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Information on EC 2.5.1.47 - cysteine synthase and Organism(s) Arabidopsis thaliana and UniProt Accession P47998

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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:
Arabidopsis thaliana
UNIPROT: P47998
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
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
(OAS-TL)-like protein
-
cysteine synthase 1
UniProt
O-acetylserine (thiol) lyase
-
O-acetylserine sulfhydrylase
-
O-acetylserine sulfhydrylase A
-
O-acetylserine(thiol)lyase
-
protein ONSET OF LEAF DEATH 3
-
(OAS-TL)-like protein
-
acetylserine sulfhydrylase
-
-
-
-
CSase
-
-
-
-
cysteine synthase, chloroplastic/chromoplastic
UniProt
cysteine synthase, mitochondrial
UniProt
cysteine synthetase
-
-
-
-
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
-
-
-
-
O-acetylserine (thiol)lyase
-
-
-
-
O-acetylserine sulfhydrylase
-
-
-
-
O-acetylserine sulfhydrylase A
-
-
-
-
O-acetylserine(thiol)lyase
O-acetylserine-O-acetylhomoserine sulfhydro-lyase
-
-
-
-
O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
-
OAS Shase
-
-
-
-
OAS-TL
OASS
-
-
-
-
OASTL
-
-
-
-
S-sulfocysteine synthase
-
-
-
-
synthase, cysteine
-
-
-
-
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
O-acetyl-L-Ser + H2S
L-Cys + acetate
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 + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate
show the reaction diagram
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-
-
-
-
?
O3-acetyl-L-serine + hydrogensulfide
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
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
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Aminooxyacetate
-
10 mM, 76% inhibition
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
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.37 - 0.55
H2S
3 - 6.4
hydrogen sulfide
0.64 - 4.28
O-acetyl-L-Ser
0.46
O-acetyl-L-serine
-
-
0.31 - 10.2
O3-acetyl-L-serine
0.18 - 5.7
Sulfide
0.93
thiosulfate
-
-
additional information
additional information
-
HPLC method for product quantification
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 1780
O3-acetyl-L-serine
0.22 - 2170
Sulfide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
550
-
isoform C, pH 7.5, 25°C
590
-
isoform B, pH 7.5, 25°C
900
-
isoform A, pH 7.5, 25°C
additional information
-
activity modified by protein-protein interactions within cystein synthase complex
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
root plasma membrane SO42- transporter SULTR1,2 physically interacts with the enzyme
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
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
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
-
presence of an active CS26 enzyme exclusively in the thylakoid lumen
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
malfunction
metabolism
physiological function
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CYSK1_ARATH
322
0
33805
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
300000
-
bienzyme complex with serine acetyltransferase, gel filtration
36000
-
2 * 36000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
LITERATURE
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
native protein and mutant K46A with pyridoxal 5’-phosphate and methionine covalently linked as an external aldimine
-
to elucidate the structural basis of protein–protein 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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G162E
naturally occuring mutation, the EMS-induced single nucleotide substitution in the cytosolic OASTL-A1 gene in the Ler-0 accession of Arabidopsis thaliana causes early senescence and death in plants, and is referred to as onset of leaf death3 (old3-1)
H157N
-
comparable to wild-type
H157Q
-
reduced kcat-value, reduced Km-value
K46A
-
no enzymic activity, crystallization data
N77A
-
reduced kcat-value
N77D
-
drastically reduced kcat-value
Q147A
Q147E
-
drastically reduced kcat-value, increased Km-value
S269A
-
reduced kcat-value, reduced Km-value
S269T
-
reduced kcat-value, reduced Km-value
S75N
-
drastically reduced kcat-value
T182A
-
reduced kcat-value
T182S
-
comparable to wild-type
T185A
-
drastically reduced kcat-value
T185S
-
drastically reduced kcat-value
T74A
-
drastically reduced kcat-value
T78A
-
reduced kcat-value, reduced Km-value
T78S
-
reduced kcat-value, reduced Km-value
Y302A
-
loss of enzymic activity
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein of isoforms A,B,C
-
using Ni-NTA chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein
-
gene OASC, ssemi-quantitative RT-PCR isozyme expression analysis
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Droux, M.; Ruffet, M.L.; Douce, R.; Job, D.
Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants. Structural and kinetic properties of the free and bound enzymes
Eur. J. Biochem.
255
235-245
1998
Arabidopsis thaliana
Manually annotated by BRENDA team
Noji, M.; Saito, K.
Molecular and biochemical analysis of serine acetyltransferase and cysteine synthase towards sulfur metabolic engineering in plants
Amino Acids
22
231-243
2002
Arabidopsis thaliana, Spinacia oleracea, Triticum aestivum, Zea mays
Manually annotated by BRENDA team
Hell, R.; Bork, C.; Bogdanova, N.; Frolov, I.; Hauschild, R.
Isolation and characterization of two cDNAs encoding for compartment specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis thaliana
FEBS Lett.
351
257-262
1994
Arabidopsis thaliana
Manually annotated by BRENDA team
Romero, L.C.; Dominguez-Solis, J.R.; Gutierrez-Alcala, G.; Gotor, C.
Salt regulation of O-acetylserine(thiol)lyase in Arabidopsis thaliana and increased tolerance in yeast
Plant Physiol. Biochem.
39
643-647
2001
Arabidopsis thaliana
-
Manually annotated by BRENDA team
Mino, K.; Ishikawa, K.
Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1
J. Bacteriol.
185
2277-2284
2003
Aeropyrum pernix, Arabidopsis thaliana
Manually annotated by BRENDA team
Bonner, E.R.; Cahoon, R.E.; Knapke, S.M.; Jez, J.M.
Molecular basis of cysteine biosynthesis in plants: Structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana
J. Biol. Chem.
280
38803-38813
2005
Arabidopsis thaliana
Manually annotated by BRENDA team
Wirtz, M.; Droux, M.; Hell, R.
O-acetylserine (thiol) lyase: an enigmatic enzyme of plant cysteine biosynthesis revisited in Arabidopsis thaliana
J. Exp. Bot.
55
1785-1798
2004
Arabidopsis thaliana
Manually annotated by BRENDA team
Kumaran, S.; Jez, J.M.
Thermodynamics of the interaction between O-acetylserine sulfhydrylase and the C-terminus of serine acetyltransferase
Biochemistry
46
5586-5594
2007
Arabidopsis thaliana
Manually annotated by BRENDA team
Francois, J.A.; Kumaran, S.; Jez, J.M.
Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex
Plant Cell
18
3647-3655
2006
Arabidopsis thaliana
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
Heeg, C.; Kruse, C.; Jost, R.; Gutensohn, M.; Ruppert, T.; Wirtz, M.; Hell, R.
Analysis of the Arabidopsis O-acetylserine(thiol)lyase gene family demonstrates compartment-specific differences in the regulation of cysteine synthesis
Plant Cell
20
168-185
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Lopez-Martin, M.C.; Becana, M.; Romero, L.C.; Gotor, C.
Knocking out cytosolic cysteine synthesis compromises the antioxidant capacity of the cytosol to maintain discrete concentrations of hydrogen peroxide in Arabidopsis
Plant Physiol.
147
562-572
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Bermudez, M.A.; Paez-Ochoa, M.A.; Gotor, C.; Romero, L.C.
Arabidopsis S-sulfocysteine synthase activity is essential for chloroplast function and long-day light-dependent redox control
Plant Cell
22
403-416
2010
Arabidopsis thaliana
Manually annotated by BRENDA team
Wirtz, M.; Heeg, C.; Samami, A.A.; Ruppert, T.; Hell, R.
Enzymes of cysteine synthesis show extensive and conserved modifications patterns that include Nalpha-terminal acetylation
Amino Acids
39
1077-1086
2010
Arabidopsis thaliana
Manually annotated by BRENDA team
Shibagaki, N.; Grossman, A.R.
Binding of cysteine synthase to the STAS domain of sulfate transporter and its regulatory consequences
J. Biol. Chem.
285
25094-25102
2010
Arabidopsis thaliana
Manually annotated by BRENDA team
Alvarez, C.; Lozano-Juste, J.; Romero, L.C.; Garcia, I.; Gotor, C.; Leon, J.
Inhibition of Arabidopsis O-acetylserine(thiol)lyase A1 by tyrosine nitration
J. Biol. Chem.
286
578-586
2011
Arabidopsis thaliana
Manually annotated by BRENDA team
Wirtz, M.; Beard, K.F.; Lee, C.P.; Boltz, A.; Schwarzlaender, M.; Fuchs, C.; Meyer, A.J.; Heeg, C.; Sweetlove, L.J.; Ratcliffe, R.G.; Hell, R.
Mitochondrial cysteine synthase complex regulates O-acetylserine biosynthesis in plants
J. Biol. Chem.
287
27941-27947
2012
Arabidopsis thaliana
Manually annotated by BRENDA team
Bermudez, M.A.; Galmes, J.; Moreno, I.; Mullineaux, P.M.; Gotor, C.; Romero, L.C.
Photosynthetic adaptation to length of day is dependent on S-sulfocysteine synthase activity in the thylakoid lumen
Plant Physiol.
160
274-288
2012
Arabidopsis thaliana
Manually annotated by BRENDA team
Gotor, C.; Romero, L.C.
S-sulfocysteine synthase function in sensing chloroplast redox status
Plant Signal. Behav.
8
e23313
2013
Arabidopsis thaliana (O22682), Arabidopsis thaliana
Manually annotated by BRENDA team
Feldman-Salit, A.; Wirtz, M.; Lenherr, E.D.; Throm, C.; Hothorn, M.; Scheffzek, K.; Hell, R.; Wade, R.C.
Allosterically gated enzyme dynamics in the cysteine synthase complex regulate cysteine biosynthesis in Arabidopsis thaliana
Structure
20
292-302
2012
Arabidopsis thaliana
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
Tahir, J.; Watanabe, M.; Jing, H.; Hunter, D.; Tohge, T.; Nunes-Nesi, A.; Brotman, Y.; Fernie, A.; Hoefgen, R.; Dijkwel, P.
Activation of R-mediated innate immunity and disease susceptibility is affected by mutations in a cytosolic O-acetylserine (thiol) lyase in Arabidopsis
Plant J.
73
118-130
2013
Arabidopsis thaliana (P47998)
Manually annotated by BRENDA team
Birke, H.; Heeg, C.; Wirtz, M.; Hell, R.
Successful fertilization requires the presence of at least one major O-acetylserine(thiol)lyase for cysteine synthesis in pollen of Arabidopsis
Plant Physiol.
163
959-972
2013
Arabidopsis thaliana (P47998), Arabidopsis thaliana (P47999), Arabidopsis thaliana (Q43725)
Manually annotated by BRENDA team
Wawrzynska, A.; Kurzyk, A.; Mierzwinska, M.; Plochocka, D.; Wieczorek, G.; Sirko, A.
Direct targeting of Arabidopsis cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis
Plant Sci.
207
148-157
2013
Arabidopsis thaliana (Q43725), Arabidopsis thaliana
Manually annotated by BRENDA team
Mueller, S.M.; Wang, S.; Telman, W.; Liebthal, M.; Schnitzer, H.; Viehhauser, A.; Sticht, C.; Delatorre, C.; Wirtz, M.; Hell, R.; Dietz, K.J.
The redox-sensitive module of cyclophilin 20-3, 2-cysteine peroxiredoxin and cysteine synthase integrates sulfur metabolism and oxylipin signaling in the high light acclimation response
Plant J.
91
995-1014
2017
Arabidopsis thaliana (P47999)
Manually annotated by BRENDA team