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2.5.1.47: cysteine synthase

This is an abbreviated version!
For detailed information about cysteine synthase, go to the full flat file.

Word Map on EC 2.5.1.47

Reaction

O-acetyl-L-serine
+
hydrogen sulfide
=
L-cysteine
 +
acetate

Synonyms

(OAS-TL)-like protein, acetylserine sulfhydrylase, At-OASS, ATCC 23270 protein, BAbS19_I09950, beta-cyano-alanine synthase, beta-cyano-L-alanine synthase, CS-A, CS-B, CS1, CS26, CS3, CSase, CSase A, CSase B, CSaseLP, CSC, Cys synthase complex, cysK, CysK1, CysK2, CYSL, CysL-1, cysl-2, CysM, Cysteine synthase, cysteine synthase 1, cysteine synthase A, cysteine synthase B, cysteine synthase, chloroplastic/chromoplastic, cysteine synthase, mitochondrial, cysteine synthetase, DcsD, EC 4.2.99.8, EhCS, EhCS1, EhCS3, EhOASS, Fn1220, GmOAS-TL1, GmOAS-TL2, GmOAS-TL3, GmOAS-TL4, GmOAS-TL6, GmOAS-TL7, GmOASTL4, GsOAS-TL1, GYY4137, HiOASS, HiOASS-A, lanthionine synthase, LbrCS, MCSA1, Nt-OAS-TL, O -acetylserine (thiol)-lyase, O-acetyl-L-serine (thiol) lyase, 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-acetyl-serine (thiol) lyase, O-acetylserine (thiol) lyase, O-acetylserine (Thiol)-lyase, O-acetylserine (thiol)-lyase A, O-acetylserine (thiol)-lyase B, O-acetylserine (thiol)lyase, O-acetylserine sulfhydrylase, O-acetylserine sulfhydrylase A, O-acetylserine sulfhydrylase B, O-acetylserine sulfhydrylase isoenzyme B, O-acetylserine sulfhydrylase-A, O-acetylserine sulfhydrylase-B, O-acetylserine thiol lyase, O-acetylserine(thiol)lyase, O-acetylserine-(thiol)lyase, O-acetylserine-O-acetylhomoserine sulfhydro-lyase, O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase, OAS Shase, OAS thiol-lyases, OAS-TL, OAS-TL A, OAS-TL B, OAS-TL C, OASA1, OASB, OASS, OASS-A, OASS-B, OASTL, OASTL-A, OASTL-A1, old3-1, OPSS, Os01g0290600, Os03g53650, protein ONSET OF LEAF DEATH 3, RCS3, S-sulfocysteine synthase, SSC synthase, StOASTL A, StOASTL B, sulfhydrylase/cysteine synthase, synthase, cysteine, TvCS1

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.47 cysteine synthase

Inhibitors

Inhibitors on EC 2.5.1.47 - cysteine synthase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,2R)-1-(4-chlorobenzyl)-2-phenylcyclopropanecarboxylic acid
-
(1R,2R)-1-(4-methylbenzyl)-2-phenylcyclopropanecarboxylic acid
-
(1R,2R)-1-benzyl-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-ethyl-2-phenylcyclopropanecarboxylic acid
-
(1S,2R)-1-ethyl-2-phenylcyclopropanecarboxylic acid
-
(1S,2S)-1-(4-chlorobenzyl)-2-phenylcyclopropanecarboxylic acid
-
(1S,2S)-1-(4-methylbenzyl)-2-phenylcyclopropanecarboxylic acid
-
(1S,2S)-1-benzyl-2-phenylcyclopropanecarboxylic acid
-
(NH4)6Mo7O24
1,1'-(1,3-propanediyl)bis(5-benzyl-6-methylsulfanyl-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one)
-
-
1,1'-(1,3-propanediyl)bis(5-ethyl-6-methylthio-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one)
-
-
1,1'-(1,3-propanediyl)bis(5-methyl-6-methylthio-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one)
-
-
1,10-phenanthroline
-
14% inhibition at 1 mM
1,3-bis(4,6-diethylthio-1H-pyrazolo[3,4-d]pyrimidin-1-yl)propane
-
-
1,3-bis(4-ethoxy-6-methyl-sulfanyl-1H-pyrazolo[3,4-d]pyrimidin-1-yl)propane
-
-
1-(2-naphthylsulfonyl)-3-phenyl-1H-pyrazolo[3,4-d]pyrimidin-4-amine
-
-
1-(4,6-dimethylsulfanyl-1H-pyrazolo[3,4-d]pyrimidin-1-yl)-3-(5-methyl-6-methylsulfanyl-4-oxo-1,5-dihydropyrazolo[3,4-d]pyrimidin-1-yl)propane
-
-
1-(4-chlorophenyl)-1H-pyrazole-5-carboxylic acid
9% inhibition at 1 microM, 56% inhibition at 1 mM
1-(4-fluorophenyl)-1H-pyrazole-5-carboxylic acid
8% inhibition at 1 microM, 95% inhibition at 1 mM; 8% inhibition at 1 microM, 95% inhibition at 1 mM
1-ethyl-4-nitro-1H-pyrazole-5-carboxylic acid
-
1-N,4-N-bis[3-(1Hbenzimidazol-2-yl) phenyl]benzene-1,4-dicarboxamide
determined as potential inhibitor via computational inhibitor screening, molecular dynamics simulation and homology modeling
1-phenyl-1H-pyrazole-5-carboxylic acid
11% inhibition at 1 microM, 65% inhibition at 1 mM
-
1-[(2,5-dichlorophenyl)sulfonyl]-3-phenyl-1Hpyrazolo[3,4-d]pyrimidine-4-amine
-
-
1-[(4-chlorophenyl)sulfonyl]-3-phenyl-1H-pyrazolo[3,4-d]pyrimidine-4-amine
-
-
1-[(4-nitrophenyl)sulfonyl]-3-phenyl-1H-pyrazolo[3,4-d]pyrimidine-4-amine
-
-
1H-pyrazole-5-carboxylic acid
9% inhibition at 1 microM, 94% inhibition at 1 mM
2,2'-(1,2,4-thiadiazole-3,5-diyldisulfanediyl)diacetic acid
-
2,2'-(5-ethyl-5-nitrodihydropyrimidine-1,3(2H,4H)-diyl)diacetic acid
-
2-[(1-methyl-1H-tetrazol-5-yl)sulfanyl]pyridine-3-carboxylic acid
-
2-[(5-methyl-1,3,4-thiadiazol-2-yl)carbamoyl]-3-nitrobenzoic acid
-
3,3'-[(phenylsulfonyl)imino]dipropanoic acid (non-preferred name)
-
3-(morpholin-4-ylmethyl)furan-2-carboxylic acid
-
3-phenyl-1-(methylsulfonyl)-1H-pyrazolo[3,4-d]pyrimidine-4-amine
-
-
3-phenyl-1-(phenylsulfonyl)-1H-pyrazolo[3,4-d]pyrimidine-4-amine
-
-
3-phenyl-1-tosyl-1H-pyrazolo[3,4-d] pyrimidin-4-amine
-
-
3-phenyl-1H-pyrazolo[3,4-d]pyrimidin-4-amine
-
-
3-[[(3,4-dichlorophenyl)carbamoyl]amino]benzoic acid
inhibits both isoforms CysK1 and CysK2 and O-phosphoserine sulfhydrylase CysM
3-[[([1,1'-biphenyl]-3-yl)carbamoyl]amino]benzoic acid
inhibits both isoforms CysK1 and CysK2 and O-phosphoserine sulfhydrylase CysM
4,6-bis(methylsulfanyl)-1-phthalimidopropyl-1H-pyrazolo[3,4-d]-pyrimidine
-
-
4-(2-methylphenyl)-8-nitro-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one
minimum inhibitory concentration against Mycobacterium tuberculosis 0.0335 mM, cytotoxicity against HEK 293T cell 3.6% at 0.025 mM
4-(4-methoxyphenyl)-8-nitro-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one
minimum inhibitory concentration against Mycobacterium tuberculosis 0.0321 mM, cytotoxicity against HEK 293T cell 0.2% at 0.025 mM
4-(methylsulfinyl)-2-[(phenylsulfonyl)amino]butanoic acid
-
4-hydroxy-2-[2-(1H-indol-3-yl)-2-oxoethyl]sulfanyl-1H-pyrimidin-6-one
inhibitor identified by molecular docking. Conserved residues involved in hydrogen bonding interaction include T85, S86, Q159, G87, R116, and G236. The compound displays a binding affinity of 8.05 microM and inhibits about 73% activity at 0.1 mM
4-[[(3,4-dichlorophenyl)carbamoyl]amino]-2-hydroxybenzoic acid
selective for isoform CysK1, IC50 value for isoform CysK2 above 300 microM
4-[[([1,1'-biphenyl]-3-yl)carbamoyl]amino]-2-hydroxybenzoic acid
inhibits both isoforms CysK1 and CysK2 and O-phosphoserine sulfhydrylase CysM
5,5'-dithiobis(2-nitrobenzoic acid)
5-[[(3,4-dichlorophenyl)carbamoyl]amino]-2-hydroxybenzoic acid
inhibits both isoforms CysK1 and CysK2
5-[[([1,1'-biphenyl]-3-yl)carbamoyl]amino]-2-hydroxybenzoic acid
inhibits both isoforms CysK1 and CysK2 and O-phosphoserine sulfhydrylase CysM
6-(1,3,4-thiadiazol-2-ylcarbamoyl)cyclohex-3-ene-1-carboxylic acid
-
6-methyl-4,5,6,7-tetrahydro-1,2-benzoxazole-5,6-dicarboxylic acid
-
6-methyl-7-oxo-6-azabicyclo[3.2.1]oct-2-ene-2,8-dicarboxylic acid
-
6-methylsulfanyl-1-(3-phenylpropyl)-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one
-
-
6-methylsulfanyl-1-phthalimidopropyl-4(pyrrolidin-1-yl)-1H-pyrazolo[3,4-d]pyrimidine
-
-
6-[(pyridin-4-ylmethyl)carbamoyl]cyclohex-3-ene-1-carboxylic acid
-
8-nitro-4-(2-nitrophenyl)-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one
minimum inhibitory concentration against Mycobacterium tuberculosis 0.0309 mM, cytotoxicity against HEK 293T cell 1% at 0.025 mM
8-nitro-4-[2-(trifluoromethyl)phenyl]-4,4a-dihydro-2H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidine-2,5(3H)-dione
minimum inhibitory concentration against Mycobacterium tuberculosis 0.0076 mM, cytotoxicity against HEK 293T cell 5.7% at 0.025 mM
acetate
-
-
AgNO3
Aminooxyacetate
cadmium chloride
Cd2+
-
55% inhibition at 1 mM
chloroalanine
-
substrate inhibition
Co2+
-
complete inhibition at 1 mM
copper sulfate
CuSO4
-
1 mM, 99% loss of activity
cystathionine
cystine
competitive versus O-acetyl-L-serine, the cystine-binding residues are highly conserved in all OASS proteins; competitive versus O-acetyl-L-serine, the cystine-binding residues are highly conserved in all OASS proteins. Active site of CysK2–cystine binding structure, overview. Cystine occupies the substrate/product binding site of the enzyme
D-cycloserine
-
82% loss of activity at 5 mM
deacetylkinamycin C
-
deoxyfrenolicin
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
exophillic acid
from Exophiala sp.FKI-7082 , specific for isozyme CS1
FeSO4
hydroxylamine
iodoacetamide
-
1 mM, 48% loss of activity
KCN
-
15.6% inhibition by 1 mM
L-cysteine
L-homocysteine
-
competitive to sulfide
L-homoserine
lead nitrate
methionine
metronidazole
-
-
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
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
Monoiodoacetic acid
-
1 mM, complete inactivation
N-[(2,2-dimethyl-4,6-dioxo-1,3-dioxan-5-ylidene)methyl]glutamic acid
-
N-[(2,2-dimethyl-4,6-dioxo-1,3-dioxan-5-ylidene)methyl]leucine
-
N-[(3-carboxybicyclo[2.2.1]hept-5-en-2-yl)carbonyl]glycylglycine
-
N-{4-[(4-amino-3-phenyl-1H-pyrazolo[3,4-d]pyrimidin-1-yl)sulfonyl]phenyl}acetamide
-
-
NEM
-
non-competitive
NH2OH
-
97% loss of activity at 10 mM
O-acetylserine
ornidazole
-
-
p-chloromercuribenzoate
p-chloromercuriphenylsulfonic acid
-
46% inhibition at 1 mM
p-hydroxymercuribenzoate
-
-
PCMB
-
1 mM, 97% loss of activity
pencolide
shows cysteine deprivation-dependent antiamebic activity,with 7.6 times lower IC50 in the absence of cysteine than that in the presence of cysteine; shows cysteine deprivation-dependent antiamebic activity,with 7.6 times lower IC50 in the absence of cysteine than that in the presence of cysteine
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
Semicarbazide
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
Sodium borohydride
-
59% inhibition at 1 mM
Sulfide
Thiourea
-
34% inhibition at 1 mM
tinidazole
-
-
trans-1-(4-chlorobenzyl)-2-phenylcyclopropanecarboxylic acid
-
trans-1-(4-methylbenzyl)-2-phenylcyclopropanecarboxylic acid
-
trans-1-benzyl-2-phenylcyclopropanecarboxylic acid
-
trans-1-ethyl-2-phenylcyclopropanecarboxylic acid
-
trans-1-phenethyl-2-phenylcyclopropanecarboxylic acid
-
trans-2-phenylcyclopropanecarboxylic acid
-
trichloroacetic acid
inactivation at 16.6% v/v; inactivation at 16.6% v/v
trifluoroalanine
irreversible but weak inhibitor; irreversible but weak inhibitor
xanthofulvin
from Penicillium sp. if08054; from Penicillium sp. if08054 , inhibits isozymes CS1 and CS3
ZnCl2
-
1 mM, 88% loss of activity
[2-[3-acetyl-1-(2,2-dihydroxyethyl)-4-hydroxy-5-oxo-2,5-dihydro-1H-pyrrol-2-yl]phenyl](hydroxy)oxoammonium
-
[3-[(2-carboxy-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-en-7-yl)carbamoyl]-1-methyl-1H-pyrazol-4-yl](hydroxy)oxoammonium
-
[3-[(2-carboxypiperidin-1-yl)sulfonyl]phenyl](hydroxy)oxoammonium
-
additional information
-