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O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
L-Cys + acetate
?
-
involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear
-
-
?
L-Cys + acetate
O-acetyl-L-Ser + H2S
NaN3 + O-acetyl-Ser
beta-azidoalanine + sodium acetate
-
-
mutagenic
?
O-acetyl-L-Ser + 1,2,3,4-tetrazole
?
-
-
-
-
?
O-acetyl-L-Ser + 1,2,3-benzotriazole
?
-
weak activity
-
-
?
O-acetyl-L-Ser + 1,2,4-triazole
?
-
-
-
-
?
O-acetyl-L-Ser + 1-propanethiol
?
-
-
-
-
?
O-acetyl-L-Ser + 3-mercapto-1,2,4-triazole
?
-
-
-
-
?
O-acetyl-L-Ser + benzenethiol
L-cys + benzylacetate
-
-
-
-
?
O-acetyl-L-Ser + cysteamine
?
-
weak activity
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
O-acetyl-L-Ser + pyrazole
?
-
weak activity
-
-
?
O-acetyl-L-Ser + S2O32-
S-sulfocysteine + ?
-
-
-
-
?
O-acetyl-L-Ser + sodium azide
?
-
weak activity
-
-
?
O-acetyl-L-Ser + sodium thiosulfate
?
-
-
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
O-acetyl-L-serine
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
additional information
?
-
L-Cys + acetate
O-acetyl-L-Ser + H2S
-
-
-
r
L-Cys + acetate
O-acetyl-L-Ser + H2S
-
-
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
r
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
-
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
residue Arg210 near the entrance of the active site and is important for O-acetyl-L-serine substrate recognition
-
-
?
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
-
-
?
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evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
metabolism
the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview
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
enzyme CysK is organized in a complex with serine acetyltransferase (CysE), which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. CysK also activates an antibacterial nuclease toxin produced by uropathogenic Escherichia coli. Role for CysK during bacterial contact-dependent growth inhibition involving the CDI system from uropathogenic Escherichi coli, overview. CysK-binding provides a mechanism to protect the bacterial CysE from cold-inactivation and proteolysis. Escherichia coli CysK acts as a so-called permissive factor to activate an antibacterial contact-dependent growth inhibition (CDI) toxin, and interacts with CdiA-CTUPEC536 in toxin activation
physiological function
serine acetyltransferase CysE is activated when bound to O-acetylserine sulfhydrylase CysK. CysE activation results from the release of substrate inhibition. Feedback inhibition of CysE by L-Cys is also relieved in the bacterial cysteine synthase complex
physiological function
the binding interaction of CdiA-CT toxin from uropathogenic Escherichia coli 536 with CysK mimics the cysteine synthase complex of CysK:CysE. The C-terminal tails of CysE and CdiA-CT each insert into the CysK active-site cleft to anchor the respective complexes. The dissociation constant for CysK:CdiA-CT is comparable to that of the Escherichia coli cysteine synthase complex, and both complexes bind through a two-step mechanism with a slow isomerization phase after the initial encounter. CdiA-CT can effectively displace CysE from pre-formed cysteine synthase complexes, enabling toxin activation even in the presence of excess competing CysE
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific
additional information
-
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific
additional information
-
intramolecular electrostatic interaction of enzyme OASS-B, overview
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F143A
-
mutant retains one molecule of pyridoxal 5'-phosphate per subunit, mutant reacts with O-acetylserine but the rate is significantly smaller, kcat/KM (O-acetylserine): 950/Msec
F143D
-
mutant retains one molecule of pyridoxal 5'-phosphate per subunit, mutant reacts with O-acetylserine but the rate is significantly smaller, kcat/KM (O-acetylserine): 150/Msec
F143S
-
mutant retains one molecule of pyridoxal 5'-phosphate per subunit, mutant reacts with O-acetylserine but the rate is significantly smaller, kcat/KM (O-acetylserine): 380/Msec
F143Y
-
mutant retains one molecule of pyridoxal 5'-phosphate per subunit, reaction with O-acetylserine is inhibited
Q142A
-
ability of pyridoxal 5'-phosphate binding is not altered, mutant does not react with O-acetylserine
Q240A
-
ratio kcat to Km value is 0.4% of wild-type, increase in temperature dependence factors, corresponding to an appreciable increase in the activation energy
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
additional information
upon expression of the Arabidopsis thaliana enzymes of the cysteine synthase complex, serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL, cross-binding of Arabidopsis thaliana OAS-TL with Escherichia coli SAT may take place
additional information
-
upon expression of the Arabidopsis thaliana enzymes of the cysteine synthase complex, serine-acetyl-transferase SAT and O-acetyl-serine-(thiol)-lyase OAS-TL, cross-binding of Arabidopsis thaliana OAS-TL with Escherichia coli SAT may take place
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Flint, D.H.; Tuminello, J.F.; Miller, T.J.
Studies on the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase in escherichia coli crude extract. Isolation of O-acetylserine sulfhydrylases A and B and beta-cystathionase based on their ability to mobilize sulfur from cysteine and to participate in Fe-S cluster synthesis
J. Biol. Chem.
271
16053-16067
1996
Escherichia coli
brenda
Kredich, N.M.; Becker, M.A.
Cysteine biosynthesis: serine transacetylase and O-acetylserine sulfhydrylase
Methods Enzymol.
17 B
459-470
1971
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Byrne, C.R.; Monroe, R.S.; Ward, K.A.; Kredich, N.M.
DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH
J. Bacteriol.
170
3150-3157
1988
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Owais, W.M.; Gharaibeh, R.
Cloning of the E. coli O-acetylserine sulfhydrylase gene: ability of the clone to produce a mutagenic product from azide and O-acetylserine
Mutat. Res.
245
151-155
1990
Escherichia coli
brenda
Mino, K.; Yamanoue, T.; Sakiyama, T.; Eisaki, N.; Matsuyama, A.; Nakanishi, K.
Effects of bienzyme complex formation of cysteine synthetase from Escherichia coli on some properties and kinetics
Biosci. Biotechnol. Biochem.
64
1628-1640
2000
Escherichia coli
brenda
Claus, M.T.; Zocher, G.E.; Maier, T.H.; Schulz, G.E.
Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli
Biochemistry
44
8620-8626
2005
Escherichia coli (P16703), Escherichia coli
brenda
Zhao, C.; Kumada, Y.; Imanaka, H.; Imamura, K.; Nakanishi, K.
Cloning, overexpression, purification, and characterization of O-acetylserine sulfhydrylase-B from Escherichia coli
Protein Expr. Purif.
47
607-613
2006
Escherichia coli
brenda
Zocher, G.; Wiesand, U.; Schulz, G.E.
High resolution structure and catalysis of O-acetylserine sulfhydrylase isozyme B from Escherichia coli
FEBS J.
274
5382-5389
2007
Escherichia coli
brenda
Feldman-Salit, A.; Wirtz, M.; Hell, R.; Wade, R.C.
A mechanistic model of the cysteine synthase complex
J. Mol. Biol.
386
37-59
2009
Escherichia coli (P16703), Escherichia coli, Arabidopsis thaliana (P47998), Arabidopsis thaliana
brenda
Ozaki, S.; Nakahara, A.; Sakaguchi, C.
Mutagenesis of Gln-142 and Phe-143 of O-acetylserine sulfhydrylase
J. Biochem. Mol. Biol. Biophys.
4
117-124
2009
Escherichia coli
-
brenda
Wang, T.; Leyh, T.S.
Three-stage assembly of the cysteine synthase complex from Escherichia coli
J. Biol. Chem.
287
4360-4367
2012
Escherichia coli
brenda
Nakatani, T.; Ohtsu, I.; Nonaka, G.; Wiriyathanawudhiwong, N.; Morigasaki, S.; Takagi, H.
Enhancement of thioredoxin/glutaredoxin-mediated L-cysteine synthesis from S-sulfocysteine increases L-cysteine production in Escherichia coli
Microb. Cell Fact.
11
62
2012
Escherichia coli, Escherichia coli BW25113
brenda
Campanini, B.; Benoni, R.; Bettati, S.; Beck, C.M.; Hayes, C.S.; Mozzarelli, A.
Moonlighting O-acetylserine sulfhydrylase: new functions for an old protein
Biochim. Biophys. Acta
1854
1184-1193
2015
Arabidopsis thaliana (P47998), Bacillus subtilis (P37887), Caenorhabditis elegans (Q93244), Entamoeba histolytica (Q401L7), Escherichia coli (P0ABK5), Escherichia coli, Glycine max (A3RM03), Haemophilus influenzae (P45040), Mycobacterium tuberculosis (P9WP55), Salmonella enterica subsp. enterica serovar Typhimurium (P0A1E3), Staphylococcus aureus
brenda
Nakamura, T.; Asai, S.; Nakata, K.; Kunimoto, K.; Oguri, M.; Ishikawa, K.
Thermostability and reactivity in organic solvent of O-phospho-L-serine sulfhydrylase from hyperthermophilic archaeon Aeropyrum pernix K1
Biosci. Biotechnol. Biochem.
79
1280-1286
2015
Escherichia coli, Escherichia coli W3110 / ATCC 27325
brenda
Benoni, R.; De Bei, O.; Paredi, G.; Hayes, C.S.; Franko, N.; Mozzarelli, A.; Bettati, S.; Campanini, B.
Modulation of Escherichia coli serine acetyltransferase catalytic activity in the cysteine synthase complex
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591
1212-1224
2017
Escherichia coli (P0ABK5), Escherichia coli, Escherichia coli K12 (P0ABK5)
brenda
Benoni, R.; Beck, C.M.; Garza-Sanchez, F.; Bettati, S.; Mozzarelli, A.; Hayes, C.S.; Campanini, B.
Activation of an anti-bacterial toxin by the biosynthetic enzyme CysK mechanism of binding, interaction specificity and competition with cysteine synthase
Sci. Rep.
7
8817
2017
Escherichia coli (P0ABK5), Escherichia coli, Escherichia coli K12 (P0ABK5)
brenda