaCl is not inhibitory
-
additional information
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
slight activation
iodoacetamide
-
slight activation
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.018
-
5-thio-2-nitrobenzoate
-
mutant W50Y, pH 7.0, 20C
0.049
-
5-thio-2-nitrobenzoate
-
wild-type, pH 7.0, 20C
0.061
-
5-thio-2-nitrobenzoate
-
mutant W161Y, pH 7.0, 20C
0.07
-
5-thio-2-nitrobenzoate
-
K120Q mutant with 9fold decrease compared to wild type, 100 mM MES, pH 6.5, 0.5 mM O3-acetyl-L-serine, 25C; mutant H52A, pH 6.5
0.12
-
5-thio-2-nitrobenzoate
-
pH 7.0, 50C
0.6
-
5-thio-2-nitrobenzoate
-
wild type, 100 mM HEPES, pH 7.0, 0.5 mM O3-acetyl-L-serine, 25C; wild-type, pH 7.0
0.6
-
5-thio-2-nitrobenzoate
-
wild type, 100 mM HEPES, pH 7.0, 0.5 mM O3-acetyl-L-serine, 25C
2.5
-
5-thio-2-nitrobenzoate
-
H152A mutant with 4.1fold increase compared to wild type, 100 mM MES, pH 6.5, 0.5 mM O3-acetyl-L-serine, 25C; mutant H52A, pH 6.5
0.785
-
chloroalanine
-
pH 8.0, 26C, cysteine synthase B
1.053
-
chloroalanine
-
pH 8.0, 26C, cysteine synthase A
14.2
-
CN-
-
pH 8.5, enzyme form PCS-1
15.1
-
CN-
-
pH 8.5, enzyme form PCS-2
0.0384
-
cysteine
-
pH 8.5, enzyme form PCS-2
0.0512
-
cysteine
-
pH 8.5, enzyme form PCS-1
0.0526
-
cysteine
-
pH 7.5, 37C, isoenzyme C
0.0986
-
cysteine
-
isoenzyme A
0.108
-
cysteine
-
pH 8.0, 26C, cysteine synthase A
0.113
-
cysteine
-
pH 7.5, 37C, isoenzyme B
0.201
-
cysteine
-
pH 8.0, 26C, cysteine synthase B
0.7
-
dithiothreitol
E5LPF4, -
pH 7.4, 37C
6.7
-
H2S
E5LPF4, -
pH 7.4, 37C
0.12
-
hydrogen sulfide
D2Z027
30C, pH 8.0
-
3
-
hydrogen sulfide
-
isoform B, pH 7.5, 25C, Michaelis-Menten kinetics
-
3.2
-
hydrogen sulfide
-
isoform B, pH 7.5, 25C, Hill equation, Hill coefficient 0.75
-
4.6
-
hydrogen sulfide
-
isoform C, pH 7.5, 25C, Hill equation, Hill coefficient 1.05
-
4.7
-
hydrogen sulfide
-
isoform C, pH 7.5, 25C, Michaelis-Menten kinetics
-
5.6
-
hydrogen sulfide
-
isoform A, pH 7.5, 25C, Michaelis-Menten kinetics
-
6.4
-
hydrogen sulfide
-
isoform A, pH 7.5, 25C, Hill equation, Hill coefficient 0.81
-
0.7
-
L-Cys
E5LPF4, -
pH 7.4, 37C
0.8
-
L-Cys
-
37C, pH 7.8
0.25
-
L-cysteine
Q845F9
pH 7.5, 45C
0.029
-
Na2S
-
37C, pH 7.8, cosubstrate: O-phosphoserine
0.8
-
Na2S
-
37C, pH 7.8, cosubstrate: O-acetyl-L-Ser
5.2
-
NaCN
-
pH 7.4, 30C
2.3
-
NaN3
-
pH 7.6, 25C
0.037
-
O-acetyl-L-Ser
-
pH 6.8, 37C
0.045
-
O-acetyl-L-Ser
Xanthium pennsylvanicum
-
,isoenzyme 3
0.05
-
O-acetyl-L-Ser
Xanthium pennsylvanicum
-
isoenzymes 1 and 2
0.373
-
O-acetyl-L-Ser
Xanthium pennsylvanicum
-
,isoenzyme 2
0.547
-
O-acetyl-L-Ser
Xanthium pennsylvanicum
-
,isoenzyme 3
0.6
-
O-acetyl-L-Ser
E5LPF4, -
pH 7.4, 37C
0.64
-
O-acetyl-L-Ser
-
pH 7.5, 25C, recombinant free enzyme
0.7
-
O-acetyl-L-Ser
-
pH 7.5, 37C, isoenzyme 1 and 2
0.7
-
O-acetyl-L-Ser
-
pH 7.5, 37C, isoenzyme B
1
-
O-acetyl-L-Ser
-
pH 7.4, 37C, isoenzyme 1
1.29
-
O-acetyl-L-Ser
Xanthium pennsylvanicum
-
isoenzyme 1
1.3
-
O-acetyl-L-Ser
-
pH 6.8, 36C
1.3
-
O-acetyl-L-Ser
-
pH 7.5, 25C, chloroplast enzyme
1.3
-
O-acetyl-L-Ser
-
-
1.5
-
O-acetyl-L-Ser
-
pH 8.0, 30C, isoenzyme 2
2
-
O-acetyl-L-Ser
-
pH 7.5, 50C
2
-
O-acetyl-L-Ser
-
-
2.1
-
O-acetyl-L-Ser
-
pH 8.0, 30C, isoenzyme 1
2.1
-
O-acetyl-L-Ser
-
formation of beta-(isoxazylin5-on-4-yl)-L-alanine
2.1
-
O-acetyl-L-Ser
-
pH 7.5, 37C, isoenzyme A
2.17
-
O-acetyl-L-Ser
-
-
2.3
-
O-acetyl-L-Ser
-
pH 8.0, 30C, isoenzyme 2
2.5
-
O-acetyl-L-Ser
-
pH 8.0, 30C
2.6
-
O-acetyl-L-Ser
-
pH 8.0, 30C, isoenzyme 1
2.7
-
O-acetyl-L-Ser
-
pH 7.5, 30C
2.9
-
O-acetyl-L-Ser
-
isoenzyme 1
2.9
-
O-acetyl-L-Ser
-
pH 8.0, 30C
3.1
-
O-acetyl-L-Ser
-
pH 7.8, 35C
3.5
-
O-acetyl-L-Ser
-
pH 7.8, 35C
3.57
-
O-acetyl-L-Ser
-
pH 8.0, 25C, isoenzyme 1
3.8
-
O-acetyl-L-Ser
-
formation of beta-(isoxazylin5-on-2-yl)-L-alanine
3.9
-
O-acetyl-L-Ser
-
pH 7.5, 37C, isoenzyme C
4.28
-
O-acetyl-L-Ser
-
pH 7.5, 25C, recombinant complex-bound enzyme
4.8
-
O-acetyl-L-Ser
-
pH 7.5, 25C, free enzyme
4.8
-
O-acetyl-L-Ser
-
pH 7.8, 50C
5
-
O-acetyl-L-Ser
-
free enzyme; independent of sulfide concentration; pH 7.2-7.4, 25C
5.12
-
O-acetyl-L-Ser
-
pH 7.8
5.26
-
O-acetyl-L-Ser
-
pH 8.0, 25C, isoenzyme 3
5.56
-
O-acetyl-L-Ser
-
pH 8.0, 25C, isoenzyme 2
6.7
8.3
O-acetyl-L-Ser
-
pH 7.4, 30C, cosubstrate-dependent
8.2
-
O-acetyl-L-Ser
-
pH 7.6, 25C
8.3
-
O-acetyl-L-Ser
-
pH 8.0, 25, isoenzyme 1'
9
-
O-acetyl-L-Ser
-
isoenzyme 2
9.6
-
O-acetyl-L-Ser
-
pH 7.5, 50C, isoenzyme 1 and 2
15
-
O-acetyl-L-Ser
-
pH 7.4, 37C, isoenzyme 2
20
-
O-acetyl-L-Ser
-
complex-bound enzyme
24
-
O-acetyl-L-Ser
-
synthesis of S-sulfo-L-cysteine
27
-
O-acetyl-L-Ser
-
pH 7.5, 25C, enzyme bound to serine acetyltransferase
28
-
O-acetyl-L-Ser
-
sulfhydrylation of O-acetyl-L-serine
39.5
-
O-acetyl-L-Ser
-
37C, pH 7.8
50
-
O-acetyl-L-Ser
-
isoenzyme 2
0.063
-
O-Acetyl-L-serine
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
-
0.105
-
O-Acetyl-L-serine
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
-
0.11
-
O-Acetyl-L-serine
-
mutant H52A, pH 6.5
0.116
-
O-Acetyl-L-serine
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
-
0.355
-
O-Acetyl-L-serine
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
-
0.46
-
O-Acetyl-L-serine
-
-
0.6
-
O-Acetyl-L-serine
-
mutant T68S, 37C
0.7
-
O-Acetyl-L-serine
-
wild-type, 37C
1
-
O-Acetyl-L-serine
-
mutant H52A, pH 6.5
1.83
-
O-Acetyl-L-serine
-
pH 7.5, enzyme form PCS-2
2.99
-
O-Acetyl-L-serine
-
pH 7.5, enzyme form PCS-1
15
-
O-Acetyl-L-serine
-
wild-type, pH 7.0
6.67
-
O-acetylhomoserine
-
-
1.03
-
O-acetylserine
-
pH 8.0, 26C, cysteine synthase B
1.355
-
O-acetylserine
-
pH 8.0, 26C, cysteine synthase A
227
-
O-phosphoserine
-
37C, pH 7.8
0.11
-
O3-Acetyl-L-serine
-
H152A mutant with 136fold decrease compared to wild type, 100 mM MES, pH 6.5, 50 microM 5-thio-2-nitrobenzoate (TNB), 25C
0.31
-
O3-Acetyl-L-serine
-
isoform B, pH 7.5, 25C, Michaelis-Menten kinetics
0.32
-
O3-Acetyl-L-serine
-
isoform B, pH 7.5, 25C, Hill equation, Hill coefficient 1.03
0.36
-
O3-Acetyl-L-serine
-
pH 7.0, 50C
0.43
-
O3-Acetyl-L-serine
-
isoform C, pH 7.5, 25C, Michaelis-Menten kinetics
0.51
-
O3-Acetyl-L-serine
-
isoform C, pH 7.5, 25C, Hill equation, Hill coefficient 0.86
0.57
-
O3-Acetyl-L-serine
-
mutant S269A, pH 7.0, 25C
0.66
-
O3-Acetyl-L-serine
-
isoform A, pH 7.5, 25C, Hill equation, Hill coefficient 1.05
0.68
-
O3-Acetyl-L-serine
-
mutant T78A, pH 7.0, 25C
0.69
-
O3-Acetyl-L-serine
-
isoform A, pH 7.5, 25C, Michaelis-Menten kinetics
0.749
-
O3-Acetyl-L-serine
-
wild-type, pH 7.0, 20C
0.774
-
O3-Acetyl-L-serine
-
mutant W50Y, pH 7.0, 20C
0.82
-
O3-Acetyl-L-serine
-
mutant T78S, pH 7.0, 25C
0.91
-
O3-Acetyl-L-serine
-
mutant H157Q, pH 7.0, 25C
0.94
-
O3-Acetyl-L-serine
-
mutant H157N, pH 7.0, 25C
0.96
-
O3-Acetyl-L-serine
-
mutant S269T, pH 7.0, 25C
1
-
O3-Acetyl-L-serine
-
K120Q mutant with 15fold decrease compared to wild type, 100 mM MES, pH 6.5, 50 microM 5-thio-2-nitrobenzoate (TNB), 25C
1.2
-
O3-Acetyl-L-serine
-
mutant S75T, pH 7.0, 25C; mutant T182A, pH 7.0, 25C
1.4
-
O3-Acetyl-L-serine
-
wild-type, pH 7.0, 25C
1.5
-
O3-Acetyl-L-serine
-
mutant T185A, pH 7.0, 25C; mutant T74S, pH 7.0, 25C
1.6
-
O3-Acetyl-L-serine
-
mutant S75A, pH 7.0, 25C; mutant T182S, pH 7.0, 25C; mutant T185S, pH 7.0, 25C; mutant T74A, pH 7.0, 25C
1.771
-
O3-Acetyl-L-serine
-
mutant W161Y, pH 7.0, 20C
2
-
O3-Acetyl-L-serine
-
mutant S75N, pH 7.0, 25C
3.8
-
O3-Acetyl-L-serine
-
mutant Q147S, pH 7.0, 25C
4.4
-
O3-Acetyl-L-serine
-
mutant Q147A, pH 7.0, 25C
4.7
-
O3-Acetyl-L-serine
-
mutant N77A, pH 7.0, 25C
7
-
O3-Acetyl-L-serine
-
37C, pH 9.0
10.2
-
O3-Acetyl-L-serine
-
mutant N77D, pH 7.0, 25C
15
-
O3-Acetyl-L-serine
-
wild type, 100 mM HEPES, pH 7.0, 50 microM 5-thio-2-nitrobenzoate (TNB), 25C
16
-
O3-Acetyl-L-serine
Q845F9
pH 7.5, 45C
0.006
-
S2-
-
pH 7.5, 25C, free enzyme
0.013
-
S2-
-
pH 7.5, 25C, enzyme bound to serine acetyltransferase
0.022
-
S2-
-
pH 8.0, 30C
0.033
-
S2-
-
pH 8.0, 30C, isoenzyme 1
0.033
-
S2-
-
pH 7.8, 35C
0.038
-
S2-
-
pH 7.8, 35C, isoenzyme 2
0.043
-
S2-
-
pH 8.0, 30C
0.05
-
S2-
-
pH 7.8, 50C
0.24
-
S2-
-
pH 7.8, 35 C
0.25
-
S2-
-
pH 7.5, 25C
0.25
-
S2-
-
pH 7.5, 25C, chloroplast enzyme
0.37
-
S2-
-
pH 7.0, 25C, recombinant free enzyme
0.4
-
S2-
-
pH 7.4, 37C, enzyme 1
0.5
-
S2-
-
pH 7.4, 30C
0.51
-
S2-
-
pH 7.8, 35C
0.55
-
S2-
-
pH 7.5, 25C, recombinant complex-bound enzyme
0.55
-
S2-
-
pH 8.0, 25C, isoenzyme 1
0.59
-
S2-
-
pH 6.8, 37C
0.6
-
S2-
-
isoenzyme 1 and 2
0.66
-
S2-
-
pH 8.0, 25, isoenzyme 1'
0.75
-
S2-
-
pH 7.5, 50C
0.8
-
S2-
-
pH 7.5, 37C, isoenzyme 1 and 2
0.998
-
S2-
-
pH 7.5, enzyme form PCS-2
1.25
-
S2-
-
pH 8.0, 25C, isoenzyme 2
1.57
-
S2-
-
pH 7.5, enzyme form PCS-1
1.6
-
S2-
-
pH 7.4, 37C, isoenzyme 2
2.5
-
S2-
-
pH 8.0, 25C, isoenzyme 3
5.2
-
S2-
-
pH 7.5, 50C, isoenzyme 1 and 2
0.133
-
sodium thiosulfate
-
-
0.031
-
Sulfide
-
37C, pH 9.0
-
0.062
-
Sulfide
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
-
-
0.11
-
Sulfide
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
;
-
0.18
-
Sulfide
-
mutant N77D, pH 7.0, 25C
-
0.21
-
Sulfide
-
mutant S75T, pH 7.0, 25C
-
0.22
-
Sulfide
-
mutant T182S, pH 7.0, 25C; mutant T185A, pH 7.0, 25C; wild-type, pH 7.0, 25C
-
0.23
-
Sulfide
-
mutant N77A, pH 7.0, 25C
-
0.27
-
Sulfide
-
mutant Q147S, pH 7.0, 25C
-
0.3
-
Sulfide
-
mutant H157Q, pH 7.0, 25C; mutant T78S, pH 7.0, 25C
-
0.36
-
Sulfide
-
mutant T185S, pH 7.0, 25C
-
0.39
-
Sulfide
-
mutant T182A, pH 7.0, 25C
-
0.4
-
Sulfide
-
mutant H157N, pH 7.0, 25C
-
0.44
-
Sulfide
-
mutant T78A, pH 7.0, 25C
-
0.53
-
Sulfide
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
-
-
0.54
-
Sulfide
-
mutant S269A, pH 7.0, 25C
-
1.6
-
Sulfide
-
mutant S269T, pH 7.0, 25C
-
1.7
-
Sulfide
-
mutant Q147A, pH 7.0, 25C
-
3.2
-
Sulfide
-
mutant T74S, pH 7.0, 25C
-
3.9
-
Sulfide
-
mutant T74A, pH 7.0, 25C
-
4.6
-
Sulfide
-
mutant S75A, pH 7.0, 25C
-
5.7
-
Sulfide
-
mutant S75N, pH 7.0, 25C
-
0.93
-
thiosulfate
-
-
21
-
thiosulfate
-
synthesis of S-sulfo-L-cysteine
22
-
thiosulfate
D2Z027
30C, pH 8.0
additional information
-
additional information
-
-
-
additional information
-
additional information
-
various methods compared
-
additional information
-
additional information
-
Hill numbers
-
additional information
-
additional information
-
cysteine-forming activity 245 times greater than beta-cyanoalanine-forming activity
-
additional information
-
additional information
-
activity varies between sulfur sources
-
additional information
-
additional information
-
not significantly altered by immobilization
-
additional information
-
additional information
-
no Michaelis-Menten-kinetics
-
additional information
-
additional information
-
positive kinetic cooperativity with respect to O-acetylserine in the presence of sulfide
-
additional information
-
additional information
-
HPLC method for product quantification
-
additional information
-
additional information
P0A1E3, P29848
the B-isozyme has a an about 10fold lower Km for O-acetyl-L-serine than the A-isoenzyme; the B-isozyme has a an about 10fold lower Km for O-acetyl-L-serine than the A-isoenzyme
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
154
-
beta-chloro-L-alanine
-
pH 7.0, 50C
12
-
hydrogen sulfide
D2Z027
30C, pH 8.0
-
24
-
O-acetyl-L-Ser
-
synthesis of S-sulfo-L-cysteine
153
-
O-acetyl-L-Ser
-
37C, pH 7.8
202
-
O-acetyl-L-Ser
-
sulfhydrylation of O-acetyl-L-serine
11
-
O-Acetyl-L-serine
-
mutant T68S, 37C
24
-
O-Acetyl-L-serine
-
wild-type, 37C
165
-
O-phosphoserine
-
37C, pH 7.8
0.01
-
O3-Acetyl-L-serine
-
turnover for mutant K120Q is decreased 56fold compared to wild type, 25C, 100 mM HEPES, pH 7.0
0.06
-
O3-Acetyl-L-serine
-
the turnover for H152A mutant is decreased 9fold compared to the wild type, 25C, 100 mM MES, pH 6.5
0.08
-
O3-Acetyl-L-serine
-
mutant T74A, pH 7.0, 25C
0.09
-
O3-Acetyl-L-serine
-
mutant S75N, pH 7.0, 25C
0.19
-
O3-Acetyl-L-serine
-
mutant Q147S, pH 7.0, 25C
0.34
-
O3-Acetyl-L-serine
-
mutant N77D, pH 7.0, 25C
0.56
-
O3-Acetyl-L-serine
-
25C, 100 mM HEPES, pH 7.0
0.56
-
O3-Acetyl-L-serine
-
wild type, 25C, 100 mM HEPES, pH 7.0
1.07
-
O3-Acetyl-L-serine
-
mutant T185A, pH 7.0, 25C
3.11
-
O3-Acetyl-L-serine
-
mutant T185S, pH 7.0, 25C
4.02
-
O3-Acetyl-L-serine
-
mutant Q147A, pH 7.0, 25C
7.16
-
O3-Acetyl-L-serine
-
mutant S75A, pH 7.0, 25C
34.3
-
O3-Acetyl-L-serine
-
mutant S269A, pH 7.0, 25C
51.5
-
O3-Acetyl-L-serine
-
mutant S75T, pH 7.0, 25C
238
-
O3-Acetyl-L-serine
-
37C, pH 9.0
312
-
O3-Acetyl-L-serine
-
pH 7.0, 50C
403
-
O3-Acetyl-L-serine
-
mutant N77A, pH 7.0, 25C
456
-
O3-Acetyl-L-serine
-
mutant T74S, pH 7.0, 25C
554
-
O3-Acetyl-L-serine
-
mutant T78A, pH 7.0, 25C
572
-
O3-Acetyl-L-serine
-
mutant S269T, pH 7.0, 25C
775
-
O3-Acetyl-L-serine
-
mutant T78S, pH 7.0, 25C
889
-
O3-Acetyl-L-serine
-
mutant T182A, pH 7.0, 25C
1055
-
O3-Acetyl-L-serine
-
mutant H157Q, pH 7.0, 25C
1520
-
O3-Acetyl-L-serine
-
mutant H157N, pH 7.0, 25C
1660
-
O3-Acetyl-L-serine
-
mutant T182S, pH 7.0, 25C
1780
-
O3-Acetyl-L-serine
-
wild-type, pH 7.0, 25C
202
-
S2-
-
sulfhydrylation of O-acetyl-L-serine
0.22
-
Sulfide
-
mutant Q147S, pH 7.0, 25C
-
0.42
-
Sulfide
-
mutant T74A, pH 7.0, 25C
-
0.73
-
Sulfide
-
mutant N77D, pH 7.0, 25C
-
1.44
-
Sulfide
-
mutant T185A, pH 7.0, 25C
-
1.45
-
Sulfide
-
mutant S75N, pH 7.0, 25C
-
5.57
-
Sulfide
-
mutant T185S, pH 7.0, 25C
-
12.5
-
Sulfide
-
mutant Q147A, pH 7.0, 25C
-
20.2
-
Sulfide
-
mutant S75A, pH 7.0, 25C
-
29.5
-
Sulfide
-
mutant S269A, pH 7.0, 25C
-
82.7
-
Sulfide
-
mutant S75T, pH 7.0, 25C
-
155
-
Sulfide
-
mutant N77A, pH 7.0, 25C
-
370
-
Sulfide
-
mutant T78S, pH 7.0, 25C
-
537
-
Sulfide
-
mutant T78A, pH 7.0, 25C
-
929
-
Sulfide
-
mutant S269T, pH 7.0, 25C
-
1600
-
Sulfide
-
mutant T182A, pH 7.0, 25C
-
1690
-
Sulfide
-
mutant T182S, pH 7.0, 25C
-
1700
-
Sulfide
-
mutant T74S, pH 7.0, 25C
-
1780
-
Sulfide
-
mutant H157Q, pH 7.0, 25C
-
1990
-
Sulfide
-
mutant H157N, pH 7.0, 25C
-
2170
-
Sulfide
-
wild-type, pH 7.0, 25C
-
0.72
-
thiosulfate
D2Z027
30C, pH 8.0
24
-
thiosulfate
-
synthesis of S-sulfo-L-cysteine
6.6
-
L-Cys
-
37C, pH 7.8
additional information
-
additional information
P0A1E3, P29848
the B-isozyme has a turnover number 12.5fold higher than the A-isozyme; the B-isozyme has a turnover number 12.5fold higher than the A-isozyme
-
additional information
-
additional information
-
wild type and mutant exhibit almost identical values for sulfide as substrate, imidazole has no effect on the activity of wild type or H152A mutant enzyme
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0219
-
5-thio-2-nitrobenzoate
-
H152A mutant with 43fold decrease compared to wild type, 100 mM MES, pH 6.5, 0.5 mM O3-acetyl-L-serine, 25C
222648
0.141
-
5-thio-2-nitrobenzoate
-
K120Q mutant with 6.7fold decrease compared to wild type value, 100 mM MES, pH 6.5, 0.5 mM O3-acetyl-L-serine, 25C
222648
0.95
-
5-thio-2-nitrobenzoate
-
wild type, 100 mM HEPES, pH 7.0, 0.5 mM O3-acetyl-L-serine, 25C
222648
100
-
hydrogen sulfide
D2Z027
30C, pH 8.0
0
0.14
-
O-Acetyl-L-serine
D2Z027
30C, pH 8.0, cosubstrate: hydrogen sulfide
14635
0.15
-
O-Acetyl-L-serine
-
mutant F143D
14635
0.38
-
O-Acetyl-L-serine
-
mutant F143S
14635
0.95
-
O-Acetyl-L-serine
-
mutant F143A
14635
15
-
O-Acetyl-L-serine
-
wild-type
14635
0.01
-
O3-Acetyl-L-serine
-
K120Q mutant with 3.7fold decrease compared to wild type value, 100 mM MES, pH 6.5, 50 microM 5-thio-2-nitrobenzoate (TNB), 25C
14743
0.037
-
O3-Acetyl-L-serine
-
wild type, 100 mM HEPES, pH 7.0, 50 microM 5-thio-2-nitrobenzoate (TNB), 25C
14743
0.51
-
O3-Acetyl-L-serine
-
H152A mutant with 14fold increase compared to wild type, 100 mM MES, pH 6.5, 50 microM 5-thio-2-nitrobenzoate (TNB), 25C
14743
0.033
-
thiosulfate
D2Z027
30C, pH 8.0
17167
0.19
-
L-homocysteine
D2Z027
30C, pH 8.0
12250
additional information
-
additional information
-
wild type and mutant exhibit almost identical values for sulfide as substrate
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.63
-
5,5'-dithiobis(2-nitrobenzoic) acid
-
pH 6.8, 37 C
160
-
acetate
-
pH 7.5, 25 C, free enzyme
340
-
acetate
-
pH 7.5, 25 C, enzyme bound to serine acetyltransferase
0.8
-
chloroalanine
-
pH 9.8, 26 C, cysteine synthase B
1.135
-
chloroalanine
-
pH 9.8, 26 C, cysteine synthase A
5.546
-
chloroalanine
-
pH 8.0, 26 C, cysteine synthase B
70.92
-
chloroalanine
-
pH 8.0, 26 C, cysteine synthase A
2.113
-
cysteine
-
pH 8.0, 26 C, cysteine synthase B
8.6
-
cysteine
-
pH 7.5, 25 C, free enzyme
48
-
cysteine
-
pH 7.5, 25 C, enzyme bound to serine acetyltransferase
0.004
-
DYVI
-
pH 7.8, 22C
-
2.074
-
L-cysteine
-
pH 8.0, 26 C, cysteine synthase A
2.27
-
L-cysteine
-
pH 6.8, 37 C
1.32
-
L-homoserine
-
pH 6.8, 37 C
6.5
-
L-methionine
-
pH 7.5, 50 C
1.75
-
methionine
-
pH 6.8, 37 C
1.03
-
MNDGI
-
100 mM HEPES, pH 7.0, 1 microM enzyme, 20C, steady state fluorescence titration
2.27
-
MNEGI
-
100 mM HEPES, pH 7.0, 1 microM enzyme, 20C, steady state fluorescence titration
0.0387
-
MNENI
-
100 mM HEPES, pH 7.0, 1 microM enzyme, 20C, steady state fluorescence titration
3.42
-
MNETI
-
100 mM HEPES, pH 7.0, 1 microM enzyme, 20C, steady state fluorescence titration
15.2
-
MNKGI
-
100 mM HEPES, pH 7.0, 1 microM enzyme, 20C, steady state fluorescence titration
13.3
-
MNKVI
-
100 mM HEPES, pH 7.0, 1 microM enzyme, 20C, steady state fluorescence titration
0.57
-
MNLGI
-
100 mM HEPES, pH 7.0, 1 microM enzyme, 20C, steady state fluorescence titration
0.044
-
MNLNI
-
wild type serine acetyltransferase motif, 100 mM HEPES, pH 7.0, 1 microM enzyme, 20C, steady state fluorescence titration
7.1
-
MNPHI
-
100 mM HEPES, pH 7.0, 1 microM enzyme, 20C, steady state fluorescence titration
3.33
-
MNVPI
-
100 mM HEPES, pH 7.0, 1 microM enzyme, 20C, steady state fluorescence titration
0.0249
-
MNWNI
-
100 mM HEPES, pH 7.0, 1 microM enzyme, 20C, steady state fluorescence titration
0.0258
-
MNYDI
-
100 mM HEPES, pH 7.0, 1 microM enzyme, 20C, steady state fluorescence titration
0.191
-
MNYFI
-
100 mM HEPES, pH 8.0, 1 microM enzyme, 20C, steady state fluorescence titration
1.43
-
N-ethylmaleimide
-
pH 6.8, 37 C
2.3
-
NaN3
-
pH 7.4, 25 C
7.1
-
O-acetyl-L-Ser
-
pH 7.5, 25 C, free enzyme
18
-
O-acetyl-L-Ser
-
pH 7.5, 25 C, enzyme bound to serine acetyltransferase
19.56
-
O-acetylserine
-
pH 8.0, 26 C, cysteine synthase B
32.25
-
O-acetylserine
-
pH 8.0, 26 C, cysteine synthase A
2.86
-
p-chloromercuribenzoate
-
pH 6.8, 37 C
0.011
-
S2-
-
pH 7.5, 25 C, free enzyme
0.11
-
S2-
-
pH 7.5, 25 C, enzyme bound to serine acetyltransferase
0.0608
-
MNYSI
-
100 mM HEPES, pH 7.0, 1 microM enzyme, 20C, steady state fluorescence titration
additional information
-
additional information
-
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0177
-
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
-, P0A534
pH not specified in the publication, temperature not specified in the publication
0.0227
-
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
-, P0A534
pH not specified in the publication, temperature not specified in the publication
0.0303
-
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
-, P0A534
pH not specified in the publication, temperature not specified in the publication
0.0177
-
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
-, P0A534
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0283
-
-
Cys-auxotroph strain, low molecular weight enzyme
0.262
-
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
-
0.419
-
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
-
0.489
-
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
-
0.589
-
-
low molecular weight enzyme
0.724
-
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
-
1.01
-
-
isoenzyme 2
1.36
-
-
isoenzyme 1
2.43
-
-
isoenzyme 1
6.3
-
-
strain K 12
8.1
-
-
transformed strain cysk
15.4
-
-
isoenzyme 2
46
-
-, Q9YBL2
pH 7.5, 60C
96
-
-
chloroplast enzyme
98.5
-
-
reaction with O-phosphoserine
130
-
-
isoenzyme 1
143
-
-
isoenzyme 2
172.3
-
-, Q2PZM5
-
180
-
-
reaction with O-acetyl-L-Ser
180
-
-
pH 7.8, 22C
245.6
-
-
isoenzyme 2
336
-
-
isoenzyme 1
400
-
-
isoenzyme 1
435
-
-
37C, pH 9.0
550
-
-
isoform C, pH 7.5, 25C
590
-
-
isoform B, pH 7.5, 25C
728
-
-
25C
852
-
-
isoenzyme 2
880
-
-
isoenzyme 1 and 2
900
-
-
isoform A, pH 7.5, 25C
933
-
-
isoenzyme 1
1400
-
-
isoenzyme 2
1431
-
-
isoenzyme 3
5500
-
-
-
additional information
-
-
activity depends on presence of nucleophiles
additional information
-
-
activity increased during growth on cystine, as compared to growth on sulfate
additional information
-
-
activity modified by protein-protein interactions within cystein synthase complex
additional information
-
-
cysteine and methylcysteine formation of crude leaf extracts
additional information
-
-
-
additional information
-
-
activity buffer-dependent, substrate unstable in Tris-HCl buffer
additional information
-
-
maximal activity in red fruit chromoplasts
additional information
-
-
activities of various recombinant enzymes
additional information
-
-
apo-enzyme reconstituted with cofactor pyridoxal 5'-phosphate exhibits 81.4% enzyme activity compared to the native enzyme, 100 mM HEPES, pH 7.0, with 0.2 mM O3-acetyl-L-serine, and 0.05 5-thio-2-nitrobenzoate
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.7
-
-
sulfhydrylation of O-acetyl-L-serine
6.8
-
-
phosphate buffer
7
-
-
recombinant isoenzyme C
7
-
-
assay at
7.2
-
-
isoenzyme 1
7.3
8.2
-
isoenzyme 1
7.5
-
-
isoenzyme 1', lower than isoenzymes one, two, and three
7.6
-
-
all isoenzymes
7.8
-
-
potassium phosphate buffer
8
9
-
free enzyme
8
-
-
Tris-HCl buffer
8
-
-
broad optimum around
8
-
-
recombinant isoenzyme A and B
8
-
-
assay at
8
-
D2Z027
assay at
8.1
8.8
-
synthesis of L-cystathionine
8.5
-
Xanthium pennsylvanicum
-
-
9.5
-
-
enzyme bound to serine acetyltransferase
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
8
-
about 50% of maximal activity at pH 5.5 and pH 8.0
6
10
-
pH 6: about 55% of maximal activity, pH 10.0: about 40% of maximal activity
7.3
8.2
-
isoenzyme 2
additional information
-
-
altered by immobilization
additional information
-
-
pH-rate profiles for wild type and H152A mutant with O3-acetyl-L-serine and 5-thio-2-nitrobenzoate as substrates are similar, 100 mM concentrations of 2-(N-morpholino)ethanesulfonic acid (MES), pH 5.5-6.5, 3-(N-morpholino)propanesulfonic acid (MOPS), pH 7.0-7.5, N-(2-hydroxyethyl)piperazine-N'-2-ethanesulfonic acid (HEPES), pH 8.0, and 3-[[tris(hydroxymethyl)]amino]propanesulfonic acid (TAPS), pH 9.0, titrated with KOH
additional information
-
-
pH-rate profiles for wild type and H152A mutant with O3-acetyl-L-serine and beta-chloro-L-alanine as substrates are similar, 100 mM concentrations of 2-(N-morpholino)ethanesulfonic acid (MES), pH 5.5-6.5, 3-(N-morpholino)propanesulfonic acid (MOPS), pH 7.0-7.5, N-(2-hydroxyethyl)piperazine-N'-2-ethanesulfonic acid (HEPES), pH 8.0, and 3-[[tris(hydroxymethyl)]amino]propanesulfonic acid (TAPS), pH 9.0, titrated with KOH
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
30
-
-
assay at
30
-
D2Z027
assay at
50
-
-
soluble enzyme, DEAE-immobilized enzyme and silica-immobilized enzyme
50
-
-
chloroplast enzyme
60
-
-
vinylacetate-epoxy-immobilized enzyme and vinylacetate-hydroxy-immobilized enzyme
70
-
-
maximal for O-acetyl-L-serine sulfhydrylation at both 70C and at 80C
80
-
-
synthesis of L-cystathionine and sulfhydrylation of L-Ser. Maximal for O-acetyl-L-serine sulfhydrylation at both 70C and at 80C
90
-
-
synthesis of S-sulfo-L-cysteine
additional information
-
-
assay performed at room temperature
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
67
-
about 50% of maximal activity at 35C and at 67C
42
58
-
all isoenzymes
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
P0A1E3, P29848
A-isozyme expressed under aerobic and the B-isozyme expressed under anaerobic conditions
Manually annotated by BRENDA team
P0A1E3, P29848
A-isozyme expressed under aerobic and the B-isozyme expressed under anaerobic conditions
Manually annotated by BRENDA team
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
-
Manually annotated by BRENDA team
-
two isoforms
Manually annotated by BRENDA team
-
enzyme is induced in leaves exposed to salt stress
Manually annotated by BRENDA team
O81154, O81155, -
;
Manually annotated by BRENDA team
-
enzyme activities are increased in presence of Cu, As, Cd, or Pb
Manually annotated by BRENDA team
-
30-35% of activity
Manually annotated by BRENDA team
-
induction of activity under stress, 0.025-0.300 mM Cd2+, 100 mM NaCl, or 0.001 mM abscisic acid
Manually annotated by BRENDA team
-
in presence of metal ions As, Cd, and Pb, OASTL transcripts are increased especially in roots, where metal accumulation is maximal, while Cu produces a decrease in the transcript levels. Enzyme activities are increased in presence of Cu, As, Cd, or Pb
Manually annotated by BRENDA team
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
roots of seedlings; roots of seedlings; roots of seedlings
Manually annotated by BRENDA team
-
root plasma membrane SO42- transporter SULTR1,2 physically interacts with the enzyme
Manually annotated by BRENDA team
Xanthium pennsylvanicum
-
-
Manually annotated by BRENDA team
-
hydrated seeds
Manually annotated by BRENDA team
Q8W1A0
activity peaks in young developing seed and declines thereafter
Manually annotated by BRENDA team
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
mainly expressed in developing seeds
Manually annotated by BRENDA team
-
maximal activity
Manually annotated by BRENDA team
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
young stems; young stems
Manually annotated by BRENDA team
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
-
Manually annotated by BRENDA team
additional information
-
isoforms OAS-TL A and B are the most abundant isoforms in all tissues analyzed. The major isoforms present in cytosol, plastids and mitochondria show significant modifications into up to seven subspecies. Specific isoforms are found to be differentially modified in the leaves, roots, stem and cell culture. Sulfur deficiency does not alter modification of enzyme proteins purified from cell culture that shows the highest complexity of modifications. However, the pattern of enzyme modification is found to be stable within an analyzed tissue
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
both mesophyll and bundle sheath chloroplasts
Manually annotated by BRENDA team
-
68-86% of activity, stroma
Manually annotated by BRENDA team
-
different from cytosolic enzyme
Manually annotated by BRENDA team
-
different from cytosolic and mitochondrial enzymes, as revealed by polyclonal antibody studies, 3-5% of total activity
Manually annotated by BRENDA team
O22682
thylakoid lumen
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Xanthium pennsylvanicum
-
-
Manually annotated by BRENDA team
-
different from chloroplast enzyme
Manually annotated by BRENDA team
-
enzyme form PCS-1
Manually annotated by BRENDA team
-
serine O-acetyltransferase SAT3 and O-acetylserine sulfhydrolase can interact in plant mitochondria to form the cysteine synthase complex. Formation of the mitochondrial cysteine synthase complex might be promoted by the stabilizing effect of sulfide, by efficient export of O-acetylserine from mitochondria, or by a combination of both
Manually annotated by BRENDA team
-
enzyme form PCS-2
Manually annotated by BRENDA team
Paracoccus denitrificans 8944
-
-
-
-
Manually annotated by BRENDA team
-
presence of an active CS26 enzyme exclusively in the thylakoid lumen
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Geobacillus kaustophilus (strain HTA426)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Helicobacter pylori (strain ATCC 700392 / 26695)
Mycobacterium marinum (strain ATCC BAA-535 / M)
Mycobacterium ulcerans (strain Agy99)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
32000
-
-
wild type and mutants, SDS-PAGE
32000
-
E5LPF4, -
PAGE
46000
-
-
isoenzyme 2, gel filtration
50000
-
-
isoenzyme 2, gel filtration
52000
-
Xanthium pennsylvanicum
-
gel filtration
52000
-
-
gel filtration
52000
-
-
gel filtration
55000
-
-
cysteine synthase B, gel filtration
56000
-
-
isoenzyme 1 and 2, gel filtration
56000
-
-
isoenzyme 1, gel filtration
57000
-
-
isoenzyme 1, gel filtration
58000
-
-
gel filtration
58000
-
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
calculated from cDNA
59000
-
-
one of two bands gel filtration
60000
-
-
gel filtration
60000
-
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
calculated from cDNA; calculated from cDNA; calculated from cDNA; calculated from cDNA
63000
-
-
all isoenzymes, gel filtration
63000
-
-
isoenzymes one and three, gel filtration
64000
-
-
chloroplast enzyme, gel filtration
64000
-
-
gel filtration
65000
-
-
sedimentation equilibrium
65000
-
-
gel filtration
66000
-
-
gel filtration
66000
-
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
calculated from cDNA
67600
-
Q8W1A0
calculated from cDNA
68000
-
-
free enzyme, sedimentation equilibrium
68000
-
-
gel filtration
68000
-
-
one of two bands ,gel filtration
68000
-
-
isoenzyme 1', gel filtration
68000
-
-
chloroplast enzyme, gel filtration
68000
-
-
gel filtration
70000
-
Q845F9
gel filtration
70000
-
Q8W1A0
gel filtration
70580
-
-
sedimentation equilibrium
70800
-
-
gel filtration
73000
-
-
isoenzyme 2, gel filtration
74200
-
Q8W1A0
sedimentation equilibrium ultracentrifugation
81000
-
-
isoenzyme 1, gel filtration
86000
-
-
isoenzyme 2, gel filtration
93000
-
-
gel filtration
96000
-
-
wild type strain, low molecular weight enzyme, sedimentation equilibrium
99000
-
-
Cys auxotroph strain, sedimentation equilibrium
126000
-
D2Z027
gel filtration
200000
-
-
gel filtration
300000
-
-
bienzyme complex with serine acetyltransferase, gel filtration
309000
-
-
cysteine synthetase complex, sedimentation equilibrium
310000
-
-
cysteine synthetase complex, gel filtration
1390000
-
-
cysteine synthetase complex, sedimentation equilibrium
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q8W1A0
x * 34000, calculated, x * 34000, SDS-PAGE
?
-
x * 35600, calculated
dimer
-
2 * 36000
dimer
-
2 * 33000, SDS-PAGE
dimer
-
2 * 34000, SDS-PAGE
dimer
-
2 * 32000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 29000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 36000, isoenzyme 2, SDS-PAGE; 2 * 40000, isoenzyme 1, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
dimer
-
1 * 32000 + 1 * 31200, isoenzyme 2, SDS-PAGE; 2 * 32000, isoenzymes 1 and 3, SDS-PAGE
dimer
-
2 * 34000, SDS-PAGE
dimer
-
2 * 35000, SDS-PAGE
dimer
-
2 * 34000, SDS-PAGE
dimer
-
2 * 42000, SDS-PAGE
dimer
-
2 * or 3 * 36000, SDS-PAGE
dimer
Q845F9
2 * 34000, SDS-PAGE
dimer
-
crystallization data
dimer
-
2 * 32000, SDS-PAGE
dimer
-
2 * 34500, SDS-PAGE
dimer
-
crystallization data
dimer
-
2 * 32600, SDS-PAGE
dimer
-
2 * ?, determined by molecular replacement of crystal structure; crystallization data
dimer
-
2 * 34000, SDS-PAGE
-
homodimer
P16703
2 * 32893, calculated from amino acid sequence
homodimer
Q8W1A0
gel filtration
tetramer
-
4 * 51000, SDS-PAGE, association does not require disulfide linkage
tetramer
D2Z027
4 * 36000, SDS-PAGE
tetramer
Streptomyces lavendulae ATCC 11924
-
4 * 36000, SDS-PAGE
-
trimer
-
3 or 2 * 36000, SDS-PAGE
monomer
E5LPF4, -
1 * 32000, SDS-PAGE, 1 * 34900, calculated
additional information
Xanthium pennsylvanicum
-
amino acid composition
additional information
-
two dimeric enzyme molecules form complex with tetrameric serine acetyltransferase, complex does not dissociate during catalysis
additional information
-
amino acid analysis, one sulfhydryl group per subunit, essential for restoration of native subunit structure
additional information
-
at least tetramer, equilibrium between aggregated and disintegrated cysteine synthetase complex can be shifted by various effectors, has consequences for enzyme function, model of structural-functional relationships
additional information
-
amino acid composition
additional information
-
cysteine synthase complex contains 2 mol O-acetylserine sulfhydrylase per mol serine-O-transacetylase
additional information
-
amino acid composition
additional information
-
amino acid analysis, N-terminal amino acid is serine
additional information
-
amino acid composition
additional information
-
amino acid composition; isoenzymes have different cysteine and methionine content
additional information
-
amino acid composition
additional information
-
amino acid composition
additional information
-
amino acid composition
additional information
-
amino acid composition
additional information
-
three-dimensional model of enzyme structure, catalytic sites
additional information
-
isoenzyme 1', N-terminal amino acid sequence differs from those of enzymes one, two, and three
additional information
-
all isoforms, but particularly isoenzyme 2 can form cysteine synthetase complex with serine acetyltransferase, as revealed by polyclonal antibody studies
additional information
-
amino acid composition
additional information
-
N-terminal amino acid sequence
additional information
-
monomer is composed of 15 helices and 9 beta-strands, it consists of two domains A and B and has a phosphate ligand bound to each domain
additional information
-
in the complex between serine acetyltransferase and O-acetylserine sulfhydrolase, the C-terminal C10 peptide of serine acetyltransferase binds to the O-acetylserine sulfhydrolase homodimer in a 2:1 complex. Interaction between O-acetylserine sulfhydrolase and C10 peptide is tight over a range of temperature from 10C to 35C and NaCl concentrations from 0.02 M to 1.3 M. Binding displays negative cooperativity at higher temperatures, and the enthalpy of interaction has a significant temperature dependence. Hydrophobic interactions drive the formation of the O-acetylserine sulfhydrolase-C10 peptide complex
additional information
-
serine acetyltransferase (SAT, EC 2.3.1.30) and O-acetylserine thiol lyase reversibly form the heterooligomeric Cys synthase complex. SAT from Arabidopsis thaliana expressed in tobacco interacts with endogenous tobacco OAS-TL
additional information
-
OASS-B does not form a complex with Escherichia coli serine acetyltransferase (SAT, EC 2.3.1.30)
additional information
Q8W1A0
a cysteine synthase complex is formed by association of serine O-acetyltransferase (SAT) and O-acetylserine sulfhydrylase (OASS). Biophysical examination cysteine synthase complex by gel filtration and sedimentation ultracentrifugation indicates that this assembly consists of a single serine O-trimer and three OASS dimers
additional information
-
amino acid composition
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
isoforms OAS-TL A and B are the most abundant isoforms in all tissues analyzed. The major isoforms present in cytosol, plastids and mitochondria show significant modifications into up to seven subspecies. Specific isoforms are found to be differentially modified in the leaves, roots, stem and cell culture. Sulfur deficiency does not alter modification of enzyme proteins purified from cell culture that shows the highest complexity of modifications. However, the pattern of enzyme modification is found to be stable within an analyzed tissue
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
structures of the enzyme without acetate, the complex formed by the K127A mutant with the external Schiff base of pyridoxal 5'-phosphate with O-phosphoserine, and the complex formed by the K127A mutant with the external Schiff base of pyridoxal 5'-phosphate with O-acetylserine, to 2.1 A resolution. No significant difference is seen in the overall structure between the free and complexed forms of the enzyme. The side chains of T152, S153, and Q224 interact with the carboxylate of the substrate. The position of R297 is significantly unchanged in the complex of the K127A mutant with the external Schiff base, allowing enough space for an interaction with O-phosphoserine. The positively charged environment around the entrance of the active site including S153 and R297 is important for accepting negatively charged substrates
-, Q9YBL2
construction of a model of the cysteine synthase complex composed of the enzymes serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL. Binding energy calculations suggest that, consistent with experiments, a ratio of two OAS-TL dimers to one SAT hexamer is likely
P47998
native protein and mutant K46A with pyridoxal 5-phosphate and methionine covalently linked as an external aldimine
-
to elucidate the structural basis of proteinprotein interactions in the plant Cys synthase complex, the crystal structure of Arabidopsis thaliana O-acetylserine sulfhydrylase bound with a peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase (C10 peptide) is determiend at 2.9 A resolution
-
hanging-drop vapour-diffusion method, crystals belong to the tetragonal space group P4(1), with unit cell parameters a = 80.3, b = 80.3, c = 112.2 A, two molecules per asymmetric unit and a complete data set is collected to a resolution of 1.86 A
-
native and in complex with its product L-cysteine, 50 mM Tris buffer, pH 8.0, with 150 mM NaCl, hanging drop method at 16C, 2.3 M ammonium sulfate as precipitant for the complex with 5 mM cysteine in 100 mM Tris, pH 7.2, with increasing glycerol concentrations, diffraction data collection at -173C; native protein at 1.86 A resolution, in complex with product cysteine at 2.4 A resolution. The dimeric interface lacks a chloride binding site. The N-terminal extension participates in dimeric interactions in a domain swapping manner. Sulfate is bound in the active site of the native structure, which is replaced by cysteine in the cysteine bound form
-
; hanging drop vapor diffusion method, using 100 mM sodium citrate, pH 5.6, 100 mM ammonium sulfate, 20% (w/v) PEG 4000
P16703
in complex with substrate analog citrate, at 1.33 A resolution. The C1-carboxylate of citrate is bound at the carboxylate position of O-acetylserine, whereas the C6-carboxylate adopts two conformations. Modeling of the unnatural substrate 5-thio-2-nitrobenzoate into the structure
-
complex with inhibitory pentapeptides MNYDI (10 mM HEPES, pH 8.0, 25 mM NaCl, 8.8 mM peptide), MNKGI (20 mM HEPES, pH 7.5, 20 mM NaCl, 12.5 mM peptide), MNWNI (10 mM HEPES, pH 7.5, 25 mM NaCl, 7.5 mM peptide), MNYFI (20 mM HEPES, pH 8.0, 20 mM NaCl, 12.7 mM peptide), MNENI (10 mM HEPES, pH 7.5, 25 mM NaCl, 9.4 mM peptide), and MNETI (20 mM HEPES, pH 7.5, 20 mM NaCl, 9.4 mM peptide), reservoir solution is 100 mM HEPES, pH 7.5, between 1.8 and 2.1 M (NH4)2SO4, and polyethylene glycol 400, except for the complex with MNWNI (100 mM CAPS, pH 10.5, 1.75 (NH4)2SO4, and 0.2 M Li2SO4), the cryoprotection solution contains glycerol, hanging drop vapor diffusion method, diffraction data are measured at -183C; the X-ray structure of three (MNWNI, MNYDI, and MNENI) high affinity pentapeptide-OASS complexes are compared with the docked poses
-
in complex with C-terminal peptide of serine acetyltransferase
-
to 1.8 A resolution. The biologically active unit, a dimer, constitutes the asymmetric unit. Subunit A contains residues 3-213 and 241-333, whilst subunit B comprises residues 4-214 and 241-333. A surface loop from residues 214 to 241 is disordered. The subunit contains two domains. The smaller domain I is constructed by residues 51-158, which primarily form a four-stranded beta-sheet surrounded by four alpha-helices. The larger domain II comprises residues 21-50 and 159-306. Domain II contains four alpha-helices and six beta-strands which, together with a beta-strand contributed from the partner-subunit domain I, form a seven-membered beta-sheet. In addition, residues 307-333 at the C-terminus form an extended helix-loop-helix structure that stretches across the surface of the partner subunit
-
identification of inhibitors by docking into crystal structure, PDB entry 2Q3C
-, P0A534
trapping of the alpha-aminoacrylate reaction intermediate and determination of its structure by cryocrystallography, 2.2 A resolution. Determination of the crystal structure of the enzyme bound to an inhibitory four-residue peptide derived from the C-terminus of Mycobacterium tuberculosis CysE (SAT, Rv2335). The structure of this inhibited form of CysK1 may provide the basis for the design of strong binding inhibitors of this enzyme
-
crystal structure of the enzyme with chloride bound at an allosteric site and sulfate bound at the active site
-
crystal structure of the enzyme with chloride bound at an allosteric site and sulfate bound at the active site; structural model based on crystallographic data
-
hanging-drop vapor diffusion method, structure of O-acetylserine sulfhydrylase B solved to 2.3 A
P0A1E3, P29848
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
10
-
37C, 60 min, stable
8
12
-
50C, 30 min, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
60
-
1 h, pH 7.5, stable
0
-
-
12 h, about 20% loss of activity
2
-
-
inactivated above, after a few days
20
40
-
12 h, stable
21
-
-
pH 8.0, 50 mM dithiothreitol, 0.08 mM pyridoxal phosphate, 30 min, stable
40
-
-
stable below
45
-
-
stable below
50
-
-
10 min, unstable above
50
-
-
10 min, no loss of activity
50
-
-
2 min, all isoenzymes stable
55
-
-
5 min, 45% loss of activity, without pyridoxal 5'-phosphate
60
-
-
10 min, no loss of activity
60
-
-
10 min, 85% loss of activity
60
-
-
1 min, no loss of activity
60
-
-
12 h, about 15% loss of activity
60
-
Q845F9
30 min, stable in pH-range of 6.0-10.0
65
-
-
5 min, complete loss of activity
65
-
-
5 min, complete loss of activity, without pyridoxal 5'-phosphate
65
-
-
2 min, isoenzyme 1 loses 50% loss of activity, isoenzymes 2 loses 25% of its activity, no loss of activity, isoenzyme 3
70
-
-
3 min, stable
70
-
-
10 min, 10% loss of activity of immobilized enzyme, 65-80% loss of activity of native enzyme
70
-
-
pH 7.8, 60 min, stable
70
-
Q845F9
30 min, pH 7.5, stable
77
-
-
5 min, complete loss of activity
80
-
-
3 min, unstable
80
-
-
3 min, unstable
80
-
-
60 min, 10 mM dithiothreitol, less than 10% of activity
100
-
-
pH 6.1 and 6.7, 6 h, 10% loss of activity
additional information
-
-
pyridoxal 5'-phosphate stabilizes against heat inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
extended dimeric interface interactions contribute to the stability of the dimer under physiological conditions
-
stable to several freeze-thaw cycles
-
relatively stable
-
holo-O-acetylserine sulfhydrylase exhibits greater conformational stability than the apoenzyme form. Role of pyridoxal 5'-phosphate in the structural stabilization of O-acetylserine sulfhydrylase
-
chloroplast enzyme very unstable
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Glycerol
-
5% glycerol and 5 mM 2-mercaptoethanol are essential for maintaining the long-term stability of the enzyme
mercaptoethanol
-
5% glycerol and 5 mM 2-mercaptoethanol are essential for maintaining the long-term stability of the enzyme
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0 C, potassium phosphate buffer, pH 8, mercaptoethanol, EDTA, three months, no loss of activity
-
-20 C, polybuffer 74, pH 4.0, glycerol, 4 months
-
-20 C, phosphate buffer, pH 7.5, glycerol, pyridoxal-5'-phosphate, 8 days, 50% loss of activity
-
-70C, Tris-HCl, pH 8.1, glycerol, 6 months, no loss of activity
-
-20 C, complete loss of activity after 2 months
-
-20 C, potassium phosphate buffer, pH 6.5, 1 mM EDTA, at least several days, no loss of activity
-
-20 C, Tris-HCl buffer, pH 7.6, bovine serum albumine, 8 months, 10% loss of activity
-
20 C, room temperature, Tris-HCl buffer, pH 7.6, bovine serum albumine, several days, no loss of activity
-
0 C, potassium phosphate buffer, pH 8.0, 2-mercaptoethanol, EDTA, several months, no loss of activity
-
-15 C, potassium phosphate buffer, dithiothreitol, one week, 50% loss of activity
-
-15 C, phosphate buffer, pH 7.2, several months, no loss of activity
-
2 C, inactivated above, after a few days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the soluble protein is purified by one-step affinity chromatography to apparent homogeneity
-
cells are harvested by centrifugation, washed with sterile water, again harvested by centrifugation, suspended in 20 mM potassium phosphate buffer, pH 7.4, containing 0.5 M NaCl, lysed with lysozyme at room temperature, one-step affinity chromatography with nickel metal-affinity resin columns, dialyzed against 20 mM potassium phosphate buffer, pH 7.5, 5% glycerol, and 5 mM 2-mercaptoethanol
-
recombinant enzyme
-
recombinant protein of isoforms A,B,C
-
using Ni-NTA chromatography
-
Source 30Q column chromatography and Superdex 75 gel filtration
P16703
using a GSTrap 4 B column and anion-exchange chromatography
-
ethanol precipitation, ammonium sulfate precipitation, preparative electrophoresis, phenyl sepharose
Q845F9
purified using nickel-affinity and gel filtration. Thrombin digestion is used to remove the His tag from each protein
Q8W1A0
using gel filtration; using gel filtration; using Glutathione Sepharose 4B column; using Glutathione Sepharose 4B column; using Glutathione Sepharose 4B column; using Glutathione Sepharose 4B column
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
Ni-NTA affinity and Superdex 200 pg gel filtration chromatography; using Ni-NTA chromatography and gel filtration
-
cell harvesting are resuspended in 50 mM Tris buffer, pH 8.0, containing 10 mM EDTA, 15 mM beta-mercaptoethanol, 0.05 mM N-p-tosyl-L-lysine chloromethylketone, leupeptin, aprotinin, pepstatin, lysozyme and pyridoxal 5'-phosphate, centrifuged, supernatant loaded on a DE52 anion exchange column, washed with 50 mM Tris buffer, pH 8.0, with 10 mM EDTA, and 15 mM beta-mercaptoethanol, elution with NaCl gradient in buffer, active fractions are pooled, concentrated and applied to a GSTrap 4B column, washed with PBS buffer, pH 7.4, containing 140 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, and 1.8 mM KH2PO4, elution with 50 mM Tris, pH 8.0, with 20 mM reduced glutathione and thrombin, dialyzed with 15 mM potassium phosphate, pH 7.2, applied on a DE 52 column, separation of enzyme from GST-tag and thrombin with a gradient of 15-300 mM potassium phosphate buffer, pH 7.2
-
nickel-NTA column; the apoenzyme of OASS-B is prepared using hydroxylamine as the resolving reagent. Apoenzyme is reconstituted to holoenzyme by addition of pyridoxal 5'-phosphate; using Ni-NTA chromatography
-
Q-Sepharose and phenyl Sepharose column, active fractions are pooled and concentrated
-
isoenzyme A and B
-
-
Xanthium pennsylvanicum
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
PCR-amplification, expression of His-tagged wild type and mutant enzyme in Escherichia coli BL21(DE3) with expression vector pLM1
-
expression in Escherichia coli
-
expression of isoenzyme A, B and C in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expression in Escherichia coli
P47998
overexpression of the Atcys-3A gene of the cytosolic isoform in Saccharomyces cerevisiae can support the growth of the yeast cells at high concentrations of sodium chloride, suggesting that the plant protein is able to confer salt tolerance in yeast
-
expression in Escherichia coli NK3
-, Q2PZM5
expression in Escherichia coli
-
expression in Escherichia coli BLR with pET-28a
-
expressed as a GST-fusion protein
-
expressed in Escherichia coli BL21(DE3) cells
P16703
overexpressed in Escherichia coli using pUC19 with a lacUV5 promoter
-
expressed in Escherichia coli as a His-tagged fusion protein
Q8W1A0
expressed in Escherichia coli as GST-fusion proteins; expressed in Escherichia coli as GST-fusion proteins; expressed in Escherichia coli as GST-fusion proteins; expressed in Escherichia coli as GST-fusion proteins; expressed in Escherichia coli as GST-fusion proteins; expressed in Escherichia coli as GST-fusion proteins
A3RM03, A3RM04, A3RM05, A5YT86, A5YT88
expression in Escherichia coli
-
expressed in Escherichia coli
-
expression in Escherichia coli BL21(DE3) with pET28a; HiOASS is overexpressed in Escherichia coli
-
expression in Escherichia coli
E5LPF4, -
cotyledon segments of seedlings of Ipomoea aquatica are transformed with Arabidopsis serine acetyltransferase gene and Oryza sativa cysteine synthase gene under the control of the cauliflower mosaic virus 35S promoter. Strengthening of serine acetyltransferase and cysteine synthase results in increase not only in sulfate uptake, but also in total biomass
-
H2S is a major environmental pollutant, highly toxic to living organisms at high concentrations. Even at low concentrations, it causes an unpleasant odor from wetlands, especially from wastewater. Plants can utilize hydrogen sulfide as a sulfur source to synthesize cysteine. It is thus feasible to use aquatic plants, which possess high potential for sulfur assimilation, to remove hydrogen sulfide from the wetland. Transgenic rice plants over-expressing cysteine synthase exhibit 3fold elevated cysteine synthase activity, and incorporate more H2S into cysteine and glutathione than their wild type counterparts upon exposure to a high level of H2S. Overexpression of cysteine synthase in aquatic plants is a viable approach to remove H2S from polluted environments
Q9XEA6
expressed in Escherichia coli NM522 with plasmid pRSM40
-
expression in with plasmid pRSM40 in Escherichia coli NM522
-
expression of the glutathione S-transferase (GST)-fusion enzyme in Escherichia coli BL21 with pGEX 4T-2 vector
-
to decrease the activity of OASTL, potato plants are transformed with the vector pBinAR harboring a cDNA encoding a sequence from either the StOASTL A or the StOASTL B gene in reverse orientation with respect to the cauliflower mosaic virus 35S promoter. THe transgenic approach is used to downregulate specifically the plastidial and cytosolic isoforms in Solanum tuberosum. This approach results in decreased RNA, protein, and enzymatic activity levels. H2S-releasing capacity is also reduced in these lines. The thiol levels in the transgenic lines are, regardless of the selected OASTL isoform, significantly elevated. Levels of metabolites such as serine, O-acetyl-L-Ser, methionine, threonine, isoleucine, and lysine also increase in the investigated transgenic lines; to decrease the activity of OASTL, potato plants are transformed with the vector pBinAR harboring a cDNA encoding a sequence from either the StOASTL A or the StOASTL B gene in reverse orientation with respect to the cauliflower mosaic virus 35S promoter. THe transgenic approach is used to downregulate specifically the plastidial and cytosolic isoforms in Solanum tuberosum. This approach results in decreased RNA, protein, and enzymatic activity levels. H2S-releasing capacity is also reduced in these lines. The thiol levels in the transgenic lines are, regardless of the selected OASTL isoform, significantly elevated. Levels of metabolites such as serine, O-acetyl-L-Ser, methionine, threonine, isoleucine, and lysine also increase in the investigated transgenic lines
O81154, O81155, -
construction of transgenic Nicotiana tabacum carrying either spinach cytosolic cDNA, designated 3F plants, or chimeric CSAse A cDNA fused with the sequence for chloroplast-targeting transit peptide of pea Rubisco small subunit, designated 4F plants. Generation of F1 transgenic tobacco, highly tolerant to sulfur-containing pollutants, in which Csase activities are enhanced both in cytosol and in the chloroplasts by crossing 3F plants with 4F plants
-
expressed in Escherichia coli
-
expression in Escherichia coli
D2Z027
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression is not regulated by presence of cysteine
E5LPF4, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
H150A
-
in contrast to the wild-type protein the mutant protein is colorless after purification, and UV-Vis scanning of the mutant proteins show that there are no absorptions between 300 and 500 nm, mutant protein does not show a comparable activity to the wild-type protein. This suggests that the mutated residue is crucial or pyridoxal 5'-phosphate binding and stabilization
H168A
-
in contrast to the wild-type protein the mutant protein is colorless after purification, and UV-Vis scanning of the mutant proteins show that there are no absorptions between 300 and 500 nm, mutant protein does not show a comparable activity to the wild-type protein. This suggests that the mutated residue is crucial or pyridoxal 5'-phosphate binding and stabilization
K30A
-
in contrast to the wild-type protein the mutant protein is colorless after purification, and UV-Vis scanning of the mutant proteins show that there are no absorptions between 300 and 500 nm, mutant protein does not show a comparable activity to the wild-type protein. This suggests that the mutated residue is crucial or pyridoxal 5'-phosphate binding and stabilization
K41A
-
mutant protein is also colourful as the wild-type protein, mutant protein does not show the same activity as the wild-type protein
H150A
-
not active, crucial for cofactor binding
H168A
-
not active, crucial for cofactor binding
K30A
-
not active, crucial for cofactor binding
K127A
-, Q9YBL2
mutant is inactive for cysteine synthesis and does not form the alpha-aminoacrylate intermediate
Q224A
-, Q9YBL2
0.2% of wild-type activity
R297A
-, Q9YBL2
61% of wild-type activity
R297E
-, Q9YBL2
52% of wild-type activity
R297K
-, Q9YBL2
48% of wild-type activity
S153A
-, Q9YBL2
117% of wild-type activity
S153T
-, Q9YBL2
8% of wild-type activity
T152A
-, Q9YBL2
2% of wild-type activity
T152S
-, Q9YBL2
93% of wild-type activity
T203A
-, Q9YBL2
41% of wild-type activity
T203M
-, Q9YBL2
20% of wild-type activity
H157N
-
comparable to wild-type
H157Q
-
reduced kcat-value, reduced Km-value
N77A
-
reduced kcat-value
N77D
-
drastically reduced kcat-value
Q147A
-
drastically reduced kcat-value, increased Km-value
Q147A
-
mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
Q147E
-
drastically reduced kcat-value, increased Km-value
S269A
-
reduced kcat-value, reduced Km-value
S269T
-
reduced kcat-value, reduced Km-value
S75A
-
drastically reduced kcat-value
S75A
-
mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
S75N
-
drastically reduced kcat-value
S75T
-
drastically reduced kcat-value
S75T
-
mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
T182A
-
reduced kcat-value
T182S
-
comparable to wild-type
T185A
-
drastically reduced kcat-value
T185S
-
drastically reduced kcat-value
T74A
-
drastically reduced kcat-value
T74S
-
reduced kcat-value
T74S
-
mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase
T78A
-
reduced kcat-value, reduced Km-value
T78S
-
reduced kcat-value, reduced Km-value
Y302A
-
loss of enzymic activity
F143A
-
mutant retains one molecule of pyridoxal 5'-phosphate per subunit, mutant reacts with O-acetylserine but the rate is significantly smaller, kcat/KM (O-acetylserine): 950/Msec
F143D
-
mutant retains one molecule of pyridoxal 5'-phosphate per subunit, mutant reacts with O-acetylserine but the rate is significantly smaller, kcat/KM (O-acetylserine): 150/Msec
F143S
-
mutant retains one molecule of pyridoxal 5'-phosphate per subunit, mutant reacts with O-acetylserine but the rate is significantly smaller, kcat/KM (O-acetylserine): 380/Msec
Q140E
-
inactive
Q142A
-
ability of pyridoxal 5'-phosphate binding is not altered, mutant does not react with O-acetylserine
Q240A
-
ratio kcat to Km value is 0.4% of wild-type, increase in temperature dependence factors, corresponding to an appreciable increase in the activation energy
R210A
-
ratio kcat to Km value is 2% of wild-type
T68A
-
ratio kcat to Km value is 0.1% of wild-type, increase in temperature dependence factors, corresponding to an appreciable increase in the activation energy
T68S
-
ratio kcat to Km value is 55% of wild-type
DELTAE115-K118
-
mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
K118A
-
mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
K221A/P222E/G223E/P224E
-
mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
W162A
-
mutation increases the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
Y188A
-
mutation increases the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
DELTAE115-K118
Saccharomyces cerevisiae P169-4A
-
mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
-
K118A
Saccharomyces cerevisiae P169-4A
-
mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
-
K221A/P222E/G223E/P224E
Saccharomyces cerevisiae P169-4A
-
mutation disables the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
-
W162A
Saccharomyces cerevisiae P169-4A
-
mutation increases the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
-
Y188A
Saccharomyces cerevisiae P169-4A
-
mutation increases the interaction of O-acetylserine (thiol) lyase with serine acetyltransferase
-
N71A
-
mutant exhibits formation of the alpha-aminoacrylate intermediate, but the rate constant for its formation from the external Schiff base is decreased by 1 order of magnitude compared to that of the wild type
Q142A
-
mutant is unable to form the alpha-aminoacrylate intermediate but produces pyruvate at a rate much greater than that of the wild-type enzyme
S69A
-
mutant exhibits formation of the alpha-aminoacrylate intermediate, but the rate constant for its formation from the external Schiff base is decreased by 1 order of magnitude compared to that of the wild type
T68A
-
mutant is unable to form the alpha-aminoacrylate intermediate but produces pyruvate at a rate much greater than that of the wild-type enzyme
H152A
-
shift in the ketoenamine to enolimine tautomeric equilibrium toward the neutral enolimineine, the internal Schiff base of the free enzyme, the amino acid external Schiff base, and the alpha-aminoacrylate intermediate. The decreased rate of the mutant likely reflects a decrease in the amount of active enzyme as a result of an increased flexibility of the cofactor , which leads to increased rates of interconversion of the open and closed forms of the enzyme and additional interactions between the cofactor and enzyme in the closed form of the enzyme. Analysis of spectral properties; shift in the ketoeneamine to enolimine tautomeric equilibrium towards neutral enolimine in the internal Shiff base of the free enzyme, the amino acid external Schiff base, and the alpha-aminoacrylate intermediate, 2 enzyme conformers are present, decreased rate of the enzyme likely reflects a decrease in the amount of active enzyme as result of the increased cofactor flexibility which stabilizes the nonproductive binding of O3-acetyl-L-serine in the external Schiff base
K120Q
-
mutation results in a shift in the tautomeric equilibrium toward the neutral enolimine and an increase in the rate of interconversion of the open and closed forms of the enzyme. A decrease in the rate of both half reactions reflects the stabilization of the external Schiff base. Role of K120 in helping to stabilize the closed conformation of the enzyme by participating in a new bond to the backbone carbonyl of A231; shift in the tautomeric equilibrium toward the neutral enolimine and an increase of the rate of interconversion of the open and closed forms of the enzyme, probably reflecting the stabilization of the external Schiff base
R186L
-
retains one cofactor per subunit, accelerates the reaction with substrate O3-acetyl-L-serine 1.8fold, intermediates are formed faster by 1.5 and 1.3fold, respectively, with azide or thiosulfate than in the wild type
R186P
-
loss of cofactor leads to enzyme inactivation
S272A
-
mutant enzyme catalyzes the overall reaction, first half-reaction is decreased by factor 3, the decrease in rate of elimination is compensated by an increase in affinity for O-acetyl-L-Ser
S272D
-
mutant enzyme catalyzes the overall reaction
W161Y
-
2fold increase in Vmax and Km-value of O3-acetyl-L-serine
W50Y
-
no effect on catalytic rate or affinity of enzyme to first substrate, Km-value for 5-thio-2-nitrobenzoate decrease by 2.7fold
H152A
Salmonella enterica subsp. enterica serovar Typhimurium DW378
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shift in the ketoenamine to enolimine tautomeric equilibrium toward the neutral enolimineine, the internal Schiff base of the free enzyme, the amino acid external Schiff base, and the alpha-aminoacrylate intermediate. The decreased rate of the mutant likely reflects a decrease in the amount of active enzyme as a result of an increased flexibility of the cofactor , which leads to increased rates of interconversion of the open and closed forms of the enzyme and additional interactions between the cofactor and enzyme in the closed form of the enzyme. Analysis of spectral properties; shift in the ketoeneamine to enolimine tautomeric equilibrium towards neutral enolimine in the internal Shiff base of the free enzyme, the amino acid external Schiff base, and the alpha-aminoacrylate intermediate, 2 enzyme conformers are present, decreased rate of the enzyme likely reflects a decrease in the amount of active enzyme as result of the increased cofactor flexibility which stabilizes the nonproductive binding of O3-acetyl-L-serine in the external Schiff base
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K214A
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mutant retains high activity with O-acetylserine and sulfide (40% of the activity of the wild type enzyme), but its activity with O-phosphoserine and sulfide is reduced by more than 100fold. The ability to use thiosulfate as an alternative nucleophile in the sulfhydrylase reaction is greatly reduced, but the mutant shows no change in cysteine desulfurase activity
K43A
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protein is yellow, indicating that it binds pyridoxal 5'-phosphate but has no detectable activity as a cysteine synthase with O-acetylserine or O-phosphoserine and no detectable cysteine desulfurase activity
K46A
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no enzymic activity, crystallization data
additional information
P47998
upon expression of the enzymes of the cysteine synthase complex, serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL, cross-binding of Arabidopsis thaliana OAS-TL with Escherichia coli SAT may take place
additional information
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null alleles of cytosolic isoform oas-tl A or plastid isoform oas-tl B alone show that cytosolic OAS-TL A and plastid OAS-TL B are completely dispensable, although together they contribute 95% of total OAS-TL activity. An oas-tl AB double mutant, relying solely on mitochondrial OAS-TL C for Cys synthesis, shows 25% growth retardation. Although OAS-TL C alone is sufficient for full development, oas-tl C plants also show retarded growth
additional information
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knockout of the most abundant cytosolic OAS-TL isoforms oas-a1.1 and osa-a1.2. Total intracellular Cys and glutathione concentrations are reduced, and the glutathione redox state is shifted in favor of its oxidized form. The capability of the mutants to chelate heavy metals does not differ from that of the wild type, but the mutants have an enhanced sensitivity to cadmium. The oas-a1.1 mutant plants are oxidatively stressed, H2O2 production is localized in shoots and roots, spontaneous cell death lesions occur in the leaves, and lignification and guaiacol peroxidase activity are significantly increased
F143Y
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mutant retains one molecule of pyridoxal 5'-phosphate per subunit, reaction with O-acetylserine is inhibited
additional information
P16703
upon expression of the Arabidopsis thaliana enzymes of the cysteine synthase complex, serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL, cross-binding of Arabidopsis thaliana OAS-TL with Escherichia coli SAT may take place
K120Q
Salmonella enterica subsp. enterica serovar Typhimurium DW378
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mutation results in a shift in the tautomeric equilibrium toward the neutral enolimine and an increase in the rate of interconversion of the open and closed forms of the enzyme. A decrease in the rate of both half reactions reflects the stabilization of the external Schiff base. Role of K120 in helping to stabilize the closed conformation of the enzyme by participating in a new bond to the backbone carbonyl of A231; shift in the tautomeric equilibrium toward the neutral enolimine and an increase of the rate of interconversion of the open and closed forms of the enzyme, probably reflecting the stabilization of the external Schiff base
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additional information
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enzyme knockout mutant, grows poorly in cysteine-limiting conditions and produces significantly less cysteine than wild-type. Mutant shows increased sensitivity to tellurite, hydrogen peroxide, acid, and diamide. Mutant cells have a significantly reduced ability to recover from starvation in amino acid- or phosphate-limiting conditions
additional information
Staphylococcus aureus SH1000
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enzyme knockout mutant, grows poorly in cysteine-limiting conditions and produces significantly less cysteine than wild-type. Mutant shows increased sensitivity to tellurite, hydrogen peroxide, acid, and diamide. Mutant cells have a significantly reduced ability to recover from starvation in amino acid- or phosphate-limiting conditions
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Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
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synthesis of L-Cys, therefore immobilization
medicine
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target for novel peptidomimetic antibiotics based on the C-terminal pentapeptide of serine acetyltransferase
biotechnology
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transgenic plants expressing serine acetyltransferase and cysteine synthase can mitigate detrimental effects of cadmium toxicity, perhaps by efficiently producing and accumulating sulfuric compounds
environmental protection
Q9XEA6
H2S is a major environmental pollutant, highly toxic to living organisms at high concentrations. Even at low concentrations, it causes an unpleasant odor from wetlands, especially from wastewater. Plants can utilize hydrogen sulfide as a sulfur source to synthesize cysteine. It is thus feasible to use aquatic plants, which possess high potential for sulfur assimilation, to remove hydrogen sulfide from the wetland. Transgenic rice plants over-expressing cysteine synthase exhibit 3fold elevated cysteine synthase activity, and incorporate more H2S into cysteine and glutathione than their wild type counterparts upon exposure to a high level of H2S. Overexpression of cysteine synthase in aquatic plants is a viable approach to remove H2S from polluted environments
pharmacology
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involved in beta-lactam synthesis
synthesis
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overexpression of enzyme in cytosol, chloroplast, or both of Nicotiana tabacum, transgenic plants show significantly more tolerance than wild-type against Cd2+, Se2+, and Ni2+. Application of transgenic plants to phyto-remediation of Cd2+ from contaminated soils
medicine
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humans lack cysteine synthase. Therefore, this parasite enzyme could be an exploitable drug target