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 hide
2.5.1.47
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RECOMMENDED NAME
GeneOntology No.
cysteine synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-O bond cleavage
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elimination
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-cysteine biosynthesis I
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seleno-amino acid biosynthesis
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cysteine metabolism
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Cysteine and methionine metabolism
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Sulfur metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
animal
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Automatic Mining of ENzyme DAta
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain Sp7
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain 10-1
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Manually annotated by BRENDA team
strain 10-1
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
halophilic bacterium
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
protozoa
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Automatic Mining of ENzyme DAta
strain P169-4A
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Manually annotated by BRENDA team
subsp. enterica serovar Typhimurium
UniProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
strain 6301, two isoenzymes
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Manually annotated by BRENDA team
strain 6301, two isoenzymes
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Xanthium pennsylvanicum
three isoforms
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Manually annotated by BRENDA team
yeasts
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Automatic Mining of ENzyme DAta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
-
-
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-
?
beta-chloro-L-alanine + 2-nitro-5-thiobenzoate
?
show the reaction diagram
-
-
-
-
?
chloroalanine + sulfide
cysteine + chloride
show the reaction diagram
cyanide + cysteine
beta-cyanoalanine + sulfide
show the reaction diagram
-
-
-
?
cysteine + CN-
cyanoalanine + H2S
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
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L-Cys + acetate
O-acetyl-L-Ser + H2S
show the reaction diagram
L-Cys + dithiothreitol
beta-cyanoalanine + H2S
show the reaction diagram
-
-
-
?
L-cysteine + cyanide
cyanoalanine + H2S
show the reaction diagram
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
show the reaction diagram
L-homocysteine + L-serine
L-cystathionine + H2O
show the reaction diagram
-
-
-
?
L-homoserine + sulfide
?
show the reaction diagram
-
1.6% of the activity with O-acetyl-L-serine
-
-
?
NaN3 + O-acetyl-Ser
beta-azidoalanine + sodium acetate
show the reaction diagram
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
-
-
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-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
show the reaction diagram
O-acetyl-L-Ser + 3-mercapto-1,2,4-triazole
?
show the reaction diagram
-
-
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?
O-acetyl-L-Ser + 5-mercapto-2-nitrobenzoate
S-(3-carboxy-4-nitrophenyl)-L-cysteine + ?
show the reaction diagram
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-
-
?
O-acetyl-L-Ser + benzenethiol
L-cys + benzylacetate
show the reaction diagram
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?
O-acetyl-L-Ser + cysteamine
?
show the reaction diagram
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weak activity
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-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
O-acetyl-L-Ser + isoxazylin-5-one
?
show the reaction diagram
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
show the reaction diagram
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + 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
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?
O-acetyl-L-Ser + S2O32-
S-sulfocysteine + ?
show the reaction diagram
O-acetyl-L-Ser + sodium azide
?
show the reaction diagram
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weak activity
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?
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-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 + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
show the reaction diagram
O-acetyl-L-serine + sulfide
L-Cys + acetate
show the reaction diagram
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?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate
show the reaction diagram
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate + H+
show the reaction diagram
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?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + sodium acetate
show the reaction diagram
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?
O-acetyl-Ser + selenide
selenocysteine + acetate
show the reaction diagram
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maximal 40% rate of cysteine synthesis
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?
O-acetylhomoserine + H2S
homocysteine + ?
show the reaction diagram
O-diazoacetyl-L-serine + sulfide
?
show the reaction diagram
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44% of the activity with O-acetyl-Ser
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?
O-phosphoserine + H2S
L-Cys + phosphate
show the reaction diagram
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?
O-succinyl-L-homoserine + sulfide
?
show the reaction diagram
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3.6% of the activity with O-acetyl-L-serine
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?
O3-acetyl-L-serine
alpha-aminoacrylate
show the reaction diagram
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in absence of S2- and at 50C, not below
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?
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 + benzylmercaptan
S-benzyl-L-cysteine + acetate
show the reaction diagram
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?
O3-acetyl-L-serine + cyanide
beta-cyano-L-alanine + acetate
show the reaction diagram
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?
O3-acetyl-L-serine + ethylmercaptan
S-ethyl-L-cysteine + acetate
show the reaction diagram
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?
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
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?
O3-acetyl-L-serine + methylmercaptan
S-methyl-L-cysteine + acetate
show the reaction diagram
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?
O3-acetyl-L-serine + phenol
O-phenyl-L-serine + acetate
show the reaction diagram
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?
O3-acetyl-L-serine + phenylmercaptan
S-phenyl-L-cysteine + acetate
show the reaction diagram
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?
O3-acetyl-L-serine + propylmercaptan
S-propyl-L-cysteine + acetate
show the reaction diagram
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?
O3-acetyl-L-serine + sulfide
L-cysteine + acetate
show the reaction diagram
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?
Ser + sulfide
?
show the reaction diagram
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1.8% of the activity with O-acetyl-L-serine
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cysteine + CN-
cyanoalanine + H2S
show the reaction diagram
Xanthium pennsylvanicum
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involved in cyanide metabolism during seed germination
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L-Cys + acetate
?
show the reaction diagram
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involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear
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L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
show the reaction diagram
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the side reaction of the enzyme seems to contribute massively to the total H2S release of higher plants at least at higher pH values
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O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
O-acetyl-L-Ser + isoxazylin-5-one
?
show the reaction diagram
O-acetyl-L-Ser + S2O32-
S-sulfocysteine + ?
show the reaction diagram
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 + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
P16703
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?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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slight activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)6Mo7O24
1,10-phenanthroline
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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
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-hydroxy-2-[2-(1H-indol-3-yl)-2-oxoethyl]sulfanyl-1H-pyrimidin-6-one
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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)
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
AgNO3
Aminooxyacetate
cadmium chloride
Cd2+
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55% inhibition at 1 mM
chloroalanine
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substrate inhibition
Co2+
-
complete inhibition at 1 mM
copper sulfate
CuSO4
-
1 mM, 99% loss of activity
cystathionine
D-cycloserine
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82% loss of activity at 5 mM
DYVI
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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
hydroxylamine
iodoacetamide
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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
MNDGI
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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
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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
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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
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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
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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
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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
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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
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pentapeptide inhibitor; wild type pentapeptide of serine acetyltransferase
MNPHI
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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
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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
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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
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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
Monoiodoacetic acid
-
1 mM, complete inactivation
NEM
-
non-competitive
O-acetylserine
p-chloromercuribenzoate
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
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
ZnCl2
-
1 mM, 88% loss of activity
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
slight activation
iodoacetamide
-
slight activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018 - 2.5
5-thio-2-nitrobenzoate
0.12
acetyl-CoA
0.785 - 1.053
chloroalanine
14.2 - 15.1
CN-
0.0384 - 0.201
cysteine
0.7
dithiothreitol
pH 7.4, 37C
6.7
H2S
pH 7.4, 37C
0.12 - 6.4
hydrogen sulfide
0.7 - 0.8
L-Cys
0.25
L-cysteine
pH 7.5, 45C
0.7
L-Ser
0.029 - 0.8
Na2S
5.2
NaCN
-
pH 7.4, 30C
2.3
NaN3
-
pH 7.6, 25C
0.037 - 50
O-acetyl-L-Ser
0.063 - 15
O-acetyl-L-serine
6.67
O-acetylhomoserine
-
-
1.03 - 1.355
O-acetylserine
227
O-phosphoserine
-
37C, pH 7.8
0.11 - 16
O3-acetyl-L-serine
0.006 - 5.2
S2-
0.133
sodium thiosulfate
-
-
0.031 - 5.7
Sulfide
0.93 - 22
thiosulfate
additional information
additional information
-