Information on EC 2.3.1.30 - serine O-acetyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.3.1.30
-
RECOMMENDED NAME
GeneOntology No.
serine O-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Cysteine and methionine metabolism
-
-
D-cycloserine biosynthesis
-
-
L-cysteine biosynthesis I
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
seleno-amino acid biosynthesis
-
-
Sulfur metabolism
-
-
cysteine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:L-serine O-acetyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9023-16-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
Chinese chive
-
-
Manually annotated by BRENDA team
allelic gene cysA1 and cysA103
O13389
SwissProt
Manually annotated by BRENDA team
cv. Dita
-
-
Manually annotated by BRENDA team
gene CysE
UniProt
Manually annotated by BRENDA team
gene CysE
UniProt
Manually annotated by BRENDA team
chloroplast isoform, constitutive gene cmSAT; red alga
-
-
Manually annotated by BRENDA team
strain HMM1:IMSS trophozoites
UniProt
Manually annotated by BRENDA team
strain C600, CysE gene
-
-
Manually annotated by BRENDA team
gene FGSG_00186
UniProt
Manually annotated by BRENDA team
gene FGSG_00186
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene cysE or LSEI 0479
UniProt
Manually annotated by BRENDA team
gene cysE or LSEI 0479
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
mouse cell line
-
-
Manually annotated by BRENDA team
gene cysE or MSMEG_5947
UniProt
Manually annotated by BRENDA team
gene cysE or MSMEG_5947
UniProt
Manually annotated by BRENDA team
gene Rv2335 or cysE
UniProt
Manually annotated by BRENDA team
gene Rv2335 or cysE
UniProt
Manually annotated by BRENDA team
strain 8944
-
-
Manually annotated by BRENDA team
strain 8944
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene dcsE; gene dcsE
UniProt
Manually annotated by BRENDA team
gene dcsE; gene dcsE
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + L-Ser
CoA + O-acetyl-L-Ser
show the reaction diagram
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
show the reaction diagram
acetyl-CoA + L-threonine
CoA + O-acetyl-L-threonine
show the reaction diagram
L-serine + acetyl-CoA
O-acetyl serine + CoA
show the reaction diagram
-
subsequently, cysteine synthase forms L-cysteine from O-acetyl serine
-
?
L-serine + acetyl-CoA
O-acetyl-L-serine + CoA
show the reaction diagram
L-serine + acetyl-CoA
O-acetylserine + CoA
show the reaction diagram
no major contribution to total cysteine biosynthesis
-
-
?
propionyl-CoA + L-serine
CoA + O-propionyl-L-serine
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + L-Ser
CoA + O-acetyl-L-Ser
show the reaction diagram
Q6F4D7
key enzyme in L-cysteine biosynthesis
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
show the reaction diagram
L-serine + acetyl-CoA
O-acetyl serine + CoA
show the reaction diagram
Q401L4, Q401L5
-
subsequently, cysteine synthase forms L-cysteine from O-acetyl serine
-
?
L-serine + acetyl-CoA
O-acetyl-L-serine + CoA
show the reaction diagram
L-serine + acetyl-CoA
O-acetylserine + CoA
show the reaction diagram
Q42538, Q42588
no major contribution to total cysteine biosynthesis
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
4 mol per mol of cysteine synthase complex
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
0.1 mM, 31.7fold activation
Fe2+
enzyme contains Zn2+ and Fe2+
Ni2+
0.1 mM, 12fold activation
Zn2+
enzyme contains Zn2+ and Fe2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
-
ATP
-
mixed non-competitive with respect to serine
cysteine
D-Cysteine
EDTA
1.0 mM, complete inhibition
glutathione
-
weak, allosteric inhibition
glycine
hydroxylamine
iodoacetamide
-
-
L-alanine
-
noncompetitive against acetyl-CoA
L-cysteic acid
-
-
L-cysteine
L-cystine
-
allosteric inhibition
L-homocysteine
L-homoserine
L-methionine
L-Ser
-
-
L-serine
N-acetyl-L-cysteine
N-acetyl-L-serine
0.5 mM, weak inhibition
N-ethylmaleimide
-
-
O-acetyl-L-serine
oxidized glutathione
0.5 mM, weak inhibition
p-chloromercuribenzoate
reduced glutathione
0.5 mM weak inhibition; 0.5 mM, weak inhibition
S-methyl-L-cysteine
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011 - 45.1
acetyl-CoA
2.27
L-Ser
-
pH 8.0
0.013 - 160
L-serine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.068 - 200
acetyl-CoA
0.48 - 43.83
L-serine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.32 - 1.23
L-serine
95
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.042
3-oxo-2-phenyl-3,5-dihydro-2H-pyrazolo[3,4-d]thieno[2,3-b]pyridine-7-carboxylic acid
-
72 micromol, 0.1 M Tris-HCl, pH 7.5, room temperature
0.064
CoA
-
versus acetyl-CoA
0.0006 - 0.95
L-Cys
0.0025 - 0.46
L-cysteine
0.0076 - 0.0112
L-Ser
additional information
additional information
-
overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
0.0031 - 3.5
L-cysteine
additional information
L-cysteine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00036
purified recombinant mitochondrial isozyme A, mutant H327A
0.00134
purified recombinant mitochondrial isozyme A, mutant V353E
0.0025
-
wild-type strain C600
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
-
25C, pH 7.5, mutant enzyme V95R/D96P
1.067
-
25C, pH 7.5, mutant enzyme M256I
1.1
-
25C, pH 7.5, mutant enzyme R99T/T90R
1.22
-
25C, pH 7.5, mutant enzyme R89S/T90L
1.44
-
25C, pH 7.5, mutant enzyme V95G/D96G
1.47
-
25C, pH 7.5, mutant enzyme V95L/D96P
1.6
-
25C, pH 7.5, mutant enzyme R89P
1.68
-
25C, pH 7.5, wild-type enzyme
1.9
-
25C, pH 7.5, mutant enzyme R89H/T90V/P93A/A94T
2.69
-
25C, pH 7.5, mutant enzyme A94T
4.4
-
recombinant protein, crude extract from E. coli
10.66
purified recombinant His-tagged enzyme, pH 7.5, 37C
14.7
-
recombinant protein
23.42
Vmax with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25C
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, 25C
41.39
Vmax with L-serine, 50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25C
46
-
recombinant enzyme, crude extract
65.75
Vmax with L-serine, 50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25C
70
-
purified recombinant enzyme
95.1
Vmax with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25C
176.8
Vmax with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25C
205
-
purified enzyme, pH 7.5
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
50% of maximal activity at pH 5.0 and pH 10.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
50% of maximal activity at 20C and 80C
45 - 80
45C: about 50% of maximal activity, 80C: about 55% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
predicted from sequence
5.99
predicted from sequence
6.52
-
calculation from nucleotide sequence
6.63
predicted from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
SATase isoform genes, Serat1,1 is highly expressed both in root and in dark-grown plant
Manually annotated by BRENDA team
-
low-abundance enzyme
Manually annotated by BRENDA team
-
C-1008 cell line
Manually annotated by BRENDA team
additional information
-
accumulation in etiolated plants
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24600
x * 30000, recombinant His-tagged enzyme, SDS-PAGE, x * 24600, about, sequence calculation
26200
x * 26200, recombinant His-tagged enzyme, SDS-PAGE
29261
-
4 * 29261, ultracentrifugation, gel filtration, crystallographic data
30000
x * 30000, recombinant His-tagged enzyme, SDS-PAGE, x * 24600, about, sequence calculation
31000
-
x * 31000, recombinant enzyme, SDS-PAGE
32000
x * 32000 recombinant enzyme, SDS-PAGE
34000
-
2 * 34000, serine acetyltransferase + 2 * 36000, O-acetylserine (thiol) lyase, forming the cysteine synthase complex, SDS-PAGE
34330
-
x * 34330, cytosolic isozyme, amino acid sequence determination
34400
calculated from sequence, 305 amino acids
34800
calculated from sequence, 311 amino acids
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
37700
calculated from sequence, 336 amino acids
38400
-
x * 38400, amino acid sequence determination
40000
SDS-PAGE, recombinant purified enzyme monomer with 2.6 kDa histidine tag
42500
x * 42500, calculated from sequence
43737
-
x * 43737, native enzyme, amino acid sequence determination
45000
-
SDS-PAGE
83000
trimeric enzyme, gel filtration
125000
-
ultracentrifugation experiments
145000
-
gel filtration
160000
-
gel filtration
181000
hexameric enzyme, gel filtration and dynamic light scattering
294600
x * 294600, sequence calculation
300000
-
cysteine synthase bienzyme complex, gel filtration
323400
x * 323400, sequence calculation
323800
x * 323800, sequence calculation
350000
-
gel filtration
450000 - 500000
-
multienzyme complex of L-serine acetyltransferase and L-cysteine synthase, gel filtration
2000000
-
enzyme aggregate, gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
monomer
; 1 * 34400, SDS-PAGE; 1 * 34800, SDS-PAGE
tetramer
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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, 16C, 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
crystal structure of the enzyme with its inhibitor L-cysteine
-
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, 1% 2-methyl-2,3-pentanediol, 0.5 M sodium thiocyanate, 5.5 mM cysteine, and SeMet SAT (10 mg/ml) sitting drops, at 20C 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, 20C, 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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
-
SAT DELTAC10 mutant, lacking 10 amino acid residues at the C-terminal end is inactivated after 12 h
50
-
half-life: 25 min
60
-
half-life: 2 min
80
-
5 min, 50% loss of activity
90
-
5 min, complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 1 week, stable
-
-30C or -80C, 50 mM Tris-HCl, pH 8.0, 10-20% glycerol in small aliquots, fully active after more than 3 months
-
20C, 0.4 M NaCl, 2 weeks, stable
-
2C, 50% loss of activity after 1 week
-
4C, the purified recombinant wild-type and mutant isozyme EhSAT1 proteins are stable over long storage
4C, the purified recombinant wild-type and mutant isozyme EhSAT3 proteins are unstable due to protein aggregation over long storage
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
partially, 3 isozymes
-
partially, recombinant isozymes SAT-p, SAT-m, and SAT-c from E. coli
-
protein extraction from frozen, homogenized embryos
-
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 -80C; 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 -80C; 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 -80C
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 protein from E. coli
-
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
recombinant wild-type and mutants from E. coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
C-terminal deletion mutants, expression in Escherichia coli strain JM70
-
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
-
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 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
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 mutant ezymes 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; 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
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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; 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
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overexpression in Escherichia coli
overexpression in Escherichia coli, construction of an expression vector which increases the expression to 17% of the soluble cell protein
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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)
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recombinant expression
EXPRESSION
ORGANISM
UNIPROT
LITERATURE