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(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
2-amino-9-naphthalen-2-yl-9H-purin-6-ol
-
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
4,10-dihydroxy-1,7-phenanthroline-3,9-dicarboxylic acid
-
7beta,11alpha,17-trihydroxyhelioscopinolide E
-
-
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
-
-
apocynin
41% inhibition at 0.005 mM with 500 ng enzyme
ATP
-
mixed non-competitive with respect to serine
Berberine
the ligand binds at the trimer-trimer interface, 24% inhibition at 0.005 mM with 500 ng enzyme
EDTA
1.0 mM, complete inhibition
glutathione
-
weak, allosteric inhibition
L-alanine
-
noncompetitive against acetyl-CoA
L-cystine
-
allosteric inhibition
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
N-acetyl-L-serine
0.5 mM, weak inhibition
oxidized glutathione
0.5 mM, weak inhibition
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
CoA
-
-
cysteine
feedback inhibition; feedback inhibition
cysteine
competitive inhibitor of Ser
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
D-cysteine
-
-
D-cysteine
-
no inhibition
glycine
-
competitive against L-serine, noncompetitive against acetyl-CoA
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
hydroxylamine
-
-
L-cysteine
-
IC50: 0.0031 mM
L-cysteine
-
feed-back inhibition; weak
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
-
allosteric inhibition
L-cysteine
-
recombinant wild-type and mutants, not mutant M280I, inhibitor binding motif
L-cysteine
-
feed-back inhibition
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
-
feed-back inhibition
L-cysteine
-
allosteric inhibition
L-cysteine
feedback inhibition; feedback inhibition; feedback inhibition; feedback inhibition, isozyme VvSERAT2-1 is almost insensitive to cysteine inhibition
L-homocysteine
-
weak
L-homoserine
-
weak
L-methionine
-
-
L-serine
-
above 3 mM, weak
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
N-acetyl-L-cysteine
-
weak
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
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
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 inhibition by N-acetylserine
-
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
-
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0.0000304
-
substrate L-serine, pH 7.5, 37°C, recombinant mutant D94A
0.0000812
-
substrate L-serine, pH 7.5, 37°C, recombinant mutant R129A
0.000141
-
substrate L-serine, pH 7.5, 37°C, recombinant mutant N148A
0.000218
-
substrate L-serine, pH 7.5, 37°C, recombinant mutant H95A
0.00036
purified recombinant mitochondrial isozyme A, mutant H327A
0.000696
-
substrate L-serine, pH 7.5, 37°C, recombinant mutant K128A
0.00134
purified recombinant mitochondrial isozyme A, mutant V353E
0.0025
-
wild-type strain C600
0.00389
-
substrate L-serine, pH 7.5, 37°C, recombinant wild-type enzyme
0.00513
purified recombinant mitochondrial isozyme A, mutant G354A
0.0127
-
pH and temperature not specified in the publication
0.032
purified recombinant mitochondrial isozyme A, wild-type
0.715
25°C, pH 7.5, mutant enzyme V95R/D96P
1.067
25°C, pH 7.5, mutant enzyme M256I
1.1
25°C, pH 7.5, mutant enzyme R99T/T90R
1.22
25°C, pH 7.5, mutant enzyme R89S/T90L
1.44
25°C, pH 7.5, mutant enzyme V95G/D96G
1.47
25°C, pH 7.5, mutant enzyme V95L/D96P
1.6
25°C, pH 7.5, mutant enzyme R89P
1.68
25°C, pH 7.5, wild-type enzyme
1.9
25°C, pH 7.5, mutant enzyme R89H/T90V/P93A/A94T
10.66
purified recombinant His-tagged enzyme, pH 7.5, 37°C
14.7
-
recombinant protein
176.8
Vmax with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C
2.69
25°C, pH 7.5, mutant enzyme A94T
205
-
purified enzyme, pH 7.5
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
4.4
-
recombinant protein, crude extract from E. coli
41.39
Vmax with L-serine, 50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C
46
-
recombinant enzyme, crude extract
65.75
Vmax with L-serine, 50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C
70
-
purified recombinant enzyme
95.1
Vmax with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C
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
-
coupled assay system
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
-
-
additional information
-
at acetyl-CoA concentration 15fold higher than L-serine concentration, a nonproductive ternary complex of enzyme-CoA-L-serine is formed, kinetics
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
coupled assay system
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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
A0A3L6DLJ7
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
A0A3L6DLJ7
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
A0A3L6DLJ7
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
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
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
-
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
additional information
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
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 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
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homology model building and molecular docking of CysE, overview. Six residues (Asp29, Asp94, His95, Lys128, Arg129 and Asn148) of CysE are showed to be bound with L-Ser
additional information
homology modeling and identification of amino acids involved in the catalytic process. The conserved amino acid residues D67, H82 and H117 may be involved in the catalytic activity and, thus, the function of CysE
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
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additional information
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homology model building and molecular docking of CysE, overview. Six residues (Asp29, Asp94, His95, Lys128, Arg129 and Asn148) of CysE are showed to be bound with L-Ser
-
additional information
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homology modeling and identification of amino acids involved in the catalytic process. The conserved amino acid residues D67, H82 and H117 may be involved in the catalytic activity and, thus, the function of CysE
-
additional information
-
homology modeling and identification of amino acids involved in the catalytic process. The conserved amino acid residues D67, H82 and H117 may be involved in the catalytic activity and, thus, the function of CysE
-
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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biotechnology
5fold increase of O-acetylserine concentration and 26fold increase compared to controls of free cystein in transgenic developing narrow leaf lupin embryos (Lupinus angustifolius) without effect on free methionine levels in developing embryos or total cysteine and methionine concentrations in mature seeds
E282A
site-directed mutagenesis in C-terminal hexapeptide-repeat domain, enhanced activity, complementation of inactivated Escherichia coli mutant
G354A
site-directed mutagenesis in C-terminal hexapeptide-repeat domain, reduced activity, partial complementation of inactivated Escherichia coli mutant
H309A
site-directed mutagenesis in C-terminal hexapeptide-repeat domain, strongly reduced activity
H327A
site-directed mutagenesis in C-terminal hexapeptide-repeat domain, nearly no activity
E278L
-
site-directed mutagenesis, about 1.7fold more sensitive to inhibition by L-cysteine
F285Y
-
site-directed mutagenesis, about 1.7fold less sensitive to inhibition by L-cysteine
G277C
-
site-directed mutagenesis, about 27fold less sensitive to inhibition by L-cysteine
H282Q
-
site-directed mutagenesis, about 3.5fold less sensitive to inhibition by L-cysteine
M280I
-
site-directed mutagenesis, insensitive to inhibition by L-cysteine
S279T
-
site-directed mutagenesis, as sensitive to inhibition by L-cysteine as the wild-type
H208S
site-directed mutagenesis, a combination of comparative modeling, multiple molecular dynamics simulations and free energy calculation studies, the mutant shows a loss of cysteine inhibition by 64% compared to wild-type isozyme SAT1
S208H
naturally occuring polymorphism and site-directed mutagenesis, 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. The mutant shows a gain of cysteine inhibition by 36% and the IC50 of 3.5 mM, while the wild-type isozyme is almosst insensitive
A94T
activity is 160.2% of wild-type value, Ki for L-Cys is 5.7fold higher than wild-type value
del266T-273I
-
no complex formation with O-acetylserine sulfhydrylase A
del268E-273I
-
no complex formation with O-acetylserine sulfhydrylase A
del270G-273I
-
no complex formation with O-acetylserine sulfhydrylase A
delI273
-
no complex formation with O-acetylserine sulfhydrylase A
delI273I/delG272
-
no complex formation with O-acetylserine sulfhydrylase A
E166G/M201V
-
random PCR mutagenesis, cysE mutant, more insensitive to inhibition by L-cysteine than the wild-type, reduced enzyme activity
I273A
-
no complex formation with O-acetylserine sulfhydrylase A
I273E
-
no complex formation with O-acetylserine sulfhydrylase A
M201R
-
random PCR mutagenesis, cysE mutant, more insensitive to inhibition by L-cysteine than the wild-type, reduced enzyme activity
M201T
-
random PCR mutagenesis, cysE mutant, more insensitive to inhibition by L-cysteine than the wild-type, reduced enzyme activity
M256A
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random PCR mutagenesis, cysE mutant, more insensitive to inhibition by L-cysteine than the wild-type, reduced enzyme activity
M256I
Ki for L-Cys is 24fold higher than wild-type value
N51K/R91H/H233Y
-
random PCR mutagenesis, cysE mutant, more insensitive to inhibition by L-cysteine than the wild-type, reduced enzyme activity
P252R
-
random PCR mutagenesis, cysE mutant, more insensitive to inhibition by L-cysteine than the wild-type, reduced enzyme activity
R89H/T90V/P93A/A94T
activity is 113.1% of wild-type value, Ki for L-Cys is 658fold higher than wild-type value
R89P
activity is 95.2% of wild-type value, Ki for L-Cys is 700fold higher than wild-type value
R89S/T90L
activity is 72.6% of wild-type value, Ki for L-Cys is 25fold higher than wild-type value
R99T/T90R
activity is 65.5% of wild-type value, Ki for L-Cys is 7.5fold higher than wild-type value
S253L
-
random PCR mutagenesis, cysE mutant, more insensitive to inhibition by L-cysteine than the wild-type, reduced enzyme activity
T167K
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random PCR mutagenesis, cysE mutant, more insensitive to inhibition by L-cysteine than the wild-type, reduced enzyme activity
V95G/D96G
activity is 85.7% of wild-type value, Ki for L-Cys is 190fold higher than wild-type value
V95L/D96P
activity is 87.5% of wild-type value, Ki for L-Cys is 850fold higher than wild-type value
V95R/D96P
activity is 42.5% of wild-type value, Ki for L-Cys is 1583fold higher than wild-type value
D139N
Km (mM): 0.12 (acetyl-CoA), 160 (L-serine)
H154N
Km (mM): 0.21 (acetyl-CoA), 0.6 (L-serine)
H154N/H189N
Km (mM): 0.24 (acetyl-CoA), 27 (L-serine)
H189N
Km (mM): 32 (L-serine)
DELTA1-127
-
truncated variant of in which the first amino acids are deleted, systematically renders insoluble protein
DELTA1-67
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truncated variant of in which the first amino acids are deleted, systematically renders insoluble protein
D67A
site-directed mutagenesis, the mutant shows 9.79% activity compared to wild-type enzyme
H117A
site-directed mutagenesis, the mutant shows 20.82% activity compared to wild-type enzyme
H82A
site-directed mutagenesis, the mutant shows 14.31% activity compared to wild-type enzyme
D67A
-
site-directed mutagenesis, the mutant shows 9.79% activity compared to wild-type enzyme
-
H117A
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site-directed mutagenesis, the mutant shows 20.82% activity compared to wild-type enzyme
-
H82A
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site-directed mutagenesis, the mutant shows 14.31% activity compared to wild-type enzyme
-
D67A
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site-directed mutagenesis, the mutant shows 9.79% activity compared to wild-type enzyme
-
H117A
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site-directed mutagenesis, the mutant shows 20.82% activity compared to wild-type enzyme
-
H82A
-
site-directed mutagenesis, the mutant shows 14.31% activity compared to wild-type enzyme
-
D29A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
D94A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
H95A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
K128A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
N148A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
R129A
-
site-directed mutagenesis, soluble Asp29Ala fails to be expressed
D29A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
D94A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
K128A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
N148A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
R129A
-
site-directed mutagenesis, soluble Asp29Ala fails to be expressed
-
G52A
site-directed mutagenesis, no activity with L-serine, but with L-homoserine
G52A/P55G
site-directed mutagenesis, no activity with L-serine, but with L-homoserine
P55G
site-directed mutagenesis, increased activity with L-serine and with L-homoserine compared to the wild-type enzyme
G52A
-
site-directed mutagenesis, no activity with L-serine, but with L-homoserine
-
G52A/P55G
-
site-directed mutagenesis, no activity with L-serine, but with L-homoserine
-
P55G
-
site-directed mutagenesis, increased activity with L-serine and with L-homoserine compared to the wild-type enzyme
-
V353E
site-directed mutagenesis in C-terminal hexapeptide-repeat domain, nearly no activity
V353E
mutant enzyme does not bind O-acetylserine (thiol) lyase
V353E
strain BB1
V353E
mutant enzyme does not bind O-acetylserine (thiol) lyase
additional information
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SAT of transgenic Arabidopsis plants overexpressing the point-mutated watermelon gene are not inhibited by L-cysteine, regardless if the recombinant enzyme is targeted to the chloroplast or expressed in the cytosol
additional information
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transgenic Arabidopsis plants expressing recombinant wild-type SATase are inhibited by L-cysteine
additional information
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Sat3 expression is down-regulated by artificial micro RNA (amiRNA) expression against Sat3. Reduction of RNA levels, protein contents, SAT enzymatic activity and phenotype strongly correlate in independent amiSAT3 lines and cause significantly retarded growth. Expression of the other four Sat genes in Arabidopsis genome are not affected. Application of radiolabeled serine to leaf pieces reveales severely reduced incorporation rates into cysteine and even into glutathione. Steady-state levels of O-acetylserine are 4fold reduced
additional information
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single and multiple knockout mutants of all five Arabidopsis SERAT gene family members are analyzed: all five quadruple mutants with a single gene survived, with three mutants show dwarfism and the quintuple mutant lacking all SERAT genes is embryo-lethal. Thus, all five isoforms show functional redundancy in vivo
additional information
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the thermodynamics of formation of a complex of Arabidopsis thaliana O-acetylserine sulfhydrylase and the C-terminal ligand of AtSAT (C10 peptide) as a function of temperature and salt concentration using fluorescence spectroscopy and isothermal titration calorimetry is analysed. Results show that the C-terminus of AtSAT provides the major contribution to the total binding energy in the plant cysteine synthase complex. The C10 peptide binds to the O-acetylserine sulfhydrylase homodimer in a 2:1 complex. Interaction between AtOASS and the C10 peptide is tight (Kd: 5-100 nM) over a range of temperatures (10-35°C) and NaCl concentrations (0.02-1.3 M)
additional information
T-DNA insertion mutants lead to complete disruption of the respective enzyme genes, mutants for cytosolic (csat) and plastidic (psat) enzyme isoforms, and double mutants (dmsat) of the 2 isoforms by crossing
additional information
T-DNA insertion mutants lead to complete disruption of the respective enzyme genes, mutants for cytosolic (csat) and plastidic (psat) enzyme isoforms, and double mutants (dmsat) of the 2 isoforms by crossing
additional information
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T-DNA insertion mutants lead to complete disruption of the respective enzyme genes, mutants for cytosolic (csat) and plastidic (psat) enzyme isoforms, and double mutants (dmsat) of the 2 isoforms by crossing
additional information
the transgenic events in Zea mays leaves exhibit up to 12fold higher SAT activity without negative impact on growth. S-assimilation is increased in the leaves of SAT overexpressing plants, followed by higher levels of storage protein mRNA and storage proteins, particularly the 10-kDa D-zein, during endosperm development. This zein is known to impact the level of Met stored in kernels. The elite event with the highest expression of AtSAT1 shows 1.40fold increase in kernel Met
additional information
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the transgenic events in Zea mays leaves exhibit up to 12fold higher SAT activity without negative impact on growth. S-assimilation is increased in the leaves of SAT overexpressing plants, followed by higher levels of storage protein mRNA and storage proteins, particularly the 10-kDa D-zein, during endosperm development. This zein is known to impact the level of Met stored in kernels. The elite event with the highest expression of AtSAT1 shows 1.40fold increase in kernel Met
additional information
-
SAT of transgenic Arabidopsis plants overexpressing the point-mutated watermelon gene are not inhibited by L-cysteine, regardless if the recombinant enzyme is targeted to the chloroplast or expressed in the cytosol
additional information
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transgenic Arabidopsis plants expressing recombinant wild-type SATase are inhibited by L-cysteine
additional information
a mutant with a C terminus of EhSAT1 mutated to DWSI (4 amino acids changed) inhibits EhOASS efficiently
additional information
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a mutant with a C terminus of EhSAT1 mutated to DWSI (4 amino acids changed) inhibits EhOASS efficiently
additional information
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-
additional information
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-
additional information
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construction of deletion mutants lacking 10 to 25 amino acid residues at the C-terminal end, deletions alter the sensitivity against L-cysteine inhibition and the interaction with O-acetylserine (thiol) lyase, overview, DELTAC30 mutant is inactive
additional information
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e cysteine and cystine production level of mutants
additional information
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-
-
additional information
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-
-
additional information
generation of three deletion mutants of FgSAT, DELTAFgSAT-1, -2 and -18, using a gene replacement strategy. The three mutants show no recognizable phenotypic changes on potato dextrose agar medium, but exhibit a very weak growth on fructose gelatin agar medium containing sulfate as sole sulfur source. Supplementation of O-acetylserine, cysteine, or methionine, but not serine, rescues the defect of mycelial growth in FgSAT deletion mutants. The three mutants have a decrease in conidiation in mung bean liquid, but not in carboxymethyl cellulose. The mutant virulence, deoxynivalenol production and fungicide sensitivity is not altered compared to the wild-type. Real-time PCR assays detect an increase in expression levels of cysteine synthase (FgOAS), cystathionine gamma-synthase (FgCGS), cystathionine beta-lyase (FgCBL) genes involved in the alternative pathway in FgSAT deletion mutants, suggesting that the alternative pathway in Fusarium graminearum is present and can operate. Phenotype, overview
additional information
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generation of three deletion mutants of FgSAT, DELTAFgSAT-1, -2 and -18, using a gene replacement strategy. The three mutants show no recognizable phenotypic changes on potato dextrose agar medium, but exhibit a very weak growth on fructose gelatin agar medium containing sulfate as sole sulfur source. Supplementation of O-acetylserine, cysteine, or methionine, but not serine, rescues the defect of mycelial growth in FgSAT deletion mutants. The three mutants have a decrease in conidiation in mung bean liquid, but not in carboxymethyl cellulose. The mutant virulence, deoxynivalenol production and fungicide sensitivity is not altered compared to the wild-type. Real-time PCR assays detect an increase in expression levels of cysteine synthase (FgOAS), cystathionine gamma-synthase (FgCGS), cystathionine beta-lyase (FgCBL) genes involved in the alternative pathway in FgSAT deletion mutants, suggesting that the alternative pathway in Fusarium graminearum is present and can operate. Phenotype, overview
additional information
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generation of three deletion mutants of FgSAT, DELTAFgSAT-1, -2 and -18, using a gene replacement strategy. The three mutants show no recognizable phenotypic changes on potato dextrose agar medium, but exhibit a very weak growth on fructose gelatin agar medium containing sulfate as sole sulfur source. Supplementation of O-acetylserine, cysteine, or methionine, but not serine, rescues the defect of mycelial growth in FgSAT deletion mutants. The three mutants have a decrease in conidiation in mung bean liquid, but not in carboxymethyl cellulose. The mutant virulence, deoxynivalenol production and fungicide sensitivity is not altered compared to the wild-type. Real-time PCR assays detect an increase in expression levels of cysteine synthase (FgOAS), cystathionine gamma-synthase (FgCGS), cystathionine beta-lyase (FgCBL) genes involved in the alternative pathway in FgSAT deletion mutants, suggesting that the alternative pathway in Fusarium graminearum is present and can operate. Phenotype, overview
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additional information
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transgenic Ipomoea aquatica plants, which simultaneously express serine acetyltransferase and cysteine synthase are analyzed with respect to effect of cadmium on their physiological and biochemical features. Upon hydroponical cultivation in the presence of 200 microM cadmium for 7 days, two transgenic lines (SR1 and SR2) accumulated 2- to 4fold higher levels of cysteine and glutathione than the wild-type plants. Exposition to 100 microM cadmium for 30 days results in death or greatly retarded growth of wild-type and transgenic SR2 plant, whereas transgenic SR1 exhibited a 1.7fold increase in total biomass in comparison with the initial weight at day-0 of cadmium treatment
additional information
generation of a MSMEG_5947 knockout mutant strain through homologous recombination, the mutant strain grows slowlier than the wild-type strain, and the lack of the CysE protein causes drastic morphological changes, overview
additional information
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generation of a MSMEG_5947 knockout mutant strain through homologous recombination, the mutant strain grows slowlier than the wild-type strain, and the lack of the CysE protein causes drastic morphological changes, overview
additional information
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generation of a MSMEG_5947 knockout mutant strain through homologous recombination, the mutant strain grows slowlier than the wild-type strain, and the lack of the CysE protein causes drastic morphological changes, overview
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additional information
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transformation via Agrobacterium tumefaciens, transgenic Nicotiana tabacum plants overexpressing recombinant Arabidopsis thaliana SAT A isozyme, expression with and without mitochondrial transit peptide
additional information
transformation via Agrobacterium tumefaciens, transgenic Nicotiana tabacum plants overexpressing recombinant Arabidopsis thaliana SAT A isozyme, expression with and without mitochondrial transit peptide
additional information
transformation via Agrobacterium tumefaciens, transgenic Nicotiana tabacum plants overexpressing recombinant Arabidopsis thaliana SAT A isozyme, expression with and without mitochondrial transit peptide
additional information
transformation via Agrobacterium tumefaciens, transgenic Nicotiana tabacum plants overexpressing recombinant Arabidopsis thaliana SAT A isozyme, expression with and without mitochondrial transit peptide
additional information
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CysE mutants show strongly reduced enzyme activity
additional information
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construction of transgenic plants by introduction of Escherichia coli cysE gene, targeted into the chloroplasts by fusing a signal sequence of rubisco from Arabidopsis thaliana, crude Solanum tuberosum leaf extract show 20fold higher enzyme activity
additional information
A0A3L6DLJ7
overexpression of Arabidopsis thaliana AtSAT1 in maize under control of the leaf bundle sheath cell-specific rbcS1 promoter to determine the impact on seed storage protein expression. The transgenic events exhibit up to 12fold higher SAT activity without negative impact on growth. S-assimilation is increased in the leaves of SAT overexpressing plants, followed by higher levels of storage protein mRNA and storage proteins, particularly the 10-kDa D-zein, during endosperm development. This zein is known to impact the level of Met stored in kernels. The elite event with the highest expression of AtSAT1 shows 1.40fold increase in kernel Met. Efficacy of increasing maize nutritional value by SAT overexpression without apparent yield loss. Maternal overexpression of SAT in vegetative tissues is necessary for high-Met zein accumulation. Moreover, SAT overcomes the shortage of S-amino acids that limits the expression and accumulation of high-Met zeins during kernel development. Mature kernels of AtSAT1 overexpressing maize show changes in zein expression profile. The measured enzyme activity is a combination of endogenous SAT and that derived from expression of AtSAT1
additional information
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overexpression of Arabidopsis thaliana AtSAT1 in maize under control of the leaf bundle sheath cell-specific rbcS1 promoter to determine the impact on seed storage protein expression. The transgenic events exhibit up to 12fold higher SAT activity without negative impact on growth. S-assimilation is increased in the leaves of SAT overexpressing plants, followed by higher levels of storage protein mRNA and storage proteins, particularly the 10-kDa D-zein, during endosperm development. This zein is known to impact the level of Met stored in kernels. The elite event with the highest expression of AtSAT1 shows 1.40fold increase in kernel Met. Efficacy of increasing maize nutritional value by SAT overexpression without apparent yield loss. Maternal overexpression of SAT in vegetative tissues is necessary for high-Met zein accumulation. Moreover, SAT overcomes the shortage of S-amino acids that limits the expression and accumulation of high-Met zeins during kernel development. Mature kernels of AtSAT1 overexpressing maize show changes in zein expression profile. The measured enzyme activity is a combination of endogenous SAT and that derived from expression of AtSAT1
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C-terminal deletion mutants, expression in Escherichia coli strain JM70
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cloning and DNA sequencing of 3 isozymes, complementation of Cys- mutant Escherichia coli strain JM39 with the 3 isozymes, sequence analysis of cytosolic isozyme
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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
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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
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expressed as a His-tagged fusion protein
-
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 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 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
-
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 mutant enzymes in Escherichia coli
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
expression of wild-type and mutants in Escherichia coli
expression of wild-type and mutants in Escherichia coli SAT inactivated mutant as S-tagged protein
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 cysE or SP_0589, recombinant expression of His-tagged enzyme in Escherichia coli strain codon optimized strain BL21(DE3)-RIL
gene cysE, recombinant expression of C-terminally His-tagged in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain NovaBlue using vector pET29b
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gene cysE, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene cysE, recombinant overexpression of Arabidopsis thaliana AtSAT1 in Zea mays leaves lines OE1 and OE3 under control of the leaf bundle sheath cell-specific rbcS1 promoter resulting in 12fold higher SAT activity, increased S-assimilation in the leaves, and higher levels of storage protein mRNA and storage proteins, particularly the 10-kDa D-zein, during endosperm development. Quantitative RT-PCR expression analysis, the measured enzyme activity is a combination of endogenous SAT and that derived from expression of AtSAT1
gene CysE, sequence comparisons, recombinant expression of wild-type and mutant C-terminally His-tagged enzymes 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
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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
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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
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
-
overexpression of 3 isozymes SAT-m, SAT-p, SAT-c in Escherichia coli BL21 (DE3)
-
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)
SAT1 is closely linked to SAT5, high DNA sequence homology
-
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expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
expression of wild-type and mutants in Escherichia coli
-
expression of wild-type and mutants in Escherichia coli
-
overexpression in Escherichia coli
-
overexpression in Escherichia coli
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Burnell, J.N.; Whatley, F.R.
Sulphur metabolism in Paracoccus denitrificans. Purification, properties and regulation of serine transacetylase, O-acetylserine sulphydrylase and beta-cystathionase
Biochim. Biophys. Acta
481
246-265
1977
Paracoccus denitrificans, Paracoccus denitrificans 8944
brenda
Kredich, N.M.; Tomkins, G.M.
The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium
J. Biol. Chem.
241
4955-4965
1966
Escherichia coli, Escherichia coli B / ATCC 11303, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Smith, I.K.; Thompson, J.F.
Purification and characterization of L-serine transacetylase and O-acetyl-L-serine sulfhydrylase from kidney bean seedlings (Phaseolus vulgaris)
Biochim. Biophys. Acta
227
288-295
1971
Phaseolus vulgaris
brenda
Smith, I.K.
Studies of L-cysteine biosynthetic enzymes in Phaseolus vulgaris L.
Plant Physiol.
50
477-479
1972
Phaseolus vulgaris
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