2.3.1.30: serine O-acetyltransferase
This is an abbreviated version!
For detailed information about serine O-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.30
-
2.3.1.30
-
o-acetylserine
-
sulfur
-
l-cysteine
-
sulfhydrylase
-
o-acetyl-l-serine
-
foot-and-mouth
-
desulfhydrase
-
oas-tls
-
o-acetylserinethiollyase
-
assimilatory
-
slc26a1
-
nasi-1
-
thlaspi
-
bienzyme
-
phytochelatins
-
molecular biology
-
agriculture
-
drug development
-
medicine
- 2.3.1.30
- o-acetylserine
- sulfur
- l-cysteine
-
sulfhydrylase
- o-acetyl-l-serine
- foot-and-mouth
- desulfhydrase
- oas-tls
-
o-acetylserinethiollyase
-
assimilatory
-
slc26a1
-
nasi-1
- thlaspi
-
bienzyme
- phytochelatins
- molecular biology
- agriculture
- drug development
- medicine
Reaction
Synonyms
acetyltransferase, serine, AtOASS, AtSAT, AtSAT1, AtSerat 2;1, BvSAT, CysE, cytosolic serine acetyltransferase, DcsE, EhSAT1, EhSAT2, EhSAT3, GmSerat2,1, HISAT, Kpn CysE, L-serine acetyltransferase, L-serine O-acetyltransferase, L-serineO-acetyltransferase, More, plastidic serine acetyltransferase, SAT, SAT isoform 1, SAT-1, SAT1, SAT2, SAT3, SATase, SERAT, Serat1,1, SERAT1.1, Serat2,1, Serat2,2, SERAT2.1, Serat3,1, Serat3,2, serine acetlytransferase, serine acetyltransferase, serine acetyltransferase 1, serine acetyltransferase 2,1, serine O-acetyltransferase, serine O-acetyltransferase 1, serine transacetylase, Spn cysE, SP_0589
ECTree
2.3.1.30 serine O-acetyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.3.1.30 - serine O-acetyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
V353E
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
E166G/M201V
-
random PCR mutagenesis, cysE mutant, more insensitive to inhibition by L-cysteine than the wild-type, reduced enzyme activity
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
-
random PCR mutagenesis, cysE mutant, more insensitive to inhibition by L-cysteine than the wild-type, reduced enzyme activity
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
-
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
DELTA1-127
-
truncated variant of in which the first amino acids are deleted, systematically renders insoluble protein
DELTA1-67
-
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
-
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
-
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
-
V353E
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
Staphylococcus aureus ATCC 33591
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
D94A
Staphylococcus aureus ATCC 33591
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
K128A
Staphylococcus aureus ATCC 33591
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
N148A
Staphylococcus aureus ATCC 33591
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
R129A
Staphylococcus aureus ATCC 33591
-
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
-
additional information
V353E
site-directed mutagenesis in C-terminal hexapeptide-repeat domain, nearly no activity
V353E
mutant enzyme does not bind O-acetylserine (thiol) lyase
V353E
mutant enzyme does not bind O-acetylserine (thiol) lyase
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
-
transgenic Arabidopsis plants expressing recombinant wild-type SATase are inhibited by L-cysteine
additional information
-
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
-
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
-
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
-
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
-
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
-
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
-
a mutant with a C terminus of EhSAT1 mutated to DWSI (4 amino acids changed) inhibits EhOASS efficiently
additional information
-
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
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
-
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
-
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
-
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
-
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
-
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
-
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
-
CysE mutants show strongly reduced enzyme activity
additional information
-
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
-
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
