BRENDA home
History
Information on EC 2.3.1.30 - serine O-acetyltransferase
for references in articles please use BRENDA:EC2.3.1.30Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.1.30 serine O-acetyltransferaseSpecify your search results
Word Map
- 2.3.1.30
- o-acetylserine
- sulfur
- l-cysteine
-
sulfhydrylase
- o-acetyl-l-serine
- foot-and-mouth
- desulfhydrase
- oas-tls
-
assimilatory
-
o-acetylserinethiollyase
-
slc26a1
-
bienzyme
- phytochelatins
- thlaspi
-
nasi-1
- agriculture
- drug development
- medicine
- molecular biology
The enzyme appears in viruses and cellular organisms
Synonyms
acetyltransferase, serine, AtOASS, AtSAT, AtSAT1, AtSerat 2;1, BvSAT, CysE, cytosolic serine acetyltransferase, DcsE, EhSAT1, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyltransferase, serine
-
-
-
-
CysE
DcsE
EhSAT1
L-serine acetyltransferase
-
-
-
-
L-serine O-acetyltransferase
SAT
SAT1
SAT3
SATase
SERAT
Serat1,1
Serat2,1
Serat2,2
Serat3,1
Serat3,2
serine acetyltransferase
serine acetyltransferase 1
serine O-acetyltransferase
serine transacetylase
-
-
-
-
Spn cysE
SP_0589
additional information
SATase
-
-
-
-
serine acetyltransferase
-
-
-
-
additional information
-
serine acetyltransferase and O-acetylserine (thiol) lyase form the cysteine synthase complex, consisting of 2 of each enzymes as a tetramer
additional information
serine acetyltransferase and O-acetylserine (thiol) lyase form the cysteine synthase complex
additional information
serine acetyltransferase and O-acetylserine (thiol) lyase form the cysteine synthase complex
additional information
serine acetyltransferase and O-acetylserine (thiol) lyase form the cysteine synthase complex
additional information
-
serine acetyltransferase and O-acetylserine (thiol) lyase form the cysteine synthase complex
additional information
-
physical association of serine acetyltransferase with about 5% of the total cellular O-acetylserine sulfhydrylase to form a multienzyme complex given the trivial name cysteine synthethase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
ping pong bi bi mechanism
-
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
steady-state random-order mechanism
-
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
a C-terminal hexapeptide-repeat domain is common for Arabidopsis thaliana isoforms and several other enzyme DNA sequences, it has a catalytic bifunctionality as serine acetyltransferase and in interaction with O-acetylserine (thiol) lyase and is involved in cysteine biosynthesis regulation, computational modeling
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
binding motif for O-acetylserine (thiol) lyase is located within 10 amino acid residues at the C-terminal end
-
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
ordered kinetic mechanism with acetyl CoA bound prior to L-serine and O-acetyl-L-serine released prior to CoA. The rate-limiting step along the reaction pathway is the nucleophilic attack of the serine hydroxyl on the thioester of acetyl CoA. Product release contributes to rate-limitation at saturating concentrations of reactants. The reaction is catalyzed by an active site general base with a pK of 7, which accepts a proton from the serine hydroxyl as a tetrahedral intermediate is formed between the reactants, and donates it to the thiol of CoA as the intermediate collapses to give products
-
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
there is no conformational difference in the enzyme between the apo and the substrate-bound states, indicating lock and key binding and the absence of an induced fit mechanism
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
there is no conformational difference in the enzyme between the apo and the substrate-bound states, indicating lock and key binding and the absence of an induced fit mechanism
-
-
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
ping pong bi bi mechanism
-
-
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:L-serine O-acetyltransferase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9023-16-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
L-serine + acetyl-CoA
O-acetyl serine + CoA
-
subsequently, cysteine synthase forms L-cysteine from O-acetyl serine
-
?
L-serine + acetyl-CoA
O-acetylserine + CoA
no major contribution to total cysteine biosynthesis
-
-
?
acetyl-CoA + L-Ser
CoA + O-acetyl-L-Ser
key enzyme in L-cysteine biosynthesis
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
key role in the sulfur assimilatory pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
rate-limiting step of cysteine biosynthesis
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
regulatory role in cysteine biosynthesis
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
regulatory role in cysteine biosynthesis
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
regulatory role in cysteine biosynthesis
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
key role in the sulfur assimilatory pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
the complex array of compartment-specific SATase isoforms with distinct enzymatic properties and expression patterns ensures the provision of Cys in response to revelopmental and environmental changes
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
cysteine biosynthesis in plants is partly regulated by the physical association of O-acetylserine sulfhydrylase and serine acetyltransferase. Thermodynamics of the interaction is analyzed
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
each serine acetyltransferase isoform seems to have its specific role for cysteine biosynthesis
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
simultaneous expression of serine acetyltransferase and cysteine synthase results in enhanced sulfate uptake and increased biomass in Ipomaea aquatica
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
enzyme is involved in cysteine biosynthesis. Increase in cysteine production confers enhanced resistance against osmotic stress in the osmosensitive yeast strain. Cysteine biosynthesis is a limiting factor in osmotic stress tolerance in yeast
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
dependent on L-serine and acetyl-CoA
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
regulatory role in cysteine biosynthesis
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
key role in the sulfur assimilatory pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
enzyme activity is sensitive to feedback inhibition by L-cysteine. Enzyme synthesis is repressed by L-methionine. Corynebacterium glutamicum synthesizes L-cysteine from L-serine via O-acetyl-L-serine through the pathway involving L-serineO-acetyltransferase and O-acetyl-L-serine sulfhydrylase. The enzyme is regulated at both the transcriptional and posttranslational level
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first enzyme in L-cysteine synthesis pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first enzyme in L-cysteine synthesis pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
first step of L-cysteine synthesis
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
Escherichia coli B / ATCC 11303
-
first enzyme in L-cysteine synthesis pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
L-serine acetylation is an equilibrium ordered mechanism
-
-
r
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
enzyme catalyzes the committed step in the de novo synthesis of L-cysteine. Serine acetyltransferase is regulated by feedback inhibition by the end product L-cysteine, which acts by binding to the serine site in the active site and inducing a conformational change that prevents reactant binding
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
serine acetyltransferase is a key enzyme in the sulfur assimilation pathway and forms a bienzyme complex with O-acetylserine sulfhydrylase, the last enzyme in the cysteine biosynthetic pathway. Serine acetyltransferase 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
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
specific for L-serine
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
enzyme in metabolic pathway of sulfur from sulfide to methionine
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
specific for L-serine
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first enzyme in L-cysteine synthesis pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
r
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
r
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
equilibrium constant in direction of L-serine acetylation
-
r
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first enzyme in L-cysteine synthesis pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first enzyme in L-cysteine synthesis pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
r
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
equilibrium constant in direction of L-serine acetylation
-
r
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
regulatory role in cysteine biosynthesis
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
key role in the sulfur assimilatory pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first enzyme in L-cysteine synthesis pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
key role in the sulfur assimilatory pathway
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-threonine
CoA + O-acetyl-L-threonine
-
0.5% of the activity with L-serine
-
-
?
acetyl-CoA + L-threonine
CoA + O-acetyl-L-threonine
Escherichia coli B / ATCC 11303
-
0.5% of the activity with L-serine
-
-
?
additional information
?
-
-
cysteine synthase is a bienzyme complex build of serine acetyltransferase and O-acetylserine (thiol) lyase, no channeling of substrate within the complex
-
-
?
additional information
?
-
O13389
enzyme performs L-serine acetylation, but has evolutionary evolved from serine O-acetyltransferase, high DNA sequence homology with the latter
-
-
?
additional information
?
-
coenzyme A binds to the C-terminal region, making mostly hydrophobic contacts from the center of the active site extending up to the surface of the protein. There is no conformational difference in the enzyme between the apo and the substrate-bound states, indicating lock and key binding and the absence of an induced fit mechanism
-
-
?
additional information
?
-
-
coenzyme A binds to the C-terminal region, making mostly hydrophobic contacts from the center of the active site extending up to the surface of the protein. There is no conformational difference in the enzyme between the apo and the substrate-bound states, indicating lock and key binding and the absence of an induced fit mechanism
-
-
?
additional information
?
-
coenzyme A binds to the C-terminal region, making mostly hydrophobic contacts from the center of the active site extending up to the surface of the protein. There is no conformational difference in the enzyme between the apo and the substrate-bound states, indicating lock and key binding and the absence of an induced fit mechanism
-
-
?
additional information
?
-
-
multienzyme complex is formed between serine acetyltransferase and cysteine synthase possibly leading to metabolic channeling
-
-
?
additional information
?
-
-
no activity: O-acetylserine, O-acetylhomoserine
-
-
?
additional information
?
-
-
Saccharomyces cerevisiae has detectable activity of L-serine O-acetyltransferase, but synthesizes L-cysteine exclusively via cystathionine by cystathionine beta-synthase and cystathionine gamma-lyase. The enzyme cannot support L-cysteine biosynthesis in vivo either because of very low activity or localization
-
-
?
additional information
?
-
-
serine acetyltransferase activity of CysE protein is detected by both DTNB [5,5'-dithiobis-(2-nitrobenzoic acid)] colorimetric assay and HPLC assay. Post-docking interactions between active site residues of protein (MRSA CysE) with ligand (L-Ser)
-
-
-
additional information
?
-
Staphylococcus aureus ATCC 33591
-
serine acetyltransferase activity of CysE protein is detected by both DTNB [5,5'-dithiobis-(2-nitrobenzoic acid)] colorimetric assay and HPLC assay. Post-docking interactions between active site residues of protein (MRSA CysE) with ligand (L-Ser)
-
-
-
additional information
?
-
the enzyme prefers L-serine as a substrate, but is also active with L-homoserine, EC 2.3.1.31, substrate specificity, overview
-
-
?
additional information
?
-
the enzyme prefers L-serine as a substrate, but is also active with L-homoserine, EC 2.3.1.31, substrate specificity, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
acetyl-CoA + L-Ser
CoA + O-acetyl-L-Ser
key enzyme in L-cysteine biosynthesis
-
-
?
L-serine + acetyl-CoA
O-acetyl serine + CoA
-
subsequently, cysteine synthase forms L-cysteine from O-acetyl serine
-
?
L-serine + acetyl-CoA
O-acetylserine + CoA
no major contribution to total cysteine biosynthesis
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
key role in the sulfur assimilatory pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
rate-limiting step of cysteine biosynthesis
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
regulatory role in cysteine biosynthesis
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
regulatory role in cysteine biosynthesis
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
regulatory role in cysteine biosynthesis
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
key role in the sulfur assimilatory pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
the complex array of compartment-specific SATase isoforms with distinct enzymatic properties and expression patterns ensures the provision of Cys in response to revelopmental and environmental changes
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
cysteine biosynthesis in plants is partly regulated by the physical association of O-acetylserine sulfhydrylase and serine acetyltransferase. Thermodynamics of the interaction is analyzed
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
each serine acetyltransferase isoform seems to have its specific role for cysteine biosynthesis
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
simultaneous expression of serine acetyltransferase and cysteine synthase results in enhanced sulfate uptake and increased biomass in Ipomaea aquatica
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
enzyme is involved in cysteine biosynthesis. Increase in cysteine production confers enhanced resistance against osmotic stress in the osmosensitive yeast strain. Cysteine biosynthesis is a limiting factor in osmotic stress tolerance in yeast
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
regulatory role in cysteine biosynthesis
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
key role in the sulfur assimilatory pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
enzyme activity is sensitive to feedback inhibition by L-cysteine. Enzyme synthesis is repressed by L-methionine. Corynebacterium glutamicum synthesizes L-cysteine from L-serine via O-acetyl-L-serine through the pathway involving L-serineO-acetyltransferase and O-acetyl-L-serine sulfhydrylase. The enzyme is regulated at both the transcriptional and posttranslational level
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first enzyme in L-cysteine synthesis pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first enzyme in L-cysteine synthesis pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
first step of L-cysteine synthesis
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
Escherichia coli B / ATCC 11303
-
first enzyme in L-cysteine synthesis pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
enzyme catalyzes the committed step in the de novo synthesis of L-cysteine. Serine acetyltransferase is regulated by feedback inhibition by the end product L-cysteine, which acts by binding to the serine site in the active site and inducing a conformational change that prevents reactant binding
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
enzyme in metabolic pathway of sulfur from sulfide to methionine
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first enzyme in L-cysteine synthesis pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
r
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first enzyme in L-cysteine synthesis pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first enzyme in L-cysteine synthesis pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
r
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
regulatory role in cysteine biosynthesis
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
key role in the sulfur assimilatory pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first enzyme in L-cysteine synthesis pathway
-
ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
key role in the sulfur assimilatory pathway
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
-
-
?
additional information
?
-
-
cysteine synthase is a bienzyme complex build of serine acetyltransferase and O-acetylserine (thiol) lyase, no channeling of substrate within the complex
-
-
?
additional information
?
-
O13389
enzyme performs L-serine acetylation, but has evolutionary evolved from serine O-acetyltransferase, high DNA sequence homology with the latter
-
-
?
additional information
?
-
-
multienzyme complex is formed between serine acetyltransferase and cysteine synthase possibly leading to metabolic channeling
-
-
?
additional information
?
-
-
Saccharomyces cerevisiae has detectable activity of L-serine O-acetyltransferase, but synthesizes L-cysteine exclusively via cystathionine by cystathionine beta-synthase and cystathionine gamma-lyase. The enzyme cannot support L-cysteine biosynthesis in vivo either because of very low activity or localization
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
additional information
-
salt concentrations less than 0.02 M or greater than 0.2 M appreciably decrease reaction rate
additional information
Mg2+ has no effect on the enzyme activity
additional information
-
Mg2+ has no effect on the enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1aR,1bS,4aR,7bS,8R,9R,9aS)-4a,7b,9-trihydroxy-3-(hydroxymethyl)-1,1,6,8-tetramethyl-5-oxo-1,1a,1b,4,4a,5,7a,7b,8,9-decahydro-9aH-cyclopropa[3,4]benzo[1,2-e]azulen-9a-yl acetate
-
-
11beta,12alpha,17-trihydroxy-5beta,9beta,10alpha-12,16-epoxyabieta-8(14),13(15)-dien-16-one
-
-
2-amino-9-(naphthalen-2-yl)-9H-purin-6-ol
0.05 microg/microl showing 38% inhibition in the presence of 0.10 mM acetyl-CoA, binding to active site
3-oxo-2-phenyl-3,5-dihydro-2H-pyrazolo[3,4-d]thieno[2,3-b]pyridine-7-carboxylate
most potent inhibitor, 0.05 microg/microl showing 50% inhibition in the presence of 0.10 mM acetyl-CoA, binding to active site, increasing Km, decreasing Vmax
3-oxo-2-phenyl-3,5-dihydro-2H-pyrazolo[3,4-d]thieno[2,3-b]pyridine-7-carboxylic acid
-
4,10-dihydroxy-1,7-phenanthroline-3,9-dicarboxylate
0.05 microg/microl showing 24% inhibition in the presence of 0.10 mM acetyl-CoA, binding to active site
8,11beta,14beta-trihydroxy-5beta,8alpha,9beta,10alpha,12beta-12,16-epoxyabiet-13(15)-en-16-one
-
-
8,14alpha-dihydroxy-5beta,9beta,10alpha,12alpha-12,16-epoxyabiet-13(15)-ene-11,16-dione
-
-
8,14beta,17-trihydroxy-5beta,8alpha,9beta,10alpha-12,16-epoxyabieta-11,13(15)-dien-16-one
-
-
Berberine
the ligand binds at the trimer-trimer interface, 24% inhibition at 0.005 mM with 500 ng enzyme
mangiferin
the ligand is involved in hydrophilic as well as hydrophobic interactions with enzyme Kpn CysE, 22% inhibition at 0.005 mM with 500 ng enzyme
quercetin
uncompetitive inhibitor, molecular dynamics simulations carried out to elucidate the binding mode of quercetin reveal that this small molecule binds at the trimer-trimer interface of hexameric CysE, a site physically distinct from the active site of the enzyme, overview. Binding of quercetin to CysE leads to conformation changes in the active site loops and proximal loops that affect its internal dynamics and consequently its affinity for substrate/co-factor binding, justifying the reduced enzyme activity. Quercetin binding kinetics and analysis provide mechanistic understanding of allosteric modulation. The ligand is involved in hydrophilic as well as hydrophobic interactions with Kpn CysE, 62% inhibition at 0.005 mM with 500 ng enzyme
reduced glutathione
0.5 mM weak inhibition; 0.5 mM, weak inhibition
vasicine
the ligand binds at the trimer-trimer interface, 46% inhibition at 0.005 mM with 500 ng enzyme
cysteine
-
competitive versus acetyl-CoA, mixed non-competitive with respect to serine
cysteine
competitive, binds at the serine substrate site, negatively regulates its own synthesis
glycine
-
mixed non-competitive inhibitor of propionyl transfer to serine with respect to propionyl-CoA
glycine
-
competitive versus L-serine, uncompetitive versus acetyl-CoA
glycine
-
competitive against L-serine, noncompetitive against acetyl-CoA
L-cysteine
-
feed-back inhibition of cytosolic isozyme SAT-c, not of mitochondrial and plastidic isozymes SAT-m and SAT-p
L-cysteine
-
feed-back inhibition of cytosolic isozyme SAT-c, not of mitochondrial and plastidic isozymes SAT-m and SAT-p
L-cysteine
-
feedback inhibition, isoform Serat3,1, noncompetitive versus L-serine, competitive versus acetyl-CoA
L-cysteine
competitive inhibition versus L-serine, noncompetitive inhibition versus acetyl-CoA
L-cysteine
-
recombinant wild-type and mutants, not mutant M280I, inhibitor binding motif
L-cysteine
0.03 mM, 0.5 mM, and 1 mM, strong inhibition, 5-500 microM L-cysteine in the presence of 0.5 mM L-serine inhibits the enzyme remarkably, much less but still significantly in the presence of 3 mM L-serine, 90% inhibition by 0.3 mM L-cysteine with 3 mM L-serine (as found in throphozoite culture), acetyl-CoA concentration influences the inhibitory efficiency as well; 0.5 mM inhibits by 75.3%, no inhibition with 0.03 mM, 1 mM not determined, 20% inhibition by 0.3 mM L-cysteine with 3 mM L-serine (as found in throphozoite culture); 1 mM, weak inhibition, no inhibition by 0.3 mM L-cysteine with 3 mM L-serine (as found in throphozoite culture) or at other L-cysteine concentrations from 10-1000 micoM in the presence of 3 mM L-serine
L-cysteine
feedback inhibition; feedback inhibition; feedback inhibition, isozyme SAT3 is almost insensitive to cysteine inhibition. A combination of comparative modeling, multiple molecular dynamics simulations and free energy calculation studies shows a difference in binding energies of wild-type isozyme SAT3 and of a S208H-SAT3 mutant for cysteine
L-cysteine
-
competitive in response to acetyl-CoA, noncompetitive in presence of L-Ser
L-cysteine
-
dead-end inhibitor, competitive against botn substrates in both reaction directions
L-cysteine
a feedback inhibitor, binding structure from crystal structure analysis of the enzyme-bound complex. A cysteine molecule bound at the active site pocket at the interface of two Kpn CysE subunits. Each Kpn CysE trimer in-houses three cysteine molecules at the equivalent sites related by a 3fold axis, that, in turn, are related to remaining 3 active sites by 2 fold symmetry. Cysteine at the interface of two subunits is stabilized by interactions from one subunit involving Asp92, Pro93 and Ala94 (residues of turn connecting alpha5 and alpha6 helices) and Asp157, His158 (residues of L?betaloop) as well as from Gly183, Gly184, Thr185, Arg192, His193 (residues of substrate binding loop) of the adjacent subunit. About 50% inhibition at 0.005 mM with 500 ng enzyme
L-cysteine
-
under physiological conditions L-cysteine specifically inhibits chloroplast enzyme activity, which is linked to the sulfate assimilation network. This metabolic feedback control does not apply to the enzyme activity located in cytosol
L-cysteine
feedback inhibition; feedback inhibition; feedback inhibition; feedback inhibition, isozyme VvSERAT2-1 is almost insensitive to cysteine inhibition
L-serine
-
product inhibition is noncompetitive with respect to O-acetyl-L-serine and CoA
L-serine
-
product inhibition, competitive against CoA and noncompetitive against O-acetyl-L-serine
N-acetyl-L-cysteine
1 mM weak inhibition; 1 mM, weak inhibition; 1 mM, weak inhibition
O-acetyl-L-serine
-
product inhibition is noncompetitive against acetyl-CoA and uncompetitive against L-serine
O-acetyl-L-serine
-
product inhibition, competitive against acetyl-CoA and noncompetitive against O-acetyl-L-serine
S-methyl-L-cysteine
-
competitive versus O-acetyl-L-serine and competitive versus CoA
S-methyl-L-cysteine
-
competitive against O-acetyl-L-serine, noncompetitive against CoA
additional information
-
isoform Serat3,1 is insensitive to feedback inhibition by L-Cys
-
additional information
-
beta-(pyrazol-1-yl)-L-alanine has no inhibitory effect
-
additional information
-
no inhibition by 0.03 mM L-cystine, 0.5 mM D-cysteine, DL-homocysteine, DL-homoserine, and oxidized glutathione (reduced glutathione not determined); no inhibition with 0.03 and 0.5 mM L-cystine, 0.5 mM D-cysteine, DL-homocysteine, DL-homoserine, and N-acetyl-L-serine; no inhibition with 0.03 mM L-cystine, 0.5 mM D-cysteine, DL-homocysteine, DL-homoserine, N-acetyl-L-serine, and oxidized glutathione
-
additional information
no inhibition by 0.03 mM L-cystine, 0.5 mM D-cysteine, DL-homocysteine, DL-homoserine, and oxidized glutathione (reduced glutathione not determined); no inhibition with 0.03 and 0.5 mM L-cystine, 0.5 mM D-cysteine, DL-homocysteine, DL-homoserine, and N-acetyl-L-serine; no inhibition with 0.03 mM L-cystine, 0.5 mM D-cysteine, DL-homocysteine, DL-homoserine, N-acetyl-L-serine, and oxidized glutathione
-
additional information
no inhibition by 0.03 mM L-cystine, 0.5 mM D-cysteine, DL-homocysteine, DL-homoserine, and oxidized glutathione (reduced glutathione not determined); no inhibition with 0.03 and 0.5 mM L-cystine, 0.5 mM D-cysteine, DL-homocysteine, DL-homoserine, and N-acetyl-L-serine; no inhibition with 0.03 mM L-cystine, 0.5 mM D-cysteine, DL-homocysteine, DL-homoserine, N-acetyl-L-serine, and oxidized glutathione
-
additional information
-
histidine 208 appears to be one of the important residues that distinguish the serine substrate from the cysteine inhibitor
-
additional information
histidine 208 appears to be one of the important residues that distinguish the serine substrate from the cysteine inhibitor
-
additional information
histidine 208 appears to be one of the important residues that distinguish the serine substrate from the cysteine inhibitor
-
additional information
structural information of a ligand-bound receptor complex via molecular dynamics simulation, docking study, overview
-
additional information
-
structural information of a ligand-bound receptor complex via molecular dynamics simulation, docking study, overview
-
additional information
-
no growth inhibition of mouse cell culture with 4,10-dihydroxy-1,7-phenanthroline-3,9-dicarboxylic acid, 2-amino-9-naphthalen-2-yl-9H-purin-6-ol, or 3-oxo-2-phenyl-3,5-dihydro-2H-pyrazolo[3,4-d]thieno[2,3-b]pyridine-7-carboxylic acid in a MTT assay
-
additional information
-
analysis of cytotoxicity of compounds 8,14alpha-dihydroxy-5beta,9beta,10alpha,12alpha-12,16-epoxyabiet-13(15)-ene-11,16-dione and 8,14beta,17-trihydroxy-5beta,8alpha,9beta,10alpha-12,16-epoxyabieta-11,13(15)-dien-16-one, inhibition types of different inhibitors on MRSA CysE, overview; ligand molecular docking study
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Amebiasis
Identification of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites.
Colonic Neoplasms
Evaluation of SAT-1, SAT-2 and GalNAcT-1 mRNA in colon cancer by real-time PCR.
Foot-and-Mouth Disease
Characterisation of a SAT-1 outbreak of foot-and-mouth disease in captive African buffalo (Syncerus caffer): clinical symptoms, genetic characterisation and phylogenetic comparison of outbreak isolates.
Foot-and-Mouth Disease
Comparison of SAT-1 foot-and-mouth disease virus isolates obtained from East Africa between 1971 and 2000 with viruses from the rest of sub-Saharan Africa.
Foot-and-Mouth Disease
Experimental infection of giraffe (Giraffa camelopardalis) with SAT-1 and SAT-2 foot-and-mouth disease virus.
Foot-and-Mouth Disease
First confirmation of foot and mouth disease virus serotype SAT-1 in cattle and small ruminants in Ethiopia in 2007/08.
Foot-and-Mouth Disease
Genetic heterogeneity of SAT-1 type foot-and-mouth disease viruses in southern Africa.
Foot-and-Mouth Disease
Isolation and partial characterization of temperature-sensitive mutants of the SAT-1 strain of foot-and-mouth disease virus.
Foot-and-Mouth Disease
Retrospective genetic analysis of SAT-1 type foot-and-mouth disease outbreaks in southern Africa.
Foot-and-Mouth Disease
Retrospective genetic analysis of SAT-1 type foot-and-mouth disease outbreaks in West Africa (1975-1981).
Foot-and-Mouth Disease
The isoelectrofocusing technique in comparison of some Sudanese type SAT-1 foot-and-mouth disease viruses.
Genetic Diseases, Inborn
Cloning and characterization of SLC26A6, a novel member of the solute carrier 26 gene family.
Hyperoxaluria
Absence of the sulfate transporter SAT-1 has no impact on oxalate handling by mouse intestine and does not cause hyperoxaluria or hyperoxalemia.
Hyperoxaluria
In female rats, ethylene glycol treatment elevates protein expression of hepatic and renal oxalate transporter sat-1 (Slc26a1) without inducing hyperoxaluria.
Hypersensitivity
Novel method to analyze cell kinetics for the rapid diagnosis and determination of the causative agent in allergy.
Infections
Experimental infection of giraffe (Giraffa camelopardalis) with SAT-1 and SAT-2 foot-and-mouth disease virus.
Infections
Immune-driven alterations in mucin sulphation is an important mediator of Trichuris muris helminth expulsion.
Infections
Yersinia pestis acetyltransferase-mediated dual acetylation at the serine and lysine residues enhances the auto-ubiquitination of ubiquitin ligase MARCH8 in human cells.
Intestinal Neoplasms
Evaluation of SAT-1, SAT-2 and GalNAcT-1 mRNA in colon cancer by real-time PCR.
Kidney Calculi
Absence of the sulfate transporter SAT-1 has no impact on oxalate handling by mouse intestine and does not cause hyperoxaluria or hyperoxalemia.
Kidney Failure, Chronic
Molecular aspects of renal tubular handling and regulation of inorganic sulfate.
Kidney Failure, Chronic
Sulfate homeostasis, NaSi-1 cotransporter, and SAT-1 exchanger expression in chronic renal failure in rats.
Mouth Diseases
First confirmation of foot and mouth disease virus serotype SAT-1 in cattle and small ruminants in Ethiopia in 2007/08.
Neoplasms
Inhibitors of Escherichia coli serine acetyltransferase block proliferation of Entamoeba histolytica trophozoites.
Rhinitis, Allergic, Seasonal
Novel method to analyze cell kinetics for the rapid diagnosis and determination of the causative agent in allergy.
serine o-acetyltransferase deficiency
Cysteine biosynthesis in Saccharomyces cerevisiae: mutation that confers cystathionine beta-synthase deficiency.
Starvation
Impact of sulfur starvation on cysteine biosynthesis in T-DNA mutants deficient for compartment-specific serine-acetyltransferase.
Starvation
Regulation of sulfur assimilation in higher plants: a sulfate transporter induced in sulfate-starved roots plays a central role in Arabidopsis thaliana.
Tuberculosis
Identification and characterization of serine acetyltransferase encoded by the Mycobacterium tuberculosis Rv2335 gene.
Tuberculosis, Bovine
Characterisation of a SAT-1 outbreak of foot-and-mouth disease in captive African buffalo (Syncerus caffer): clinical symptoms, genetic characterisation and phylogenetic comparison of outbreak isolates.
Urolithiasis
In female rats, ethylene glycol treatment elevates protein expression of hepatic and renal oxalate transporter sat-1 (Slc26a1) without inducing hyperoxaluria.
Urolithiasis
Lack of evidence for the association of ornithine decarboxylase (+316 G>A), spermidine/spermine acetyl transferase (-1415 T>C) gene polymorphisms with calcium oxalate stone disease.
Urolithiasis
The liver and kidney expression of sulfate anion transporter sat-1 in rats exhibits male-dominant gender differences.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0513
acetyl-CoA
pH 7.5, 37°C, recombinant His-tagged enzyme
0.176
acetyl-CoA
recombinant isozyme A, mutant G354A
0.2
acetyl-CoA
SAT2, 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C
0.25
acetyl-CoA
SAT2, 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C
0.55
acetyl-CoA
50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C
0.0264
L-serine
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0435
L-serine
wild-type isozyme SAT1, pH 8.0, temperature not specified in the publication
0.052
L-serine
wild-type isozyme SAT3, pH 8.0, temperature not specified in the publication
0.0673
L-serine
wild-type isozyme SAT3, pH 8.0, temperature not specified in the publication, in presence of 10 mM L-cysteine
0.0684
L-serine
isozyme SAT1 mutant H208S, pH 8.0, temperature not specified in the publication
0.09
L-serine
SAT2, 50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C
0.1
L-serine
SAT2, 50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C
0.12
L-serine
50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C
0.1275
L-serine
recombinant enzyme, pH 8.0, temperature not specified in the publication
0.1855
L-serine
isozyme SAT3 mutant S208H, pH 8.0, temperature not specified in the publication
0.1923
L-serine
recombinant enzyme, pH 8.0, temperature not specified in the publication, in presence of 5 mM L-cysteine
0.2109
L-serine
isozyme SAT3 mutant S208HS, pH 8.0, temperature not specified in the publication, in presence of 10 mM L-cysteine
0.2178
L-serine
wild-type isozyme SAT1, pH 8.0, temperature not specified in the publication, in presence of 10 mM L-cysteine
0.2321
L-serine
isozyme SAT1 mutant H208S, pH 8.0, temperature not specified in the publication, in presence of 10 mM L-cysteine
0.2783
L-serine
recombinant enzyme, pH 8.0, temperature not specified in the publication, in presence of 10 mM L-cysteine
0.5
L-serine
recombinant His-tagged mutant P55G enzyme, pH 8.0, 30°C
4.9
L-serine
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
25.55
L-serine
recombinant isozyme A, mutant G354A
additional information
additional information
-
Km for L-serine and acetyl-CoA of recombinant L-cysteine-binding motif mutants, overview
-
additional information
additional information
-
cysteine synthase bienzyme complex
-
additional information
additional information
-
Km of mutant enzymes
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
Michaelis-Menten kinetics, overview
-
additional information
additional information
Michaelis-Menten kinetics, overview
-
additional information
additional information
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
Michalis-Menten kinetics
-
additional information
additional information
-
Michalis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14.59
acetyl-CoA
50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C
58.63
acetyl-CoA
50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C
117.9
acetyl-CoA
50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C
200
acetyl-CoA
-
cosubstrate L-serine
0.62
L-serine
recombinant His-tagged mutant P55G enzyme, pH 8.0, 30°C
1.58
L-serine
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
17.31
L-serine
50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C
25.52
L-serine
50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C
43.83
L-serine
50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.32
L-serine
recombinant His-tagged wild-type enzyme, pH 8.0, 30°C
1.23
L-serine
recombinant His-tagged mutant P55G enzyme, pH 8.0, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.042
3-oxo-2-phenyl-3,5-dihydro-2H-pyrazolo[3,4-d]thieno[2,3-b]pyridine-7-carboxylic acid
72 micromol, 0.1 M Tris-HCl, pH 7.5, room temperature
0.0047
L-cysteine
competitive inhibition with L-serine but no inhibition with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 25°C
0.02779
L-cysteine
competitive inhibition with L-serine, 50 mM Tris-HCl, pH 8.0, 25°C
0.0947
L-cysteine
non-competitive inhibition with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 0.25 mM acetyl-CoA, 25°C
0.46
L-cysteine
mixed inhibition with L-serine but no inhibition with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 0.5 mM L-serine, 25°C
additional information
additional information
-
overview
-
additional information
additional information
inhibition kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00152
2-amino-9-naphthalen-2-yl-9H-purin-6-ol
Entamoeba histolytica
count of viable trophozoites after 72 h compared to control measured with 32.16, 64.32, and 160.8 microM inhibitor
0.00061 - 0.072
3-oxo-2-phenyl-3,5-dihydro-2H-pyrazolo[3,4-d]thieno[2,3-b]pyridine-7-carboxylic acid
0.00107
4,10-dihydroxy-1,7-phenanthroline-3,9-dicarboxylic acid
Entamoeba histolytica
count of viable trophozoites after 72 h compared to control measured with 32.16, 64.32, and 160.8 microM inhibitor
0.02983
7beta,11alpha,17-trihydroxyhelioscopinolide E
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.07184
8,14alpha-dihydroxy-5beta,9beta,10alpha,12alpha-12,16-epoxyabiet-13(15)-ene-11,16-dione
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.07184
8,14beta,17-trihydroxy-5beta,8alpha,9beta,10alpha-12,16-epoxyabieta-11,13(15)-dien-16-one
Staphylococcus aureus
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.00061
3-oxo-2-phenyl-3,5-dihydro-2H-pyrazolo[3,4-d]thieno[2,3-b]pyridine-7-carboxylic acid
Entamoeba histolytica
count of viable trophozoites after 72 h compared to control measured with 32.16, 64.32, and 160.8 microM inhibitor
0.072
3-oxo-2-phenyl-3,5-dihydro-2H-pyrazolo[3,4-d]thieno[2,3-b]pyridine-7-carboxylic acid
Escherichia coli
72 micromol, 0.1 M Tris-HCl, pH 7.5, room temperature
0.16
L-cysteine
Vitis vinifera
isozyme VvSERAT2-2, pH and temperature not specified in the publication
1.9
L-cysteine
Vitis vinifera
isozyme VvSERAT2-1, pH and temperature not specified in the publication
3.5
L-cysteine
Entamoeba histolytica
isozyme SAT3, pH 8.0, temperature not specified in the publication
additional information
L-cysteine
Entamoeba histolytica
-
0.03 mM inhibits by 97.3%, 0.5 mM by 95.4%, 1 mM by 98.5%
additional information
L-cysteine
Entamoeba histolytica
0.03 mM inhibits by 97.3%, 0.5 mM by 95.4%, 1 mM by 98.5%
additional information
L-cysteine
Entamoeba histolytica
0.03 mM inhibits by 97.3%, 0.5 mM by 95.4%, 1 mM by 98.5%
additional information
L-cysteine
Entamoeba histolytica
-
0.5 mM inhibits by 75.3%, no inhibition with 0.03 mM
additional information
L-cysteine
Entamoeba histolytica
0.5 mM inhibits by 75.3%, no inhibition with 0.03 mM
additional information
L-cysteine
Entamoeba histolytica
0.5 mM inhibits by 75.3%, no inhibition with 0.03 mM
additional information
L-cysteine
Entamoeba histolytica
-
1 mM inhibits by 37.8%, no inhibition with 0.5 mM and 0.03 mM
additional information
L-cysteine
Entamoeba histolytica
1 mM inhibits by 37.8%, no inhibition with 0.5 mM and 0.03 mM
additional information
L-cysteine
Entamoeba histolytica
1 mM inhibits by 37.8%, no inhibition with 0.5 mM and 0.03 mM
additional information
N-acetyl-L-cysteine
Entamoeba histolytica
-
1 mM weak inhibition (25%)
additional information
N-acetyl-L-cysteine
Entamoeba histolytica
1 mM weak inhibition (25%)
additional information
N-acetyl-L-cysteine
Entamoeba histolytica
1 mM weak inhibition (25%)
additional information
N-acetyl-L-cysteine
Entamoeba histolytica
1 mM, 13.3% inhibition
additional information
N-acetyl-L-cysteine
Entamoeba histolytica
1 mM, 13.3% inhibition
additional information
N-acetyl-L-cysteine
Entamoeba histolytica
1 mM, 27.8% inhibition
additional information
N-acetyl-L-cysteine
Entamoeba histolytica
1 mM, 27.8% inhibition
additional information
N-acetyl-L-serine
Entamoeba histolytica
-
0.5 mM weak inhibition (11.8%)
additional information
N-acetyl-L-serine
Entamoeba histolytica
0.5 mM weak inhibition (11.8%)
additional information
N-acetyl-L-serine
Entamoeba histolytica
0.5 mM weak inhibition (11.8%)
additional information
oxidized glutathione
Entamoeba histolytica
0.5 mM, 19.9% inhibition
additional information
oxidized glutathione
Entamoeba histolytica
0.5 mM, 19.9% inhibition
additional information
reduced glutathione
Entamoeba histolytica
0.5 mM, 10.3% inhibition
additional information
reduced glutathione
Entamoeba histolytica
0.5 mM, 10.3% inhibition
additional information
reduced glutathione
Entamoeba histolytica
0.5 mM, 10.7% inhibition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000812
-
substrate L-serine, pH 7.5, 37°C, recombinant mutant R129A
0.00036
purified recombinant mitochondrial isozyme A, mutant H327A
0.00134
purified recombinant mitochondrial isozyme A, mutant V353E
0.00389
-
substrate L-serine, pH 7.5, 37°C, recombinant wild-type enzyme
0.00513
purified recombinant mitochondrial isozyme A, mutant G354A
0.032
purified recombinant mitochondrial isozyme A, wild-type
10.66
purified recombinant His-tagged enzyme, pH 7.5, 37°C
176.8
Vmax with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C
23.42
Vmax with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C
25
recombinant enzyme, isozyme VvSERAT2-2 in the cysteine synthase complex, pH and temperature not specified in the publication
27.77
Vmax with L-serine, 50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C
41.39
Vmax with L-serine, 50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C
65.75
Vmax with L-serine, 50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C
95.1
Vmax with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C
additional information
additional information
50 mM Tris-HCl, pH 7.5, csat mutant (deficient in cytosolic enzyme), total serine acetyltransferase activity reduced to 71% compared to wild-type in leaves, to 68% in roots
additional information
50 mM Tris-HCl, pH 7.5, csat mutant (deficient in cytosolic enzyme), total serine acetyltransferase activity reduced to 71% compared to wild-type in leaves, to 68% in roots
additional information
-
50 mM Tris-HCl, pH 7.5, csat mutant (deficient in cytosolic enzyme), total serine acetyltransferase activity reduced to 71% compared to wild-type in leaves, to 68% in roots
additional information
50 mM Tris-HCl, pH 7.5, dmsat mutant (deficient in cytosolic and plastidic enzyme), total serine acetyltransferase activity reduced to 80% compared to wild-type in roots, no significant reduction in leaves
additional information
50 mM Tris-HCl, pH 7.5, dmsat mutant (deficient in cytosolic and plastidic enzyme), total serine acetyltransferase activity reduced to 80% compared to wild-type in roots, no significant reduction in leaves
additional information
-
50 mM Tris-HCl, pH 7.5, dmsat mutant (deficient in cytosolic and plastidic enzyme), total serine acetyltransferase activity reduced to 80% compared to wild-type in roots, no significant reduction in leaves
additional information
50 mM Tris-HCl, pH 7.5, psat mutant (deficient in plastidic enzyme), without significant total serine acetyltransferase alterations in leaves and roots
additional information
50 mM Tris-HCl, pH 7.5, psat mutant (deficient in plastidic enzyme), without significant total serine acetyltransferase alterations in leaves and roots
additional information
-
50 mM Tris-HCl, pH 7.5, psat mutant (deficient in plastidic enzyme), without significant total serine acetyltransferase alterations in leaves and roots
additional information
recombinant Arabidopsis serine acetlytransferase activity in transgenic Lupinus angustifolius embryos of the T2 and T4 plant generation is increased severalfold over controls (wild-type and transgenic sunflower seed albumin lupins), 5-12fold and about 5fold in 5F1 (in vitro 4fold over wild-type), 24-31fold and about 20fold in 3A3 (in vitro 12fold over wild-type), 49fold and about 40fold in 5B3 (in vitro 30fold over wild-type), control enzyme activity is roughly about 5 nmol/min/mg protein, correlation to the concentration of key intermediates of the sulphur amino acid biosynthesis (O-acetylserine, free cysteine, glutathione)
additional information
-
recombinant Arabidopsis serine acetlytransferase activity in transgenic Lupinus angustifolius embryos of the T2 and T4 plant generation is increased severalfold over controls (wild-type and transgenic sunflower seed albumin lupins), 5-12fold and about 5fold in 5F1 (in vitro 4fold over wild-type), 24-31fold and about 20fold in 3A3 (in vitro 12fold over wild-type), 49fold and about 40fold in 5B3 (in vitro 30fold over wild-type), control enzyme activity is roughly about 5 nmol/min/mg protein, correlation to the concentration of key intermediates of the sulphur amino acid biosynthesis (O-acetylserine, free cysteine, glutathione)
additional information
-
coupling reaction with cysteine synthase, 50 mM Tris-HCl, pH 8.0, 0.4 mM acetyl-CoA, 4 mM L-serine, 5 mM Na2S, 10 mM DTT, recombinant Entamoeba histolytica cysteine synthase 3, 37°C (amount of L-cysteine produced)
additional information
coupling reaction with cysteine synthase, 50 mM Tris-HCl, pH 8.0, 0.4 mM acetyl-CoA, 4 mM L-serine, 5 mM Na2S, 10 mM DTT, recombinant Entamoeba histolytica cysteine synthase 3, 37°C (amount of L-cysteine produced)
additional information
coupling reaction with cysteine synthase, 50 mM Tris-HCl, pH 8.0, 0.4 mM acetyl-CoA, 4 mM L-serine, 5 mM Na2S, 10 mM DTT, recombinant Entamoeba histolytica cysteine synthase 3, 37°C (amount of L-cysteine produced)
additional information
-
at acetyl-CoA concentration 15fold higher than L-serine concentration, a nonproductive ternary complex of enzyme-CoA-L-serine is formed, kinetics
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 80
45 - 80
45°C: about 50% of maximal activity, 80°C: about 55% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
3 isozymes specific for subcellular compartment: SAT-c, SAT-m, SAT-p
-
-
brenda
At1g55920 SERAT2.1; T-DNA insertion mutants for cytosolic serine acetyltransferase (csat) and plastidic serine acetyltransferase (psat), double mutants of both isoforms (dmsat), and Columbia-0 wild-type
SwissProt
brenda
At5g56760, SERAT1.1; T-DNA insertion mutants for cytosolic serine acetyltransferase (csat) and plastidic serine acetyltransferase (psat), double mutants of both isoforms (dmsat), and Columbia-0 wild-type
SwissProt
brenda
trophozoites of the clonal strain HM1: IMSS cl 6
UniProt
brenda
physical association of serine acetyltransferase with about 5% of the total cellular O-acetylserine sulfhydrylase to form a multienzyme complex given the trivial name cysteine synthethase
-
-
brenda
isozyme VvSERAT2-2; cv. Touriga Nacional, isozyme VvSERAT2-2
UniProt
brenda
isozyme VvSERAT3-1; cv. Touriga Nacional, isozyme VvSERAT3-1
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
SATase isoform genes, Serat1,1 is highly expressed both in root and in dark-grown plant
brenda
additional information
-
accumulation in etiolated plants
brenda
3-week-old rosette leaves. High level of expression for Serat1,1
brenda
3-week-old rosette leaves. High level of expression of Serat2,1
brenda
3-week-old rosette leaves. High level of expression of Serat2,2
brenda
3-week-old rosette leaves. The expression of Serat3,1 is low
brenda
3-week-old rosette leaves. The expression of Serat3,2 is low
brenda
SATase isoform gene Serat1,1 is highly expressed both in root and in dark-grown plant
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
located on the surface or in the intermembrane space of chloroplasts
brenda
cytosolic SATase Serat1,1
brenda
immunofluorescence imaging with antiserum against recombinant protein, and indirectly deduced from missing N-terminal transit peptide
brenda
immunofluorescence imaging with antiserum against recombined protein, and indirectly deduced from missing N-terminal transit peptide
brenda
mitochondrial SATase Serat2,2
brenda
compartment with largest serine acetyltransferase activity of total serine acetyltransferase activity independent of cytosolic serine acetyltransferase activity
brenda
compartment with largest serine acetyltransferase activity of total serine acetyltransferase activity independent of plastidic serine acetyltransferase
brenda
-
between one-third and two-third of the activity
brenda
isozyme VvSERAT2-2, mainly
brenda
additional information
-
isozyme subcellular localization and expression analysis
-
brenda
additional information
isozyme subcellular localization and expression analysis
-
brenda
additional information
isozyme subcellular localization and expression analysis
-
brenda
additional information
isozyme subcellular localization and expression analysis
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the active site residues of isozymes EhSAT1 and of EhSAT3 are identical except for position 208, which is a histidine residue in isozyme EhSAT1 and a serine residue in isozyme EhSAT3
evolution
the enzyme is a member of the VvSERAT protein family, the identified four members of the VvSERAT protein family are assigned to three distinct groups upon their sequence similarities to Arabidopsis SERATs
evolution
enzyme CysE belongs to the hexaxadpeptide acetyltransferase family, characterized by imperfect tandem repeats of the hexapeptide motif [LIV]-[GAED]-X2-[STAV]-X
evolution
-
enzyme CysE belongs to the hexaxadpeptide acetyltransferase family, characterized by imperfect tandem repeats of the hexapeptide motif [LIV]-[GAED]-X2-[STAV]-X
-
evolution
-
enzyme CysE belongs to the hexaxadpeptide acetyltransferase family, characterized by imperfect tandem repeats of the hexapeptide motif [LIV]-[GAED]-X2-[STAV]-X
-
malfunction
-
compounds that (partially) block the Escherichia coli enzyme activity block the growth of Entamoeba histolytica trophozoites but not mammalian cells
malfunction
compounds that (partially) block the Escherichia coli enzyme activity block the growth of Entamoeba histolytica trophozoites but not mammalian cells
malfunction
compounds that (partially) block the Escherichia coli enzyme activity block the growth of Entamoeba histolytica trophozoites but not mammalian cells
malfunction
the MSMEG_5947 knockout mutant strain grows slower than the wild-type strain, and the lack of the CysE protein causes drastic morphological changes. Deletion of the serine acetyltransferase retards the growth of the organism, but serine acetyltransferase expression is not essential for the survival of the bacterium
malfunction
overexpression of Arabidopsis thaliana serine acetyltransferase in maize leaves increases seed-specific methionine-rich zeins, overexpression has the effect of, not only enhancing S-assimilation, but also, indirectly impacting expression of high-Met seed storage proteins
malfunction
-
compounds that (partially) block the Escherichia coli enzyme activity block the growth of Entamoeba histolytica trophozoites but not mammalian cells
-
malfunction
-
the MSMEG_5947 knockout mutant strain grows slower than the wild-type strain, and the lack of the CysE protein causes drastic morphological changes. Deletion of the serine acetyltransferase retards the growth of the organism, but serine acetyltransferase expression is not essential for the survival of the bacterium
-
malfunction
-
compounds that (partially) block the Escherichia coli enzyme activity block the growth of Entamoeba histolytica trophozoites but not mammalian cells
-
metabolism
first step of the L-cysteine biosynthesis pathway
metabolism
rate-limiting step in the cysteine biosynthesis
metabolism
serine acetyltransferase (SAT) catalyzes the limiting reaction in plant and microbial biosynthesis of cysteine. In addition to its enzymatic function, serine acetyltransferase forms a macromolecular complex with O-acetylserine sulfhydrylase, EC 2.5.1.47. Formation of the cysteine regulatory complex (CRC) is a critical biochemical control feature in plant sulfur metabolism. A role for CRC formation as a molecular chaperone to maintain SAT activity in response to an environmental stress, e.g. cold, is possible for the multienzyme complex in plants
metabolism
serine acetyltransferase provides O-acetylserine for the biosynthesis of cysteine and thereby regulates the activity of O-acetylserine(thiol)lyase, EC 2.5.1.47, which catalyzes the last step of cysteine biosynthesis and reversibly interacts with serine acetyltransferase in the cysteine synthase complex
metabolism
serine acetyltransferase provides O-acetylserine for the biosynthesis of cysteine and thereby regulates the activity of O-acetylserine(thiol)lyase, EC 2.5.1.47, which catalyzes the last step of cysteine biosynthesis and reversibly interacts with serine acetyltransferase in the cysteine synthase complex. Only isozyme VvSERAT2-1 lacks the canonical C-terminal tail of plant SERATs and does not form the cysteine synthase complex and is almost insensitive to cysteine inhibition
metabolism
serine O-acetyltransferase (SAT) is a key enzyme converting serine into O-acetylserine in the synthesis of sulfur-containing amino acids
metabolism
enzyme CysE is involved in the cysteine biosynthetic pathway
metabolism
serine acetyltransferase (SAT) is a key control point for S-assimilation leading to Cys and Met biosynthesis
metabolism
serine acetyltransferase (SAT) is a key control point for S-assimilation leading to Cys and Met biosynthesis. Met synthesis in maize is not strictly controlled by the enzyme cystathionine gamma-synthase (CGS)
metabolism
-
serine O-acetyltransferase (SAT) is a key enzyme converting serine into O-acetylserine in the synthesis of sulfur-containing amino acids
-
physiological function
the end product L-cysteine is essential for the synthesis of Fe-S proteins and it is necessary for growth, survival, attachment, and anti-oxidation
physiological function
in the two-step cysteine biosynthetic pathway, CysE/SAT (serine acetyltransferase) transfers acetyl moiety from acetyl-CoA to L-serine resulting in O-acetyl serine (OAS). Subsequently, pyridoxal 5'-phosphate-dependent O-acetyl serine sulfhydralase (OASS), also known as CysK, transfers reduced sulfide to OAS in a beta-replacement reaction yielding L-cysteine
physiological function
serine acetyltransferase (SAT) is a key control point for S-assimilation leading to Cys and Met biosynthesis
physiological function
serine acetyltransferase (SAT) is a key control point for S-assimilation leading to Cys and Met biosynthesis. SAT overexpression is known to enhance S-assimilation without negative impact on plant growth, it increases seed-specific methionine-rich D-zeins
additional information
enzyme residues His169 and Asp154 form a catalytic dyad for general base catalysis, and His189 may stabilize the oxyanion reaction intermediate. Glu177 helps to position Arg203 and His204 and the beta1c-beta2c loop for serine binding. A similar role for ionic interactions formed by Lys230 is required for CoA binding. Arg253 is important for the enhanced catalytic efficiency of SAT in the cysteine regulatory complex and suggest that movement of the residue may stabilize CoA binding in the macromolecular complex
additional information
-
enzyme residues His169 and Asp154 form a catalytic dyad for general base catalysis, and His189 may stabilize the oxyanion reaction intermediate. Glu177 helps to position Arg203 and His204 and the beta1c-beta2c loop for serine binding. A similar role for ionic interactions formed by Lys230 is required for CoA binding. Arg253 is important for the enhanced catalytic efficiency of SAT in the cysteine regulatory complex and suggest that movement of the residue may stabilize CoA binding in the macromolecular complex
additional information
-
histidine 208 appears to be one of the important residues that distinguish the serine substrate from the cysteine inhibitor. Homology three-dimensional structure modeling of isozyme SAT3, free or in complex with cysteine or serine, using the isozyme EhSAT1 crystal structures, PDB IDs 3P47 and 3Q1X as a templates, overview
additional information
histidine 208 appears to be one of the important residues that distinguish the serine substrate from the cysteine inhibitor. Homology three-dimensional structure modeling of isozyme SAT3, free or in complex with cysteine or serine, using the isozyme EhSAT1 crystal structures, PDB IDs 3P47 and 3Q1X as a templates, overview
additional information