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Information on EC 2.5.1.47 - cysteine synthase and Organism(s) Escherichia coli and UniProt Accession P16703

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IUBMB Comments
A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. Not identical with EC 2.5.1.51 (beta-pyrazolylalanine synthase), EC 2.5.1.52 (L-mimosine synthase) and EC 2.5.1.53 (uracilylalanine synthase).
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This record set is specific for:
Escherichia coli
UNIPROT: P16703
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
gyy4137, cysteine synthase, cysteine synthetase, o-acetylserine sulfhydrylase, oastl, oas-tl, o-acetylserine(thiol)lyase, csase, o-acetylserine (thiol) lyase, oass-a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
O-acetylserine sulfhydrylase isoenzyme B
-
acetylserine sulfhydrylase
-
-
-
-
CSase
-
-
-
-
cysteine synthase A
-
cysteine synthetase
-
-
-
-
O-acetyl-L-serine acetate-lyase (adding hydrogen sulfide)
-
-
-
-
O-acetyl-L-serine sulfhydrylase
-
-
-
-
O-acetyl-L-serine sulfhydrylase B
-
-
O-acetyl-L-serine sulfohydrolase
-
-
-
-
O-acetyl-L-serine(thiol)lyase
-
-
-
-
O-acetylserine (Thiol)-lyase
-
-
-
-
O-acetylserine (thiol)lyase
-
-
-
-
O-acetylserine sulfhydrylase
O-acetylserine sulfhydrylase A
O-acetylserine sulfhydrylase-B
-
-
O-acetylserine(thiol)lyase
-
-
-
-
O-acetylserine-O-acetylhomoserine sulfhydro-lyase
-
-
-
-
OAS Shase
-
-
-
-
OAS-TL
-
-
-
-
OASTL
-
-
-
-
S-sulfocysteine synthase
-
-
-
-
SSC synthase
-
-
synthase, cysteine
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
show the reaction diagram
geometric model of reaction, comparison isoenzyme CysK
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
C-O bond cleavage
-
-
-
-
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).
CAS REGISTRY NUMBER
COMMENTARY hide
37290-89-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-
-
-
?
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 + acetate
O-acetyl-L-Ser + H2S
show the reaction diagram
NaN3 + O-acetyl-Ser
beta-azidoalanine + sodium acetate
show the reaction diagram
-
-
mutagenic
?
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 + 3-mercapto-1,2,4-triazole
?
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 + 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 + sulfide
L-Cys + acetate
show the reaction diagram
O-acetyl-L-serine
L-cysteine + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-
-
-
?
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 + S2O32-
S-sulfocysteine + ?
show the reaction diagram
-
-
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
show the reaction diagram
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
slight activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)6Mo7O24
acetate
-
-
AgNO3
CuSO4
-
1 mM, 99% loss of activity
EDTA
-
1 mM, 16% inhibition
FeSO4
iodoacetamide
-
1 mM, 48% loss of activity
O-acetylserine
-
-
p-chloromercuribenzoate
-
1 mM, 59% inhibition
PCMB
-
1 mM, 97% loss of activity
Sulfide
-
-
Zn2+
-
1 mM, 94% inhibition
ZnCl2
-
1 mM, 88% loss of activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
slight activation
iodoacetamide
-
slight activation
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
acetyl-CoA
-
-
0.006 - 0.013
H2S
0.7
L-Ser
-
-
1.3 - 27
O-acetyl-L-Ser
0.6 - 0.7
O-acetyl-L-serine
0.133
sodium thiosulfate
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
733
O-acetyl-L-Ser
-
-
11 - 24
O-acetyl-L-serine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15 - 15
O-acetyl-L-serine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
160 - 340
acetate
8.6 - 48
cysteine
7.1 - 18
O-acetyl-L-Ser
0.011 - 0.11
S2-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150
-
pH 7.0, 37°C, 100 mM potassium phosphate
6.3
-
strain K 12
667
-
pH 7.5, 25°C, 50 mM potassium phosphate
728
-
25°C
8.1
-
transformed strain cysk
additional information
-
activity depends on presence of nucleophiles
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
-
assay at
7
-
assay at
7.2 - 9
-
-
8 - 9
-
free enzyme
9.5
-
enzyme bound to serine acetyltransferase
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
-
pH 6: about 55% of maximal activity, pH 10.0: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32893
2 * 32893, calculated from amino acid sequence
32600
-
2 * 32600, SDS-PAGE
64000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 32893, calculated from amino acid sequence
dimer
-
2 * 32600, SDS-PAGE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 100 mM sodium citrate, pH 5.6, 100 mM ammonium sulfate, 20% (w/v) PEG 4000
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
12 h, about 20% loss of activity
0 - 50
-
purified recombinant His-tagged enzyme, 1 h, completely stable at
0 - 60
-
1 h, pH 7.5, stable
20 - 40
-
12 h, stable
57 - 60
-
purified recombinant His-tagged enzyme, 1 h, 50% activity remaining
60
-
12 h, about 15% loss of activity
70
-
purified recombinant His-tagged enzyme, 1 h, inactivation
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-dioxane
-
the activity of enzyme OASS-B gradually decreases as the content of organic solvent increases
N,N-dimethylformamide
-
the activity of enzyme OASS-B gradually decreases as the content of organic solvent increases
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Source 30Q column chromatography and Superdex 75 gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography and gel filtration
-
using a GSTrap 4 B column and anion-exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed as a GST-fusion protein
-
overexpressed in Escherichia coli using pUC19 with a lacUV5 promoter
-
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
enzme OASS produces novel beta-substituted L-amino acids when offered unnatural nucleophiles instead of sulfid, which is useful in producing pharmaceuticals, such as mucolytic agent L-carbocisteine and building blocks for the synthesis of pharmaceuticals and agrochemicals
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
FEBS Lett.
591
1212-1224
2017
Escherichia coli (P0ABK5), Escherichia coli, Escherichia coli K12 (P0ABK5)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team