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Information on EC 2.3.1.30 - serine O-acetyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q42588

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.30 serine O-acetyltransferase
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q42588 not found.
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
serine acetyltransferase, sat-1, satase, hisat, serat, serine transacetylase, serine o-acetyltransferase, ehsat1, atsat1, l-serine o-acetyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
plastidic serine acetyltransferase
-
serine acetlytransferase
-
serine acetyltransferase
-
serine acetyltransferase 1
-
acetyltransferase, serine
-
-
-
-
cytosolic serine acetyltransferase
-
L-serine acetyltransferase
-
-
-
-
SATase
Serat1,1
Serat2,2
Serat3,1
Serat3,2
serine acetyltransferase
serine O-acetyltransferase
-
-
serine transacetylase
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
show the reaction diagram
a C-terminal hexapeptide-repeat domain is common for Arabidopsis thaliana isoforms and several other enzyme DNA sequences, it has a catalytic bifunctionality as serine acetyltransferase and in interaction with O-acetylserine (thiol) lyase and is involved in cysteine biosynthesis regulation, computational modeling
acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
show the reaction diagram
a C-terminal hexapeptide-repeat domain is common for Arabidopsis thaliana isoforms and several other enzyme DNA sequences, it has a catalytic bifunctionality as serine acetyltransferase and in interaction with O-acetylserine (thiol) lyase and is involved in cysteine biosynthesis regulation, computational modeling
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:L-serine O-acetyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9023-16-9
-
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-serine
CoA + O-acetyl-L-serine
show the reaction diagram
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
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
show the reaction diagram
L-serine + acetyl-CoA
O-acetylserine + CoA
show the reaction diagram
no major contribution to total cysteine biosynthesis
-
-
?
additional information
?
-
-
cysteine synthase is a bienzyme complex build of serine acetyltransferase and O-acetylserine (thiol) lyase, no channeling of substrate within the complex
-
-
?
NATURAL SUBSTRATE
NATURAL 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-serine
CoA + O-acetyl-L-serine
show the reaction diagram
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
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
show the reaction diagram
L-serine + acetyl-CoA
O-acetylserine + CoA
show the reaction diagram
no major contribution to total cysteine biosynthesis
-
-
?
additional information
?
-
-
cysteine synthase is a bienzyme complex build of serine acetyltransferase and O-acetylserine (thiol) lyase, no channeling of substrate within the complex
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
4 mol per mol of cysteine synthase complex
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
feedback inhibition
cysteine
feedback inhibition
L-cysteine
additional information
-
isoform Serat3,1 is insensitive to feedback inhibition by L-Cys
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 45.1
acetyl-CoA
0.59 - 121.4
L-serine
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025 - 0.0173
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
0.00513
purified recombinant mitochondrial isozyme A, mutant G354A
0.032
purified recombinant mitochondrial isozyme A, wild-type
4.4
-
recombinant protein, crude extract from E. coli
70
-
purified recombinant enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
AtSAT1 protein lacks a transit peptide
Manually annotated by BRENDA team
compartment with largest serine acetyltransferase activity of total serine acetyltransferase activity independent of plastidic serine acetyltransferase
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
serine acetyltransferase (SAT) is a key control point for S-assimilation leading to Cys and Met biosynthesis
metabolism
rate-limiting step in the cysteine biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SAT1_ARATH
314
0
34251
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2000000
-
enzyme aggregate, gel filtration
300000
-
cysteine synthase bienzyme complex, gel filtration
34000
-
2 * 34000, serine acetyltransferase + 2 * 36000, O-acetylserine (thiol) lyase, forming the cysteine synthase complex, SDS-PAGE
36000
-
2 * 34000, serine acetyltransferase + 2 * 36000, O-acetylserine (thiol) lyase, forming the cysteine synthase complex, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 32000-35000, SDS-PAGE
?
-
x * 33000-36500, 3 recombinant isozymes, SDS-PAGE
tetramer
-
2 * 34000, serine acetyltransferase + 2 * 36000, O-acetylserine (thiol) lyase, forming the cysteine synthase complex, SDS-PAGE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
frozen plant material is homogenized in extraction buffer (50 mM HEPES/KOH, pH 7.4) and centrifuged, supernatant desalted and used for enzyme assays
protein extraction from frozen, homogenized embryos
frozen plant material is homogenized in extraction buffer (50 mM HEPES/KOH, pH 7.4) and centrifuged, supernatant desalted and used for enzyme assays
partially, recombinant isozymes SAT-p, SAT-m, and SAT-c from E. coli
-
recombinant from E. coli
-
recombinant wild-type and mutants as S-tagged protein from E. coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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
cotyledon segments of seedlings of Ipomaea aquatica are transformed with Arabidopsis serine acetyltransferase and rice cysteine synthase genes under the control of the cauliflower mosaic virus 35S promoter. Simultaneous expression of serine acetyltransferase and cysteine synthase results in enhanced sulfate uptake and increased biomass in Ipomaea aquatica
-
expression in Escherichia coli
-
expression in Escherichia coli SAT inactivated mutant
expression of 3 isozymes SAT-m, SAT-p, SAT-c as GFP-fusion proteins in Arabidopsis thaliana
-
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
overexpression in Escherichia coli
-
overexpression of 3 isozymes SAT-m, SAT-p, SAT-c in Escherichia coli BL21 (DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
T-DNA insertion mutants lead to complete expression disruption of the respective enzyme genes and decreases in O-acetyl serine and cysteine contents in leaves and roots (double mutant), a significant gamma-glutamylcysteine decrease in double mutant leaves, and sulfide reduction in plastidic enzyme mutant leaves
T-DNA insertion mutants lead to complete expression disruption of the respective enzyme genes and decreases in O-acetyl serine and cysteine contents in leaves and roots (cytosolic enzyme and double mutant), a significant gamma-glutamylcysteine decrease in double mutant leaves and cytosolic enzyme mutant roots, a reduction of glutathione content in cytosolic enzyme mutant roots, and sulfate reduction in cytosolic enzyme mutant leaves
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
-
results show that mitochondria provide the bulk of OAS in the plant cell and are the likely site of flux regulation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Murillo, M.; Fogilia, R.; Diller, A.; Lee, S.; Leustek, T.
Serine acetyltransferase from Arabidopsis thaliana can functionally complement the cysteine requirement of a cysE mutant strain of Escherichia coli
Cell. Mol. Biol. Res.
41
425-433
1996
Escherichia coli (P0A9D4), Escherichia coli, Arabidopsis thaliana (Q39218), Arabidopsis thaliana (Q42588), Arabidopsis thaliana
Manually annotated by BRENDA team
Noji, M.; Inoue, K.; Kimura, N.; Gouda, A.; Saito, K.
Isoform-dependent differences in feedback regulation and subcellular localization of serine acetyltransferase involved in cysteine biosynthesis from Arabidopsis thaliana
J. Biol. Chem.
273
32739-32745
1998
Arabidopsis thaliana
Manually annotated by BRENDA team
Droux, M.; Ruffet, M.L.; Douce, R.; Job, D.
Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants. Structural and kinetic properties of the free and bound enzymes
Eur. J. Biochem.
255
235-245
1998
Arabidopsis thaliana
Manually annotated by BRENDA team
Inoue, K.; Noji, M.; Saito, K.
Determination of the sites required for the allosteric inhibition of serine acetyltransferase by L-cysteine in plants
Eur. J. Biochem.
266
220-227
1999
Arabidopsis thaliana, Citrullus lanatus subsp. vulgaris
Manually annotated by BRENDA team
Wirtz, M.; Berkowitz, O.; Droux, M.; Hell, R.
The cysteine synthase complex from plants: mitochondrial serine acetyltransferase from Arabidopsis thaliana carries a bifunctional domain for catalysis and protein-protein interaction
Eur. J. Biochem.
268
686-693
2001
Arabidopsis thaliana (Q39218), Arabidopsis thaliana (Q42538), Arabidopsis thaliana (Q42588), Arabidopsis thaliana, Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium (P29847)
Manually annotated by BRENDA team
Noji, M.; Saito, K.
Molecular and biochemical analysis of serine acetyltransferase and cysteine synthase towards sulfur metabolic engineering in plants
Amino Acids
22
231-243
2002
Allium tuberosum, Arabidopsis thaliana, Citrullus lanatus subsp. vulgaris, Spinacia oleracea
Manually annotated by BRENDA team
Wirtz, M.; Hell, R.
Production of cysteine for bacterial and plant biotechnology: Application of cysteine feedback-insensitive isoforms of serine acetyltransferase
Amino Acids
24
195-203
2003
Arabidopsis thaliana (Q39218), Arabidopsis thaliana (Q42538), Arabidopsis thaliana (Q42588), Arabidopsis thaliana, Escherichia coli, Escherichia coli C600, Nicotiana tabacum, Nicotiana tabacum (Q8H0P5), Nicotiana tabacum (Q8H0P6), Nicotiana tabacum (Q8H0P7)
Manually annotated by BRENDA team
Kawashima, C.G.; Berkowitz, O.; Hell, R.; Noji, M.; Saito, K.
Characterization and expression analysis of a serine acetyltransferase gene family involved in a key step of the sulfur assimilation pathway in Arabidopsis
Plant Physiol.
137
220-230
2005
Arabidopsis thaliana
Manually annotated by BRENDA team
Noji, M.; Goulart Kawashima, C.; Obayashi, T.; Saito, K.
In silico assessment of gene function involved in cysteine biosynthesis in Arabidopsis: expression analysis of multiple isoforms of serine acetyltransferase
Amino Acids
30
163-171
2006
Arabidopsis thaliana (Q39218), Arabidopsis thaliana (Q42538), Arabidopsis thaliana (Q42588), Arabidopsis thaliana (Q8S895), Arabidopsis thaliana (Q8W2B8), Arabidopsis thaliana
Manually annotated by BRENDA team
Kumaran, S.; Jez, J.M.
Thermodynamics of the interaction between O-acetylserine sulfhydrylase and the C-terminus of serine acetyltransferase
Biochemistry
46
5586-5594
2007
Arabidopsis thaliana
Manually annotated by BRENDA team
Meerak, J.; Akaracharanya, A.; Leepipatpiboon, N.; Chadchawan, S.; Kaothien-Nakayama, P.; Shinmyo, A.; Sano, H.
Simultaneous expression of serine acetyltransferase and cysteine synthase results in enhanced sulfate uptake and increased biomass in Ipomaea aquatica
Plant Biotechnol.
23
185-189
2006
Arabidopsis thaliana
-
Manually annotated by BRENDA team
Francois, J.A.; Kumaran, S.; Jez, J.M.
Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex
Plant Cell
18
3647-3655
2006
Arabidopsis thaliana
Manually annotated by BRENDA team
Watanabe, M.; Mochida, K.; Kato, T.; Tabata, S.; Yoshimoto, N.; Noji, M.; Saito, K.
Comparative Genomics and Reverse Genetics Analysis Reveal Indispensable Functions of the Serine Acetyltransferase Gene Family in Arabidopsis
Plant Cell
20
2484-2496
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Haas, F.H.; Heeg, C.; Queiroz, R.; Bauer, A.; Wirtz, M.; Hell, R.
Mitochondrial serine acetyltransferase functions as pacemaker of cysteine synthesis in plant cells
Plant Physiol.
148
1055-1067
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Tabe, L.; Wirtz, M.; Molvig, L.; Droux, M.; Hell, R.
Overexpression of serine acetlytransferase produced large increases in O-acetylserine and free cysteine in developing seeds of a grain legume
J. Exp. Bot.
61
721-733
2010
Arabidopsis thaliana (Q42588), Arabidopsis thaliana
Manually annotated by BRENDA team
Krueger, S.; Niehl, A.; Lopez Martin, M.C.; Steinhauser, D.; Donath, A.; Hildebrandt, T.; Romero, L.C.; Hoefgen, R.; Gotor, C.; Hesse, H.
Analysis of cytosolic and plastidic serine acetyltransferase mutants and subcellular metabolite distributions suggests interplay of the cellular compartments for cysteine biosynthesis in Arabidopsis
Plant Cell Environ.
32
349-367
2009
Arabidopsis thaliana (Q42538), Arabidopsis thaliana (Q42588), Arabidopsis thaliana
Manually annotated by BRENDA team
Xiang, X.; Wu, Y.; Planta, J.; Messing, J.; Leustek, T.
Overexpression of serine acetyltransferase in maize leaves increases seed-specific methionine-rich zeins
Plant Biotechnol. J.
16
1057-1067
2018
Zea mays (A0A3L6DLJ7), Zea mays, Arabidopsis thaliana (Q42588), Arabidopsis thaliana
Manually annotated by BRENDA team