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Enzyme Nomenclature
Information on EC 2.3.1.30 - serine O-acetyltransferase
for references in articles please use BRENDA:EC2.3.1.30
Word Map on EC 2.3.1.30
- 2.3.1.30
- o-acetylserine
- l-cysteine
-
sulfhydrylase
- o-acetyl-l-serine
- oas-tls
- foot-and-mouth
- desulfhydrase
-
o-acetylserinethiollyase
-
slc26a1
-
bienzyme
- thlaspi
- phytochelatins
- medicine
- molecular biology
- agriculture
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.3.1.30
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RECOMMENDED NAME
GeneOntology No.
serine O-acetyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
ping pong bi bi mechanism
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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; 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; 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
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acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
steady-state random-order mechanism
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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
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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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:L-serine O-acetyltransferase
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CAS REGISTRY NUMBER
COMMENTARY
9023-16-9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
3 isozymes specific for subcellular compartment: SAT-c, SAT-m, SAT-p
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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
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
gene SAT1-6, mitochondrial isozyme; gene SAT-1, isoform A
SwissProt
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
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isozyme VvSERAT2-2; cv. Touriga Nacional, isozyme VvSERAT2-2
UniProt
isozyme VvSERAT3-1; cv. Touriga Nacional, isozyme VvSERAT3-1
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
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; 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; 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
additional information
evolution
A0A0C5DAX6;, A0A0C5DES6;, B0LLV2;
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; 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; 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; 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
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; 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
malfunction
compounds that (partially) block the Escherichia coli enzyme activity block the growth of Entamoeba histolytica trophozoites but not mammalian cells
malfunction
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compounds that (partially) block the Escherichia coli enzyme activity block the growth of Entamoeba histolytica trophozoites but not mammalian cells
malfunction
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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
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compounds that (partially) block the Escherichia coli enzyme activity block the growth of Entamoeba histolytica trophozoites but not mammalian cells
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malfunction
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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
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metabolism
first step of the L-cysteine biosynthesis pathway; first step of the L-cysteine biosynthesis pathway; first step of the L-cysteine biosynthesis pathway
metabolism
rate-limiting step in the cysteine biosynthesis; rate-limiting step in the cysteine biosynthesis
metabolism
A0A0C5DAX6;, A0A0C5DES6;, B0LLV2;
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; 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; 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; 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 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 O-acetyltransferase (SAT) is a key enzyme converting serine into O-acetylserine in the synthesis of sulfur-containing amino acids
metabolism
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serine O-acetyltransferase (SAT) is a key enzyme converting serine into O-acetylserine in the synthesis of sulfur-containing amino acids
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additional information
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the gene lying upstream of cysK is predicted to encode a homoserine trans-succinylase (metA). The gene is cloned from Lactobacillus casei strain FAM18110. The purified, recombinant protein does not acylate L-homoserine in vitro. Instead, it catalyzes the formation of O-acetyl serine from L-serine and acetyl-CoA. Furthermore, the plasmid expressing the Lactobacillus casei gene complements an Escherichia coli cysE mutant strain but not an Escherichia coli metA mutant. This clearly demonstrates that the gene annotated as metA, EC 2.3.1.46, in fact encodes the SAT function and should be annotated as cysE, EC 2.3.1.30
additional information
the gene lying upstream of cysK is predicted to encode a homoserine trans-succinylase (metA). The gene is cloned from Lactobacillus casei strain FAM18110. The purified, recombinant protein does not acylate L-homoserine in vitro. Instead, it catalyzes the formation of O-acetyl serine from L-serine and acetyl-CoA. Furthermore, the plasmid expressing the Lactobacillus casei gene complements an Escherichia coli cysE mutant strain but not an Escherichia coli metA mutant. This clearly demonstrates that the gene annotated as metA, EC 2.3.1.46, in fact encodes the SAT function and should be annotated as cysE, EC 2.3.1.30
additional information
the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex; the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex; the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex; the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex
additional information
the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex; the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex; the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex; the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex
additional information
the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex; the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex; the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex; the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex
additional information
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the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex; the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex; the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex; the enzyme reversibly interacts with O-acetylserine(thiol)lyase in the cysteine synthase complex
additional information
the enzyme displays a high sequence homology to L-homoserine O-acetyltransferase, but it prefers L-serine over L-homoserine as the substrate, structure analysis and modeling, overview
additional information
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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
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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
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
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the gene lying upstream of cysK is predicted to encode a homoserine trans-succinylase (metA). The gene is cloned from Lactobacillus casei strain FAM18110. The purified, recombinant protein does not acylate L-homoserine in vitro. Instead, it catalyzes the formation of O-acetyl serine from L-serine and acetyl-CoA. Furthermore, the plasmid expressing the Lactobacillus casei gene complements an Escherichia coli cysE mutant strain but not an Escherichia coli metA mutant. This clearly demonstrates that the gene annotated as metA, EC 2.3.1.46, in fact encodes the SAT function and should be annotated as cysE, EC 2.3.1.30
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additional information
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the enzyme displays a high sequence homology to L-homoserine O-acetyltransferase, but it prefers L-serine over L-homoserine as the substrate, structure analysis and modeling, overview
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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
L-serine + acetyl-CoA
O-acetyl serine + CoA
-
subsequently, cysteine synthase forms L-cysteine from O-acetyl serine
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?
L-serine + acetyl-CoA
O-acetylserine + CoA
no major contribution to total cysteine biosynthesis
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?
acetyl-CoA + L-Ser
CoA + O-acetyl-L-Ser
key enzyme in L-cysteine biosynthesis
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-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
key role in the sulfur assimilatory pathway
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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
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?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
regulatory role in cysteine biosynthesis
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?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
regulatory role in cysteine biosynthesis
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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
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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
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-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
each serine acetyltransferase isoform seems to have its specific role for cysteine biosynthesis
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?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
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simultaneous expression of serine acetyltransferase and cysteine synthase results in enhanced sulfate uptake and increased biomass in Ipomaea aquatica
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?
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
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-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
dependent on L-serine and acetyl-CoA
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?
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
-
-
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ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
regulatory role in cysteine biosynthesis
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ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
key role in the sulfur assimilatory pathway
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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
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-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first enzyme in L-cysteine synthesis pathway
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ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first enzyme in L-cysteine synthesis pathway
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ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
first step of L-cysteine synthesis
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-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
Escherichia coli B / ATCC 11303
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first enzyme in L-cysteine synthesis pathway
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ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
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L-serine acetylation is an equilibrium ordered mechanism
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-
r
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
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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
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-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
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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
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-
?
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
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ir
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
-
enzyme in metabolic pathway of sulfur from sulfide to methionine
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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
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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
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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
-
key role in the sulfur assimilatory pathway
-
?
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
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0.5% of the activity with L-serine
-
-
?
L-serine + acetyl-CoA
O-acetyl-L-serine + CoA
-
-
-
?
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
?
-
-
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
?
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Q6F4D7
key enzyme in L-cysteine biosynthesis
-
-
?
L-serine + acetyl-CoA
O-acetyl serine + CoA
Q401L4, Q401L5
-
subsequently, cysteine synthase forms L-cysteine from O-acetyl serine
-
?
L-serine + acetyl-CoA
O-acetylserine + CoA
Q42538, Q42588
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
Q39218, Q42588
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
Q39218, Q42538, Q42588
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
Q39218, Q42538, Q42588
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
Q39218, Q42538, Q42588
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
Q39218, Q42588
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
Q8S895, Q8W2B8
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
A0R4T4
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
P95231
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
Q8H0P5, Q8H0P6, Q8H0P7
-
-
?
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
P29847
-
-
?
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
D2Z028
-
-
-
?
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
A0A0C5DAX6, A0A0C5DES6, B0LLV2
-
-
-
?
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.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
reduced glutathione
0.5 mM weak inhibition; 0.5 mM, weak inhibition
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
-
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
-
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
A0A0C5DAX6;, A0A0C5DES6;, B0LLV2;
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
-
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
-
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
0.145
acetyl-CoA
recombinant isozyme A, wild-type
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
-
cysteine synthase bienzyme complex
-
additional information
additional information
-
Km of mutant enzymes
-
additional information
additional information
-
Km for L-serine and acetyl-CoA of recombinant L-cysteine-binding motif mutants, 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; Michaelis-Menten kinetics, overview
-
additional information
additional information
Michaelis-Menten kinetics, overview; Michaelis-Menten kinetics, overview
-
additional information
additional information
Michaelis-Menten kinetics, overview; Michaelis-Menten kinetics, overview
-
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
additional information
additional information
-
overview
-
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
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;
Q9U8X2
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;
Q9U8X2
count of viable trophozoites after 72 h compared to control measured with 32.16, 64.32, and 160.8 microM inhibitor
0.00061
3-oxo-2-phenyl-3,5-dihydro-2H-pyrazolo[3,4-d]thieno[2,3-b]pyridine-7-carboxylic acid
Entamoeba histolytica;
Q9U8X2
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 DH5[alpha];
-
72 micromol, 0.1 M Tris-HCl, pH 7.5, room temperature
0.16
L-cysteine
Vitis vinifera;
A0A0C5DAX6, A0A0C5DES6, B0LLV2
isozyme VvSERAT2-2, pH and temperature not specified in the publication
1.9
L-cysteine
Vitis vinifera;
A0A0C5DAX6, A0A0C5DES6, B0LLV2
isozyme VvSERAT2-1, pH and temperature not specified in the publication
3.5
L-cysteine
Entamoeba histolytica;
Q401L4, Q401L5
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%; 0.5 mM inhibits by 75.3%, no inhibition with 0.03 mM; 1 mM inhibits by 37.8%, no inhibition with 0.5 mM and 0.03 mM
additional information
L-cysteine
Entamoeba histolytica;
Q401L4
0.03 mM inhibits by 97.3%, 0.5 mM by 95.4%, 1 mM by 98.5%; 0.5 mM inhibits by 75.3%, no inhibition with 0.03 mM; 1 mM inhibits by 37.8%, no inhibition with 0.5 mM and 0.03 mM
additional information
L-cysteine
Entamoeba histolytica;
Q401L5
0.03 mM inhibits by 97.3%, 0.5 mM by 95.4%, 1 mM by 98.5%; 0.5 mM inhibits by 75.3%, no inhibition with 0.03 mM; 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, 13.3% inhibition; 1 mM, 27.8% inhibition; 1 mM weak inhibition (25%)
additional information
N-acetyl-L-cysteine
Entamoeba histolytica;
Q401L4
1 mM, 13.3% inhibition; 1 mM, 27.8% inhibition; 1 mM weak inhibition (25%)
additional information
N-acetyl-L-cysteine
Entamoeba histolytica;
Q401L5
1 mM, 13.3% inhibition; 1 mM, 27.8% inhibition; 1 mM weak inhibition (25%)
additional information
N-acetyl-L-serine
Entamoeba histolytica;
-
0.5 mM weak inhibition (11.8%)
additional information
N-acetyl-L-serine
Entamoeba histolytica;
Q401L4
0.5 mM weak inhibition (11.8%)
additional information
N-acetyl-L-serine
Entamoeba histolytica;
Q401L5
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;
Q401L4
0.5 mM, 19.9% inhibition
additional information
oxidized glutathione
Entamoeba histolytica;
Q401L5
0.5 mM, 19.9% inhibition
additional information
reduced glutathione
Entamoeba histolytica;
-
0.5 mM, 10.3% inhibition; 0.5 mM, 10.7% inhibition
additional information
reduced glutathione
Entamoeba histolytica;
Q401L4
0.5 mM, 10.3% inhibition; 0.5 mM, 10.7% inhibition
additional information
reduced glutathione
Entamoeba histolytica;
Q401L5
0.5 mM, 10.3% inhibition; 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
0.00036
purified recombinant mitochondrial isozyme A, mutant H327A
0.00134
purified recombinant mitochondrial isozyme A, mutant V353E
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
23.42
Vmax with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C
25
A0A0C5DAX6;, A0A0C5DES6;, B0LLV2;
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
176.8
Vmax with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C
additional information
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
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; 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; 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; 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, csat mutant (deficient in cytosolic enzyme), total serine acetyltransferase activity reduced to 71% compared to wild-type in leaves, to 68% in roots; 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; 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; 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
-
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); 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); 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); 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); 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); 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); 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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 80
45°C: about 50% of maximal activity, 80°C: about 55% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
SATase isoform genes, Serat1,1 is highly expressed both in root and in dark-grown plant
3-week-old rosette leaves. High level of expression for Serat1,1; 3-week-old rosette leaves. High level of expression of Serat2,1; 3-week-old rosette leaves. High level of expression of Serat2,2; 3-week-old rosette leaves. The expression of Serat3,1 is low; 3-week-old rosette leaves. The expression of Serat3,2 is low
SATase isoform gene Serat1,1 is highly expressed both in root and in dark-grown plant
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
located on the surface or in the intermembrane space of chloroplasts
immunofluorescence imaging with antiserum against recombinant protein, and indirectly deduced from missing N-terminal transit peptide; immunofluorescence imaging with antiserum against recombined protein, and indirectly deduced from missing N-terminal transit peptide; immunofluorescence imaging with antiserum against recombined protein, and indirectly deduced from missing N-terminal transit peptide
compartment with largest serine acetyltransferase activity of total serine acetyltransferase activity independent of cytosolic serine acetyltransferase activity; compartment with largest serine acetyltransferase activity of total serine acetyltransferase activity independent of plastidic serine acetyltransferase
additional information
isozyme subcellular localization and expression analysis; isozyme subcellular localization and expression analysis; isozyme subcellular localization and expression analysis; isozyme subcellular localization and expression analysis
-
additional information
isozyme subcellular localization and expression analysis; isozyme subcellular localization and expression analysis; isozyme subcellular localization and expression analysis; isozyme subcellular localization and expression analysis
-
additional information
isozyme subcellular localization and expression analysis; isozyme subcellular localization and expression analysis; isozyme subcellular localization and expression analysis; isozyme subcellular localization and expression analysis
-
additional information
-
isozyme subcellular localization and expression analysis; isozyme subcellular localization and expression analysis; isozyme subcellular localization and expression analysis; isozyme subcellular localization and expression analysis
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Entamoeba histolytica;
Glycine max;
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
Streptomyces lavendulae;
Q9KNT2
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961);
P43886
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P43886
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P43886
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
P43886
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24600
x * 30000, recombinant His-tagged enzyme, SDS-PAGE, x * 24600, about, sequence calculation
29261
-
4 * 29261, ultracentrifugation, gel filtration, crystallographic data
30000
x * 30000, recombinant His-tagged enzyme, SDS-PAGE, x * 24600, about, sequence calculation
33000
34000
-
2 * 34000, serine acetyltransferase + 2 * 36000, O-acetylserine (thiol) lyase, forming the cysteine synthase complex, SDS-PAGE
36000
-
2 * 34000, serine acetyltransferase + 2 * 36000, O-acetylserine (thiol) lyase, forming the cysteine synthase complex, SDS-PAGE
37000
SDS-PAGE, recombinant purified enzyme monomer with 2.6 kDa histidine tag
37400
SDS-PAGE, recombinant purified enzyme monomer with 2.6 kDa histidine tag
40000
SDS-PAGE, recombinant purified enzyme monomer with 2.6 kDa histidine tag
181000
hexameric enzyme, gel filtration and dynamic light scattering
450000 - 500000
-
multienzyme complex of L-serine acetyltransferase and L-cysteine synthase, gel filtration
additional information
additional information
-
multi-enzyme complex is formed between serine acetyltransferase and cysteine synthase possibly leading to metabolic channeling
additional information
amino acid sequence alignment; amino acid sequence alignment; amino acid sequence alignment
additional information
amino acid sequence alignment; amino acid sequence alignment; amino acid sequence alignment
additional information
amino acid sequence alignment; amino acid sequence alignment; amino acid sequence alignment
additional information
amino acid sequence alignment
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
tetramer
trimer
additional information
?
-
x * 31000, recombinant enzyme, SDS-PAGE; x * 43737, native enzyme, amino acid sequence determination
?
x * 30000, recombinant His-tagged enzyme, SDS-PAGE, x * 24600, about, sequence calculation
?
-
x * 30000, recombinant His-tagged enzyme, SDS-PAGE, x * 24600, about, sequence calculation
-
?
A0A0C5DAX6;, A0A0C5DES6;, B0LLV2;
x * 294600, sequence calculation; x * 323400, sequence calculation; x * 323800, sequence calculation
tetramer
-
2 * 34000, serine acetyltransferase + 2 * 36000, O-acetylserine (thiol) lyase, forming the cysteine synthase complex, SDS-PAGE
tetramer
-
4 * 29261, ultracentrifugation, gel filtration, crystallographic data
tetramer
Escherichia coli B / ATCC 11303
-
4 * 29261, ultracentrifugation, gel filtration, crystallographic data
-
trimer
3 * x, predicted from homology modeling with Escherichia coli enzyme crystal structure
trimer
-
3 * x, predicted from homology modeling with Escherichia coli enzyme crystal structure
-
additional information
-
enzyme exists in a high-molecular weight enzyme complex with cysteine synthase
additional information
-
cysteine synthase from Escherichia coli is a bienzyme complex comprised of serine acetyltransferase and O-acetylserine sulfhydrylase A. The C-terminus of SAT, Ile273, along with Glu268 and Asp271, is essential for complex formation
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoryletd in vivo. Phosphorylated on Ser378 by calcium-dependent protein kinase. Phosphorylation renders the enzyme insensitive to feedback inhibition by cysteine. H2O2-induced increase in the activity of GmSerat2,1 contributes to the oxidative stress response in soybean. Phosphorylation does not affect the stability
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method. Crystal structure of Arabidopsis thaliana O-acetylserine aulfhydrylase bound with a peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase (C10 peptide) at 2.9 A resolution
-
purified recombinant enzyme in apo state and in complex with coenzyme A, hanging drop vapour diffusion methd, mixing of 14 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 150 mM NaCl, 5% glycerol, and 5 mM 2-mercaptoethanol with reservoir solution containing 7% w/v PEG 1000, 7% w/v PEG 3350, 5% v/v MPD, 0.12 methylene glycol, 0.1 M Tris-HCl, pH 7.4, and 50 mM MgCl2, 16°C, X-ray diffraction structure determination and analysis at 1.96 A and 1.87 A resolution, respectively
crystal structure of serine acetyltransferase (SAT) isoform 1 at 1.77 A, in complex with its substrate serine at 1.59 A and inhibitor Cys at 1.78 A resolution is reported
hanging drop vapour diffusion method, 8-16% polyethylene glycol 1000, 10 mM Tris-HCl, pH 7.5, 2-4 weeks, room temperature, structure analysis
-
recombinant enzyme, crystals grew from 0.1 M MES, pH 6.6, 1ß% 2-methyl-2,3-pentanediol, 0.5 M sodium thiocyanate, 5.5 mM cysteine, and SeMet SAT (10 mg/ml) sitting drops, at 20°C within 7 days. 2.2 A crystal structure of the enzyme, which is s dimer of trimers in complex with cysteine
-
purified enzyme in apoform and complexed with L-serine and CoA, hanging drop vapor diffusion method, mixing of 0.005 ml of 10-20 mg/ml protein in 10 mM Tris, pH 8.0, 50 mM NaCl, and 5 mM 2-mercaptoethanol with 0.005 ml of reservoir solution, containing 1.8 M ammonium phosphate, 100 mM imidazole, pH 8.0, and equilibration ver 0.5 ml reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.7-3.0 A resolution, method optimization
crystals of Haemophilus influenzae O-acetylserine sulfhydrylase (EC 2.5.1.47) in complex with the C-terminal 10-residue peptide of serine acetyltransferase are prepared under silicon oil by using the sitting drop method
-
X-ray crystallographic structure of the enzyme in binary complexes with cysteine and CoA and refined to resolutions of 1.85 and 2.0 A, respectively
-
purified recombinant wild-type and mutant G52A-P55G enzymes, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml of protein in 20 mM Tris-HCl, pH 7.6, 0.2 M NaCl, 5 mM dithiothreitol, and 1 mM EDTA, with 0.001 ml of precipitant solution containing 0.1 M Tris-HCl, pH 7.5, 25% w/v PEG 4000, and 0.2 M ammonium acetate, 3 weeks, structure modeling, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0
-
SAT DELTAC10 mutant, lacking 10 amino acid residues at the C-terminal end is inactivated after 12 h
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30°C or -80°C, 50 mM Tris-HCl, pH 8.0, 10-20% glycerol in small aliquots, fully active after more than 3 months
-
4°C, the purified recombinant wild-type and mutant isozyme EhSAT1 proteins are stable over long storage
4°C, the purified recombinant wild-type and mutant isozyme EhSAT3 proteins are unstable due to protein aggregation over long storage
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cells centrifuged, resuspended in 0.01 M Tris-HCl, pH 7.5, sonicated, centrifuged, supernatant subjected to streptomycin sulfate (10%) and ammonium sulfate (70%) precipitation, precipitated protein dissolved in same buffer, desalted on a G-25 column
frozen plant material is homogenized in extraction buffer (50 mM HEPES/KOH, pH 7.4) and centrifuged, supernatant desalted and used for enzyme assays; frozen plant material is homogenized in extraction buffer (50 mM HEPES/KOH, pH 7.4) and centrifuged, supernatant desalted and used for enzyme assays
partially
recombinant cells are centrifuged, pellet washed with PBS, pH 7.4, resuspended in lysis buffer (50 mM Tris-HCl, pH 8.0), incubated, sonicated, centrifuged, Ni2+ -NTA agarose column, washed with buffer (50 mM Tris-HCl, pH 8.0), eluted imidazole, SDS-PAGE, dialyzed with 50 mM Tris-HCl, pH 8.0, storage with 20% glycerol at -80°C; recombinant cells are centrifuged, pellet washed with PBS, pH 7.4, resuspended in lysis buffer (50 mM Tris-HCl, pH 8.0), incubated, sonicated, centrifuged, Ni2+ -NTA agarose column, washed with buffer (50 mM Tris-HCl, pH 8.0), eluted imidazole, SDS-PAGE, dialyzed with 50 mM Tris-HCl, pH 8.0, storage with 20% glycerol at -80°C; recombinant cells are centrifuged, pellet washed with PBS, pH 7.4, resuspended in lysis buffer (50 mM Tris-HCl, pH 8.0), incubated, sonicated, centrifuged, Ni2+ -NTA agarose column, washed with buffer (50 mM Tris-HCl, pH 8.0), eluted imidazole, SDS-PAGE, dialyzed with 50 mM Tris-HCl, pH 8.0, storage with 20% glycerol at -80°C
recombinant enzyme
recombinant enzyme by nickel affinity chromatography and gel filtration
recombinant from E. coli
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, dialysis and ultrafiltration
recombinant wild-type and mutants as S-tagged protein from E. coli
cells centrifuged, resuspended in 0.01 M Tris-HCl, pH 7.5, sonicated, centrifuged, supernatant subjected to streptomycin sulfate (10%) and ammonium sulfate (70%) precipitation, precipitated protein dissolved in same buffer, desalted on a G-25 column
-
cells centrifuged, resuspended in 0.01 M Tris-HCl, pH 7.5, sonicated, centrifuged, supernatant subjected to streptomycin sulfate (10%) and ammonium sulfate (70%) precipitation, precipitated protein dissolved in same buffer, desalted on a G-25 column
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and DNA sequencing of 3 isozymes, complementation of Cys- mutant Escherichia coli strain JM39 with the 3 isozymes, sequence analysis of cytosolic isozyme
-
construction of an inactivated mutant by targeted disruption of CysE gene for usage in complementation assays
-
construction of cysE gene mutants by random PCR mutagenesis, expression in Escherichia coli cysteine auxotrophic strain JM39-8
-
cotyledon segments of seedlings of Ipomaea aquatica are transformed with Arabidopsis serine acetyltransferase and rice cysteine synthase genes under the control of the cauliflower mosaic virus 35S promoter. Simultaneous expression of serine acetyltransferase and cysteine synthase results in enhanced sulfate uptake and increased biomass in Ipomaea aquatica
-
expression as glutathione-S-transferase fusion protein, amino acid sequence
-
expression in Cys- Escherichia coli mutant and functional complementation, transient expression as GFP-fusion and beta-glucuronidase-fusion protein in plants
-
expression in Escherichia coli
expression in Escherichia coli as a fusion protein with glutathione-S-transferase
-
expression in Escherichia coli SAT inactivated mutant; expression of wild-type and mutants in Escherichia coli SAT inactivated mutant as S-tagged protein
expression in Escherichia coli, functional complementation of Escherichia coli cysA- mutant, DNA and amino acid sequence detemination
O13389;
expression in inactivated Escherichia coli mutant, insensitive against inhibition by L-cysteine; expression in inactivated Escherichia coli mutant, unaltered L-cysteine sensitivity compared to wild-type; expression in inactivated Escherichia coli mutant, unaltered L-cysteine sensitivity compared to wild-type
Q8H0P5;, Q8H0P6;, Q8H0P7;
expression in Saccharomyces cerevisiae.Increase in cysteine production confers enhanced resistance against osmotic stress in the osmosensitive yeast strain
-
expression in Salmonella typhimurium Cys- strain DW 18.1 from plasmid
-
expression of 3 isozymes SAT-m, SAT-p, SAT-c as GFP-fusion proteins in Arabidopsis thaliana; overexpression of 3 isozymes SAT-m, SAT-p, SAT-c in Escherichia coli BL21 (DE3)
-
expression of His-tagged protein encoded on gene cmSAT in Escherichia coli, functional complementation of SAT-deficient Escherichia coli strain JM15, DNA and amino acid sequence determination
-
expression of SAT1 gene as glutathione-S-transferase fusion protein in Escherichia coli DH5alpha, complementation of serine acetyltransferase mutant Escherichia coli strain JM39, single copy gene, amino acid sequence determination; SAT1 is closely linked to SAT5, high DNA sequence homology
expression of wild-type and mutants in Escherichia coli
gene cysE or MSMEG_5947, DNA and amino acid sequence determination and analysis, functional recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene cysE or Rv2335, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene dcsE, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
gene FgSAT or FGSG_00186, DNA and amino acid sequence determination and analysisphylogenetic analysis and tree, real-time PCR expression analysis, genetic complementation of FgSAT deletion mutant
gene LSEI 0479 lying upstream of cysK is predicted to encode a homoserine trans-succinylase (metA). The gene is cloned from Lactobacillus casei strain FAM18110, and recombinantly expressed in Escherichia coli strain BL21(DE3). The purified, recombinant protein does not acylate L-homoserine in vitro. Instead, it catalyzes the formation of O-acetyl serine from L-serine and acetyl-CoA. Furthermore, the plasmid expressing the Lactobacillus casei gene complements an Escherichia coli cysE mutant strain but not an Escherichia coli metA mutant. This clearly demonstrates that the gene annotated as metA in fact encodes the SAT function and should be annotated as cysE
gene SAT1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
insertional inactivation of wild-type CysE gene from Escherichia coli C600
-
isolation of cDNA clone from Citrullus vulgaris genetic library by complementation of a Cys- Escherichia coli strain JM 39/5, single copy gene, DNA and amino acid sequence determination
-
isozyme VvSERAT1-1, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of GFP-tagged VvSERAT isozyme in Arabidopsis thaliana and in Vitis vinifera protoplasts with specific subcellular localization of the isozyme; isozyme VvSERAT2-1, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of GFP-tagged VvSERAT isozyme in Arabidopsis thaliana and in Vitis vinifera protoplasts with specific subcellular localization of the isozyme; isozyme VvSERAT2-2, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of GFP-tagged VvSERAT isozyme in Arabidopsis thaliana and in Vitis vinifera protoplasts with specific subcellular localization of the isozyme; isozyme VvSERAT3-1, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of GFP-tagged VvSERAT isozyme in Arabidopsis thaliana and in Vitis vinifera protoplasts with specific subcellular localization of the isozyme
A0A0C5DAX6;, A0A0C5DES6;, B0LLV2;
nickel and cobalt resistance engineered in Escherichia coli by overexpression of serine acetyltransferase from the nickel hyperaccumulator plant Thlaspi goesingense; nickel and cobalt resistance engineered in Escherichia coli by overexpression of serine acetyltransferase from the nickel hyperaccumulator plant Thlaspi goesingense; nickel and cobalt resistance engineered in Escherichia coli by overexpression of serine acetyltransferase from the nickel hyperaccumulator plant Thlaspi goesingense
overexpression in Escherichia coli
overexpression in Escherichia coli, construction of an expression vector which increases the expression to 17% of the soluble cell protein
-
PCR-amplification, expression of histidine tagged gene in Escherichia coli BL21 (DE3) pLysS, heat shock transformed; PCR-amplification, expression of histidine tagged gene in Escherichia coli BL21 (DE3) pLysS, heat shock transformed; PCR-amplification, expression of histidine tagged gene in Escherichia coli BL21 (DE3) pLysS, heat shock transformed
PCR-amplification, plasmid transferred to Agrobacterium tumefaciens Ag10 for transfection of Lupinus angustifolius (cultivar Kalya)
-