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Information on EC 2.5.1.47 - cysteine synthase
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2.5.1.47 cysteine synthaseIUBMB 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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Word Map
- 2.5.1.47
- h2s
- sulfur
- l-cysteine
- gsh
-
gamma-glutamyl
- acetyltransferase
- pyridoxal
-
slow-releasing
- typhimurium
- 5'-phosphate
-
gasotransmitter
-
o-acetylserinethiollyase
- nahs
- sulfite
-
gaseous
-
schiff
-
buthionine
- sulfoximine
- phytochelatins
-
assimilatory
-
plp-dependent
- desulfhydrase
-
h2s-releasing
- alpha-aminoacrylate
- thiosulfate
- oxygenase-1
- gamma-gcs
- sulphide
- dl-propargylglycine
-
transsulfuration
-
bienzyme
- 3-mercaptopyruvate
-
5'-phosphate-dependent
- beta-synthase
-
h2s-producing
-
sulfurylase
-
aldimine
-
beta-replacement
-
gamma-lyase
- sulfurtransferase
- cysb
- hydrosulfide
- biotechnology
- agriculture
- synthesis
- pharmacology
- medicine
- environmental protection
- drug development
- analysis
The enzyme appears in viruses and cellular organisms
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylserine sulfhydrylase
-
-
-
-
BAbS19_I09950
CS1
CS26
CSase
CSase A
CSase B
Cys synthase complex
-
serine acetyltransferase (EC 2.3.1.30) and O-acetylserine thiol lyase reversibly form the heterooligomeric Cys synthase complex
cysK
CysK1
CysK2
CysM
Cysteine synthase
cysteine synthase A
cysteine synthase B
cysteine synthetase
-
-
-
-
DcsD
EC 4.2.99.8
-
-
formerly
-
Fn1220
lanthionine synthase
LbrCS
O -acetylserine (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-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-A
O-acetylserine sulfhydrylase-B
O-acetylserine(thiol)lyase
O-acetylserine-O-acetylhomoserine sulfhydro-lyase
-
-
-
-
O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
-
OAS Shase
-
-
-
-
OAS-TL
OAS-TL A
OAS-TL B
OASS
OASS-A
OASS-B
OASTL
OASTL-A
OASTL-A1
S-sulfocysteine synthase
-
-
-
-
SSC synthase
synthase, cysteine
-
-
-
-
CSase
-
-
-
-
cysK
-
O-acetyl-L-serine sulfhydrylase
-
-
-
-
O-acetylserine sulfhydrylase
-
-
-
-
O-acetylserine sulfhydrylase
-
cysteine synthase is a multiprotein assembly formed by the pyridoxal 5'-phosphate-dependent enzyme O-acetylserine sulfhydrylase and serine acetyltransferase
O-acetylserine sulfhydrylase
-
-
O-acetylserine sulfhydrylase
-
O-acetylserine sulfhydrylase
-
O-acetylserine sulfhydrylase
-
-
O-acetylserine sulfhydrylase A
-
-
-
-
O-acetylserine sulfhydrylase A
-
O-acetylserine sulfhydrylase-A
-
O-acetylserine sulfhydrylase-B
-
O-acetylserine(thiol)lyase
-
-
-
-
OAS-TL
-
-
-
-
OASS
-
-
-
-
OASS-B
-
produced under unaerobic grwoth conditions in contrast to OASS-A
OASTL
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
mechanism
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
ping-pong bi-bi mechanism
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
mechanism interpreted in structural context, conformational changes during catalysis
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
mechanism similar to those of other pyridoxal enzymes
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
identification and spectral characterization of the external aldimine of the reaction, mechanism
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
mechanism of reverse reaction
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
model of reaction mechanism
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
geometric model of reaction, comparison isoenzyme CysK
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
ping-pong bi-bi mechanism
Escherichia coli W3110 / ATCC 27325
-
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
model of reaction mechanism
-
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-O bond cleavage
-
-
-
-
elimination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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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).
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CAS REGISTRY NUMBER
COMMENTARY
37290-89-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 L-cysteine
(2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) + H2S
-
-
-
?
3-chloro-L-alanine + NaHS
L-cysteine + ?
-
beta-replacement reaction, enzyme can be induced by 3-chloro-L-alanine
-
?
5-thio-2-nitrobenzoate + O-acetyl-L-serine
acetate + ?
-
-
-
-
?
L-Cys + acetate
?
-
involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear
-
-
?
L-homoserine + sulfide
?
-
1.6% of the activity with O-acetyl-L-serine
-
-
?
monofluoralanine + H2S
?
-
-
-
?
O-acetyl-L-Ser + 5-mercapto-2-nitrobenzoate
S-(3-carboxy-4-nitrophenyl)-L-cysteine + ?
-
-
-
?
O-acetyl-L-serine + H2S
pyruvate + acetate + NH3
-
-
-
?
O-acetyl-L-serine + sulfide
L-Cys + acetate
-
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate + H+
-
-
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + sodium acetate
-
-
-
-
?
O-acetyl-Ser + selenide
selenocysteine + acetate
-
maximal 40% rate of cysteine synthesis
-
?
O3-acetyl-L-serine
alpha-aminoacrylate
-
-
in absence of S2- and at 50°C, not below
-
?
O3-acetyl-L-serine + benzylmercaptan
S-benzyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + cyanide
beta-cyano-L-alanine + acetate
-
-
-
?
O3-acetyl-L-serine + ethylmercaptan
S-ethyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + methylmercaptan
S-methyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + phenol
O-phenyl-L-serine + acetate
-
-
-
?
O3-acetyl-L-serine + phenylmercaptan
S-phenyl-L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + propylmercaptan
S-propyl-L-cysteine + acetate
-
-
-
?
chloroalanine + sulfide
cysteine + chloride
-
3-6% of the activity of the cysteine synthase reaction
-
r
chloroalanine + sulfide
cysteine + chloride
-
beta-chloroalanine, 6% of the activity with O-acetyl-L-Ser
-
-
r
chloroalanine + sulfide
cysteine + chloride
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
beta-chloroalanine, 6% of the activity with O-acetyl-L-Ser
-
-
r
cysteine + CN-
cyanoalanine + H2S
Xanthium pennsylvanicum
-
involved in cyanide metabolism during seed germination
-
-
?
L-Cys + acetate
O-acetyl-L-Ser + H2S
-
-
-
r
L-Cys + acetate
O-acetyl-L-Ser + H2S
-
equilibrium constant
-
r
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
-
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
the side reaction of the enzyme seems to contribute massively to the total H2S release of higher plants at least at higher pH values
-
-
?
L-cysteine + L-cysteine
L-lanthionine + H2S
-
preferred reaction
-
-
?
L-cysteine + L-cysteine
L-lanthionine + H2S
-
preferred reaction
-
-
?
L-cysteine + L-homocysteine
L-cystathionine + H2S
-
-
-
?
NaN3 + O-acetyl-Ser
beta-azidoalanine + sodium acetate
-
-
mutagenic
?
NaN3 + O-acetyl-Ser
beta-azidoalanine + sodium acetate
-
-
mutagenic in Salmonella typhimurium
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
18% of activity with sulfide
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
6.2% of the activity with sulfide, isoenzyme 2
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
2.6% and 6.8% of the activity with sulfide, isoenzyme 1 and 2, respectively
-
-
?
O-acetyl-L-Ser + 2-propene-1-thiol
S-allyl-L-cysteine + ?
-
18% of activity with sulfide
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
enzyme that catalyzes the final step in cysteine biosynthesis. Cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
Entamoeba histolytica, the causative agent of human amoebiasis, is essentially anaerobic, requiring a small amount of oxygen for growth. It cannot tolerate the higher concentration of oxygen present in human tissues or blood. However, during tissue invasion it is exposed to a higher level of oxygen, leading to oxygen stress. Cysteine, which is a vital thiol in Entamoeba histolytica, plays an essential role in its oxygen-defence mechanisms. The major route of cysteine biosynthesis in this parasite is the condensation of O-acetylserine with sulfide by the de novo cysteine-biosynthetic pathway, which involves cysteine synthase (EhCS) as a key enzyme
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
yeast two-hybrid system for screening of a cDNA library of Nicotiana plumbaginifolia for clones encoding plant proteins interacting with two proteins of Escherichia coli: serine acetyltransferase (SAT, the product of cysE gene) and O-acetylserine (thiol) lyase A, also termed cysteine synthase (OASTL-A, the product of cysK gene). Two plant cDNA clones are identified when using the cysE gene as a bait
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
-
-
?
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
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
equilibrium constant
-
r
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
the second half of the OASS-A reaction is limited by the conformational change needed to open the active site and release the amino acid product. No quinonoid or geminal-diamine intermediates are detected. The amino acid external Schiff base of the enzyme is found to be very stable when the reaction is run in D2O
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
OASTL activity regulates not only Cys de novo synthesis but also its homeostasis
-
-
?
O-acetyl-L-Ser + isoxazolin-5-one
?
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
?
O-acetyl-L-Ser + isoxazolin-5-one
?
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
6.1% of activity with sulfide
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
2.2% of activity with sulfide, isoenzyme 1 and 2
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
2.3% and 1.6% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + mercaptoacetic acid
S-carboxymethyl-L-cysteine
-
2.5% of activity with sulfide
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
21.5% and 77% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
-
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
4% and 1% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
-
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
-
?
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
-
product identification uncertain
ir
O-acetyl-L-Ser + methyl mercaptan
S-methylcysteine + acetate
-
32% of activity with sulfide
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
6.84% and 7.64% of activity with sulfide, isoenzymes 1 and 2, respectively
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
12.3% of activity with sulfide
-
?
O-acetyl-L-Ser + NaCN
beta-cyanoalanine + sodium acetate
-
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
the cysteine synthase complex functions as a molecular sensor system that monitors the sulfur status of the cell and controls sulfate assimilation and cysteine synthesis according to the availability of sulfate
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in synthesis of antioxidants such as glutathione during fruit development
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in glutathione formation
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
controlled by feedback inhibition, adaptively significant as sulfide removal mechanism
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
repressed during growth with sulfide or thiosulfide as sulfur source
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
key role in metabolism of S-containing amino acids
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
functions as a Cys synthase rather than as a homocysteine synthase in vivo
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
enzyme transcription repressed by L-cystine, derepressed by limiting sulfide concentrations
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in thiosulfate assimilation
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
activity varies between sulfur sources, enzyme formation regulated by L-Cys concentration
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + thiosulfate
S-sulfocysteine + sodium acetate
-
-
-
?
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
o-acetyl-L-serine + H2S
L-cysteine + acetate
-
-
-
-
ir
o-acetyl-L-serine + H2S
L-cysteine + acetate
-
-
-
-
ir
o-acetyl-L-serine + H2S
L-cysteine + acetate
-
-
-
-
?
o-acetyl-L-serine + H2S
L-cysteine + acetate
-
-
-
-
?
o-acetyl-L-serine + H2S
L-cysteine + acetate
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
Escherichia coli W3110 / ATCC 27325
-
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
Escherichia coli W3110 / ATCC 27325
-
residue Arg210 near the entrance of the active site and is important for O-acetyl-L-serine substrate recognition
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate. The enzyme catalyzes the reaction with O-acetyl-L-serine and hydroxyurea with 80fold lower catalytic efficiency
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate. The enzyme catalyzes the reaction with O-acetyl-L-serine and hydroxyurea with 80fold lower catalytic efficiency
-
-
?
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
-
-
-
?
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetyl-L-serine + thiosulfate
S-sulfo-L-cysteine + acetate
the enzyme prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate
-
-
?
O-acetylhomoserine + H2S
homocysteine + ?
-
not, low molecular weight enzyme
-
-
?
O-acetylhomoserine + H2S
homocysteine + ?
-
2.4% of the activity with O-acetyl-L-Ser
-
-
?
O-acetylhomoserine + H2S
homocysteine + ?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
2.4% of the activity with O-acetyl-L-Ser
-
-
?
O-diazoacetyl-L-serine + sulfide
?
-
44% of the activity with O-acetyl-Ser
-
-
?
O-diazoacetyl-L-serine + sulfide
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
44% of the activity with O-acetyl-Ser
-
-
?
O-succinyl-L-homoserine + sulfide
?
-
3.6% of the activity with O-acetyl-L-serine
-
-
?
O-succinyl-L-homoserine + sulfide
?
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
3.6% of the activity with O-acetyl-L-serine
-
-
?
O3-acetyl-L-serine + 2-nitro-5-thiobenzoate
?
-
-
-
-
?
O3-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O3-acetyl-L-serine + 5-thio-2-nitrobenzoate
? + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
in the absence of sulfide O3-acetyl-L-serine reacts with the cofactor pyridoxal 5'-phosphate to alpha-aminoacrylate intermediate
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
970% of the activity with cyanide
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
additional information
?
-
the enzyme also catalyzes the reaction of EC 2.5.1.65, O-phosphoserine hydrolase
-
-
?
additional information
?
-
-
isoenzyme 1 and 2 have different substrate specificities towards various beta-substituted L-Cys
-
-
?
additional information
?
-
-
enzyme is induced in leaves exposed to salt stress. The results suggest that the plant enzyme is responding to the salt stress by inducing cysteine biosynthesis as a protection against high ion concentrations
-
-
?
additional information
?
-
-
model of a dynamic cysteine synthesis system with regulatory function
-
-
?
additional information
?
-
-
preferred state of sulfide is hydrogen sulfide
-
-
?
additional information
?
-
the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity
-
-
?
additional information
?
-
-
the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity
-
-
?
additional information
?
-
-
cysteine synthase CysB is the only isoform of physiological importance in Aspergillus nidulans. Starvation-induced cysteine synthase activity is under control of cross-pathway regulation
-
-
?
additional information
?
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
-
-
?
additional information
?
-
-
the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
-
-
?
additional information
?
-
-
beta-substituted alanines, low activity
-
-
?
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
-
-
?
additional information
?
-
no substrate: L-serine, L-homoserine, O-acetyl-L-homoserine, L-alanine, L-homocysteine
-
-
?
additional information
?
-
-
no substrate: L-serine, O-propionyl-L-serine, L-alanine, glycine
-
-
?
additional information
?
-
-
stopped-flow fluorescence spectroscopy is used to characterize the interaction of serine acetyltransferase with OASS and in the presence of the physiological regulators cysteine and bisulfide. Cysteine synthase assembly occurs via a two-step mechanism involving rapid formation of an encounter complex between the two enzymes, followed by a slow conformational change. The conformational change likely results from the closure of the active site of OASS upon binding of the serine acetyltransferase C-terminal peptide. Bisulfide stabilizes the cysteine synthase complex mainly by decreasing the back rate of the isomerization step. Cysteine, the product of the OASS reaction and a SAT inhibitor, slightly affects the kinetics of cysteine synthase formation leading to destabilization of the complex
-
-
?
additional information
?
-
-
the binding free energy of 400 pentapeptides, MNXXI, interacting with the HiOASS-A active site using a combined docking-scoring procedure based on GOLD and HINTare examined. The free energy prediction is verified by the experimental determination of the binding affinity of 14 of these pentapeptides, selected for spanning a large range of predicted binding affinity and presenting charged, polar, or apolar residues at mutation sites
-
-
?
additional information
?
-
the binding free energy of 400 pentapeptides, MNXXI, interacting with the HiOASS-A active site using a combined docking-scoring procedure based on GOLD and HINTare examined. The free energy prediction is verified by the experimental determination of the binding affinity of 14 of these pentapeptides, selected for spanning a large range of predicted binding affinity and presenting charged, polar, or apolar residues at mutation sites
-
-
?
additional information
?
-
no substrates: serine, phosphoserine, O-succinylhomoserine, thiosulfate
-
-
?
additional information
?
-
-
no substrates: serine, phosphoserine, O-succinylhomoserine, thiosulfate
-
-
?
additional information
?
-
no synthesis of mimosine. The enzyme is specific for cysteine synthesis. The recombinant enzyme is active with or without the leader peptide
-
-
?
additional information
?
-
-
no synthesis of mimosine. The enzyme is specific for cysteine synthesis. The recombinant enzyme is active with or without the leader peptide
-
-
?
additional information
?
-
-
enzyme additionally catalyzes synthesis of mimosine, reaction of EC 2.5.1.52. The apparent kcat for Cys production is over sixfold higher than mimosine synthesis and the apparent Km is 3.7 times lower
-
-
-
additional information
?
-
enzyme additionally catalyzes synthesis of mimosine, reaction of EC 2.5.1.52. The apparent kcat for Cys production is over sixfold higher than mimosine synthesis and the apparent Km is 3.7 times lower
-
-
-
additional information
?
-
-
enzyme is unable to synthesize mimosine, reaction of EC 2.5.1.52
-
-
-
additional information
?
-
enzyme is unable to synthesize mimosine, reaction of EC 2.5.1.52
-
-
-
additional information
?
-
enzyme is specific for synthesis of cysteine, no synthesis of mimosine
-
-
-
additional information
?
-
-
enzyme is specific for synthesis of cysteine, no synthesis of mimosine
-
-
-
additional information
?
-
-
the enzyme is induced by Al3+. Cysteine synthase may be a key player during Al response/adaptation in rice
-
-
?
additional information
?
-
protein predominately catalyzes the synthesis but not the degradation of cysteine. The L-cysteine desulfhydrase reaction may be a side reaction
-
-
-
additional information
?
-
enzyme additionally catalyzes the formation of O-ureido-L-serine from O-acetyl-L-serine and hydroxyurea, reaction of EC 2.6.99.3. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
-
-
?
additional information
?
-
-
enzyme additionally catalyzes the formation of O-ureido-L-serine from O-acetyl-L-serine and hydroxyurea, reaction of EC 2.6.99.3. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
-
-
?
additional information
?
-
enzyme additionally catalyzes the formation of O-ureido-L-serine from O-acetyl-L-serine and hydroxyurea, reaction of EC 2.6.99.3. The kcat/Km value of DcsD for L-cysteine synthesis is 80fold higher than that for O-ureido-L-serine synthesis
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cysteine + CN-
cyanoalanine + H2S
Xanthium pennsylvanicum
-
involved in cyanide metabolism during seed germination
-
-
?
L-Cys + acetate
?
-
involved in mobilization of sulfide from cysteine for Fe-S cluster formation, significance in vivo unclear
-
-
?
L-cysteine + dithiothreitol
S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
the side reaction of the enzyme seems to contribute massively to the total H2S release of higher plants at least at higher pH values
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
enzyme that catalyzes the final step in cysteine biosynthesis. Cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
-
Entamoeba histolytica, the causative agent of human amoebiasis, is essentially anaerobic, requiring a small amount of oxygen for growth. It cannot tolerate the higher concentration of oxygen present in human tissues or blood. However, during tissue invasion it is exposed to a higher level of oxygen, leading to oxygen stress. Cysteine, which is a vital thiol in Entamoeba histolytica, plays an essential role in its oxygen-defence mechanisms. The major route of cysteine biosynthesis in this parasite is the condensation of O-acetylserine with sulfide by the de novo cysteine-biosynthetic pathway, which involves cysteine synthase (EhCS) as a key enzyme
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
OASTL activity regulates not only Cys de novo synthesis but also its homeostasis
-
-
?
O-acetyl-L-Ser + isoxazolin-5-one
?
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
?
O-acetyl-L-Ser + isoxazolin-5-one
?
-
synthesis of precursor of neurotoxin beta-N-oxalyl-L-alpha,beta-diaminopropionic acid
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
the cysteine synthase complex functions as a molecular sensor system that monitors the sulfur status of the cell and controls sulfate assimilation and cysteine synthesis according to the availability of sulfate
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in synthesis of antioxidants such as glutathione during fruit development
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in glutathione formation
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
controlled by feedback inhibition, adaptively significant as sulfide removal mechanism
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
repressed during growth with sulfide or thiosulfide as sulfur source
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
key role in metabolism of S-containing amino acids
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
functions as a Cys synthase rather than as a homocysteine synthase in vivo
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
enzyme transcription repressed by L-cystine, derepressed by limiting sulfide concentrations
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
involved in thiosulfate assimilation
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
final step in Cys synthesis
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
activity varies between sulfur sources, enzyme formation regulated by L-Cys concentration
-
-
?
O-acetyl-L-Ser + sulfide
L-Cys + acetate
-
last step of assimilatory sulfate reduction
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
Escherichia coli W3110 / ATCC 27325
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
in the absence of sulfide O3-acetyl-L-serine reacts with the cofactor pyridoxal 5'-phosphate to alpha-aminoacrylate intermediate
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
O3-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
-
-
-
-
?
additional information
?
-
-
enzyme is induced in leaves exposed to salt stress. The results suggest that the plant enzyme is responding to the salt stress by inducing cysteine biosynthesis as a protection against high ion concentrations
-
-
?
additional information
?
-
-
model of a dynamic cysteine synthesis system with regulatory function
-
-
?
additional information
?
-
the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity
-
-
?
additional information
?
-
-
the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity
-
-
?
additional information
?
-
-
cysteine synthase CysB is the only isoform of physiological importance in Aspergillus nidulans. Starvation-induced cysteine synthase activity is under control of cross-pathway regulation
-
-
?
additional information
?
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
-
the enzyme is involved in tellurite resistance. OASS is not essential for cysteine biosynthesis
-
-
?
additional information
?
-
the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
-
-
?
additional information
?
-
-
the enzyme shows H2S synthesizing activity, cysteine synthase activity and also L-3-cyanoalanine synthase activity, EC 4.4.1.9
-
-
?
additional information
?
-
-
stopped-flow fluorescence spectroscopy is used to characterize the interaction of serine acetyltransferase with OASS and in the presence of the physiological regulators cysteine and bisulfide. Cysteine synthase assembly occurs via a two-step mechanism involving rapid formation of an encounter complex between the two enzymes, followed by a slow conformational change. The conformational change likely results from the closure of the active site of OASS upon binding of the serine acetyltransferase C-terminal peptide. Bisulfide stabilizes the cysteine synthase complex mainly by decreasing the back rate of the isomerization step. Cysteine, the product of the OASS reaction and a SAT inhibitor, slightly affects the kinetics of cysteine synthase formation leading to destabilization of the complex
-
-
?
additional information
?
-
-
the enzyme is induced by Al3+. Cysteine synthase may be a key player during Al response/adaptation in rice
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
-
enzyme contains pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate containing catalytic sites are not equivalent
pyridoxal 5'-phosphate
-
2.1 mol per mol of dimeric enzyme
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate-binding site covalently bound, buried deeply within protein
pyridoxal 5'-phosphate
-
stoichiometry, binds to Lys, protects against inactivation by heat, urea, and trypsin, four binding sites per mol apoenzyme, association constant
pyridoxal 5'-phosphate
-
enzyme contains 1.2 pyridoxal phosphate per subunit
pyridoxal 5'-phosphate
-
1 per subunit of free enzyme, 4 per of cysteine synthase complex
pyridoxal 5'-phosphate
-
sequence alignment and site-directed mutation of the enzyme reveal that the cofactor PLP is covalently bound in Schiff base linkage with K30, as well as the two residues H150 and H168 are the crucial residues for PLP binding and stabilization
pyridoxal 5'-phosphate
-
the 31P chemical shift of the internal and external Schiff bases of pyridoxal 5'-phosphate in OASS-B are further downfield compared to OASS-A, suggesting a tighter binding of the cofactor in the B-isozyme. The chemical shift of the internal Schiff base (ISB) of OASS-B is 6.2 ppm, the highest value reported for the ISB of a PLP-dependent enzyme. Considering the similarity in the binding sites of the pyridoxal 5'-phosphate cofactor for both isozymes, torsional strain of the C5-C5' bond (O4'-C5'-C5-C4) of the Schiff base is proposed to contribute to the further downfield shift
pyridoxal 5'-phosphate
-
enzyme sites K30, H150, and H168 are crucial for cofactor binding and stabilization
pyridoxal 5'-phosphate
gives the crystals a yellow color, covalently linked to Lys58, interaction with Gly236, Ser280, Pro307, cofactor orientation at the active site and absorbance maximum change upon binding of cysteine or methionine
pyridoxal 5'-phosphate
-
R186 interacts with the cofactor
pyridoxal 5'-phosphate
-
the 5'-phosphate is tightly bound to the enzyme via a hydrogen bond to His152, one to the residues responsible for positioning of the cofactor
pyridoxal 5'-phosphate
-
tighter binding than in OASS-A, treatment with 1 mM hydroxylamine in 500 mM phosphate, pH 7.6, with 0.2 mM dithiothreitol, followed by dialysis against 100 mM phosphate, pH 7.0, with 0.2 mM dithiothreitol gerates apo-enzyme without the cofactor
pyridoxal 5'-phosphate
-
residue K51 forms a Schiff base with pyridoxal 5'-phosphate, with conserved residues N82 and S274 forming hydrogen bonds to the cofactor. Further residues predicted to orient and hold the pyridoxal 5'-phosphate in position are G186, T182, G183 and T185
pyridoxal 5'-phosphate
-
cofactor pyridoxal 5'-phosphate is linked covalently to Lys58, which is conserved in all OASS structures and is positioned in between these two domains, and highly conserved residues, such as Gly236, Ser280 and Pro307, interact with the aromatic ring of pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
dependent on, binding site structure analysis in a cleft between the N- and C-terminal domains, the phosphate group of PLP interacts with the highly conserved Gly/Thr-rich loop (G181TGGT185) and a water molecule, overview
pyridoxal 5'-phosphate
A0A1J9VES8
cofactor is highly flexible due to the active site being wide open
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
-
(2E)-3-chloropent-2-enedioic acid
-
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)
-
-
1,3-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-phenylbutanedioic 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-[[(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-[[(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
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 CysK2âcystine binding structure, overview. Cystine occupies the substrate/product binding site of the enzyme
D-cycloserine
-
82% loss of activity at 5 mM
DYVI
-
a peptide based on the C-terminus of the partner serine acetyltransferase with which the enzyme forms a complex, competitive inhibition
exophillic acid
from Exophiala sp.FKI-7082 , specific for isozyme CS1
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
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
N-(furan-2-ylcarbonyl)leucine
-
N-(furan-2-ylcarbonyl)phenylalanine
-
N-(thiophen-2-ylsulfonyl)valine
-
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
-
-
NH2OH
-
97% loss of activity at 10 mM
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
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
-
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
[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
-
Aminooxyacetate
-
57% and 64% inhibition at 1 mM, isoenzymes 1 and 2, respectively
cadmium chloride
-
plants grown in the presence of 0.0178 mM cadmium chloride show 141% increase in activity in leaves, and 189% increase in activity in root, respectively
cadmium chloride
-
plants grown in the presence of 0.0178 mM cadmium chloride show 150% increase in activity in leaves; plants grown in the presence of 0.0178 mM cadmium chloride show 260% increase in activity in leaves, and 222% increase in activity in root, respectively
copper sulfate
-
plants grown in the presence of 0.78 mM copper sulfate show 102% increase in activity in leaves, and 98% increase in activity in root, respectively
copper sulfate
-
plants grown in the presence of 0.78 mM copper sulfate show 20% increase in activity in leaves, and 110% increase in activity in root, respectively; plants grown in the presence of 0.78 mM copper sulfate show 56% increase in activity in leaves
hydroxylamine
-
35% and 48% inhibition at 5 mM, isoenzymes 1 and 2, respectively
hydroxylamine
-
complete inhibition at 10 mM, isoenzymes 1 and 2, 90% inhibition at 10 mM, isoenzyme 3
L-cysteine
-
not inhibitory up to 3.7 mM
lead nitrate
-
plants grown in the presence of 2.4 mM lead nitrate plus 5 mM EDTA show 197% increase in activity in leaves, and 201% increase in activity in root, respectively
lead nitrate
-
plants grown in the presence of 2.4 mM lead nitrate plus 5 mM EDTA show 176% increase in activity in leaves; plants grown in the presence of 2.4 mM lead nitrate plus 5 mM EDTA show 302% increase in activity in leaves, and 300% increase in activity in root, respectively
methionine
-
46% and 37% inhibition at 1 mM, isoenzymes 1 and 2, respectively
MNYDI
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
interaction of the inhibitory pentapeptide MNYDI with CysK OASS isozyme from Salmonella typhimurium, the MNYDI peptide interacts with the HiCysK active site mainly through H-bonds involving its C-terminal carboxylate and hydrophobic interactions involving the side chains of Ile5 and Tyr3, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview
MNYDI
interaction of the inhibitory pentapeptide MNYDI with CysK OASS isozyme from Salmonella typhimurium, the MNYDI peptide interacts with the HiCysK active site mainly through H-bonds involving its C-terminal carboxylate and hydrophobic interactions involving the side chains of Ile5 and Tyr3, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview; interaction of the inhibitory pentapeptide MNYDI with CysM OASS isozyme from Salmonella typhimurium, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview. In isozyme CysM multiple H-bond interactions are made by Asn2 side chain with S205 side chain and I206 and I209 backbone carbonyl groups
p-chloromercuribenzoate
-
14% and 4% inhibition at 1 mM, isoenzymes 1 and 2, respectively
S-sulfocysteine
-
26% loss of activity at 5 mM
Semicarbazide
-
60% loss of activity at 1 mM
sodium arsenite
-
plants grown in the presence of 0.0267 mM sodium arsenite show 109% increase in activity in leaves, and 238% increase in activity in root, respectively
sodium arsenite
-
plants grown in the presence of 0.0267 mM sodium arsenite show 108% increase in activity in leaves, and 250% increase in activity in root, respectively; plants grown in the presence of 0.0267 mM sodium arsenite show 120% increase in activity in leaves
additional information
direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis, several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for SAT binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation
-
additional information
-
direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis, several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for SAT binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation
-
additional information
identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors; identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors, no inhibition of isozyme CS3 by exophillic acid from Exophiala sp.FKI-7082, which is specific for isozyme CS1
-
additional information
identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors; identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors, no inhibition of isozyme CS3 by exophillic acid from Exophiala sp.FKI-7082, which is specific for isozyme CS1
-
additional information
-
identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors; identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors, no inhibition of isozyme CS3 by exophillic acid from Exophiala sp.FKI-7082, which is specific for isozyme CS1
-
additional information
-
enzyme inhibitor development, in silico molecular docking simulations, using the three-dimensional crystal structure of O-acetyl-L-serine sulfhydrylase enzyme complexed with cysteine and pyridoxal 5'-phosphate ligands, PDB ID 3BM5, on nine pyrazolo[3,4-d]pyrimidine molecules without linkers and nine pyrazolo[3,4-d]pyrimidine molecules with a trimethylene linker along with the reference drug metronidazole, binding structures, ligand docking and interaction analysis, detiled overview
-
additional information
CysK is competitively inhibited within the cysteine synthase complex
-
additional information
-
partial inhibition of enzyme upon complex formation with serine acetyltransferase
-
additional information
activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction
-
additional information
-
activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction
-
additional information
presence of 4% NaCl is not inhibitory
-
additional information
rational structure-guided design of nanomolar thiazolidine inhibitors of Mycobacterium tuberculosis CysK1 O-acetyl serine sulfhydrylase, discovered using the crystal structure of a CysK1-peptide inhibitor complex as template, pharmacophore modeling and in vitro screening, overview. Chemical synthesis leads to improved thiazolidine inhibitors with an IC50 value of 19 nM for the best compound, a 150fold higher potency than the natural peptide inhibitor with IC50 of 0.0029 mM
-
additional information
-
rational structure-guided design of nanomolar thiazolidine inhibitors of Mycobacterium tuberculosis CysK1 O-acetyl serine sulfhydrylase, discovered using the crystal structure of a CysK1-peptide inhibitor complex as template, pharmacophore modeling and in vitro screening, overview. Chemical synthesis leads to improved thiazolidine inhibitors with an IC50 value of 19 nM for the best compound, a 150fold higher potency than the natural peptide inhibitor with IC50 of 0.0029 mM
-
additional information
activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction
-
additional information
anions, like sulfate, significantly reduce the affinity of peptides for CysK
-
additional information
anions, like sulfate, significantly reduce the affinity of peptides for CysK
-
additional information
-
anions, like sulfate, significantly reduce the affinity of peptides for CysK
-
additional information
computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview; computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview
-
additional information
computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview; computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview
-
additional information
-
computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview; computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview
-
additional information
identification of potential inhibitors of the two isozymes A and B via a ligand- and structure-based in silico screening of a subset of the ZINC library using FLAP. The binding affinities of the most promising candidates are measured in vitro on purified O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B by a direct method that exploits the change in the cofactor fluorescence, ligand binding analysis, overview; identification of potential inhibitors of the two isozymes A and B via a ligand- and structure-based in silico screening of a subset of the ZINC library using FLAP. The binding affinities of the most promising candidates are measured in vitro on purified O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B by a direct method that exploits the change in the cofactor fluorescence, ligand binding analysis, overview
-
additional information
identification of potential inhibitors of the two isozymes A and B via a ligand- and structure-based in silico screening of a subset of the ZINC library using FLAP. The binding affinities of the most promising candidates are measured in vitro on purified O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B by a direct method that exploits the change in the cofactor fluorescence, ligand binding analysis, overview; identification of potential inhibitors of the two isozymes A and B via a ligand- and structure-based in silico screening of a subset of the ZINC library using FLAP. The binding affinities of the most promising candidates are measured in vitro on purified O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B by a direct method that exploits the change in the cofactor fluorescence, ligand binding analysis, overview
-
additional information
-
identification of potential inhibitors of the two isozymes A and B via a ligand- and structure-based in silico screening of a subset of the ZINC library using FLAP. The binding affinities of the most promising candidates are measured in vitro on purified O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B by a direct method that exploits the change in the cofactor fluorescence, ligand binding analysis, overview; identification of potential inhibitors of the two isozymes A and B via a ligand- and structure-based in silico screening of a subset of the ZINC library using FLAP. The binding affinities of the most promising candidates are measured in vitro on purified O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B by a direct method that exploits the change in the cofactor fluorescence, ligand binding analysis, overview
-
additional information
molecular dynamic simulation and inhibitor prediction of cysteine synthase
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
serine acetyltransferase
CysE, 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. 20fold increase in catalytic efficiency upon binding of CysE to CysK as a result of both decreased KM for acetyl-CoA and increased kcat. Free CysE enzyme is less active and more susceptible to aggregation, inactivation and proteolysis
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
additional information
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.018
5-thio-2-nitrobenzoate
-
mutant W50Y, pH 7.0, 20°C
0.049
5-thio-2-nitrobenzoate
-
wild-type, pH 7.0, 20°C
0.061
5-thio-2-nitrobenzoate
-
mutant W161Y, pH 7.0, 20°C
0.07
5-thio-2-nitrobenzoate
-
mutant H52A, pH 6.5
0.07
5-thio-2-nitrobenzoate
-
K120Q mutant with 9fold decrease compared to wild type, 100 mM MES, pH 6.5, 0.5 mM O3-acetyl-L-serine, 25°C
0.6
5-thio-2-nitrobenzoate
-
wild-type, pH 7.0
0.6
5-thio-2-nitrobenzoate
-
wild type, 100 mM HEPES, pH 7.0, 0.5 mM O3-acetyl-L-serine, 25°C
2.5
5-thio-2-nitrobenzoate
-
mutant H52A, pH 6.5
2.5
5-thio-2-nitrobenzoate
-
H152A mutant with 4.1fold increase compared to wild type, 100 mM MES, pH 6.5, 0.5 mM O3-acetyl-L-serine, 25°C
0.0384
c