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Information on EC 2.3.1.30 - serine O-acetyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A9D4

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     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:
Escherichia coli
UNIPROT: P0A9D4 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
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
serine acetyltransferase
-
acetyltransferase, serine
-
-
-
-
L-serine acetyltransferase
-
-
-
-
SATase
-
-
-
-
serine acetyltransferase
-
-
-
-
serine transacetylase
-
-
-
-
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
-
-
-
-
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
-
-
-
?
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
propionyl-CoA + L-serine
CoA + O-propionyl-L-serine
show the reaction diagram
-
-
-
-
?
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
first step of L-cysteine synthesis
-
-
?
L-serine + acetyl-CoA
O-acetyl-L-serine + CoA
show the reaction diagram
-
-
-
?
acetyl-CoA + L-serine
CoA + O-acetyl-L-serine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
salt concentrations less than 0.02 M or greater than 0.2 M appreciably decrease reaction rate
INHIBITOR
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
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
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
cysteine
competitive, binds at the serine substrate site, negatively regulates its own synthesis
ATP
-
mixed non-competitive with respect to serine
cysteine
-
competitive versus acetyl-CoA, mixed non-competitive with respect to serine
glycine
L-alanine
-
noncompetitive against acetyl-CoA
L-cysteic acid
-
-
L-serine
-
above 3 mM, weak
N-acetyl-L-cysteine
-
-
additional information
-
no inhibition by N-acetylserine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.56
acetyl-CoA
-
-
0.11
L-serine
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.068
acetyl-CoA
-
acetyl-CoA hydrolysis
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
0.0006 - 0.95
L-Cys
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.072
3-oxo-2-phenyl-3,5-dihydro-2H-pyrazolo[3,4-d]thieno[2,3-b]pyridine-7-carboxylic acid
Escherichia coli
72 micromol, 0.1 M Tris-HCl, pH 7.5, room temperature
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
2.69
25°C, pH 7.5, mutant enzyme A94T
0.0025
-
wild-type strain C600
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
7.6 - 7.8
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
compounds that (partially) block the Escherichia coli enzyme activity block the growth of Entamoeba histolytica trophozoites but not mammalian cells
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
125000
-
ultracentrifugation experiments
145000
-
gel filtration
160000
-
gel filtration
29261
-
4 * 29261, ultracentrifugation, gel filtration, crystallographic data
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 32000-35000, SDS-PAGE
tetramer
-
4 * 29261, ultracentrifugation, gel filtration, crystallographic data
additional information
-
cysteine synthase from Escherichia coli is a bienzyme complex comprised of serine acetyltransferase and O-acetylserine sulfhydrylase A. The C-terminus of SAT, Ile273, along with Glu268 and Asp271, is essential for complex formation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme with its inhibitor L-cysteine
recombinant enzyme, crystals grew from 0.1 M MES, pH 6.6, 1ß% 2-methyl-2,3-pentanediol, 0.5 M sodium thiocyanate, 5.5 mM cysteine, and SeMet SAT (10 mg/ml) sitting drops, at 20°C within 7 days. 2.2 A crystal structure of the enzyme, which is s dimer of trimers in complex with cysteine
hanging drop vapour diffusion method, 8-16% polyethylene glycol 1000, 10 mM Tris-HCl, pH 7.5, 2-4 weeks, room temperature, structure analysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A94T
activity is 160.2% of wild-type value, Ki for L-Cys is 5.7fold higher than wild-type value
M256I
Ki for L-Cys is 24fold higher than wild-type value
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
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
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
-
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
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
additional information
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
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
recombinant enzyme
recombinant from E. coli
-
recombinant wild-type and mutants from E. coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of mutant enzymes in Escherichia coli
C-terminal deletion mutants, expression in Escherichia coli strain JM70
-
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
-
insertional inactivation of wild-type CysE gene from Escherichia coli C600
-
overexpression
-
overexpression in Escherichia coli, construction of an expression vector which increases the expression to 17% of the soluble cell protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
inhibition of enzyme blocks growth of parasite trophozoites but not of mouse cell culture
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Kredich, N.M.; Becker, M.A.
Cysteine biosynthesis: serine transacetylase and O-acetylserine sulfhydrylase (Salmonella typhimurium)
Methods Enzymol.
17
459-470
1971
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
-
Manually annotated by BRENDA team
Wigley, D.B.; Derrick, J.P.; Shaw, W.V.
The serine acetyltransferase from Escherichia coli. Over-expression, purification and preliminary crystallographic analysis
FEBS Lett.
277
267-271
1990
Escherichia coli, Escherichia coli B / ATCC 11303
Manually annotated by BRENDA team
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
Takagi, H.; Kobayashi, C.; Kobayashi, S.I.; Nakamori, S.
PCR random mutagenesis into Escherichia coli serine acetyltransferase: isolation of the mutant enzymes that cause overproduction of L-cysteine and L-cystine due to the desensitization to feedback inhibition
FEBS Lett.
452
323-327
1999
Escherichia coli
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
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
Mino, K.; Hiraoka, K.; Imamura, K.; Sakiyama, T.; Eisaki, N.; Matsuyama, A.; Nakanishi, K.
Characteristics of serine acetyltransferase from Escherichia coli deleting different lengths of amino acid residues from the C-terminus
Biosci. Biotechnol. Biochem.
64
1874-1880
2000
Escherichia coli
Manually annotated by BRENDA team
Hindson, V.J.; Shaw, W.V.
Random-order ternary complex reaction mechanism of serine acetyltransferase from Escherichia coli
Biochemistry
42
3113-3119
2003
Escherichia coli
Manually annotated by BRENDA team
Hindson, V.J.
Serine acetyltransferase of Escherichia coli: substrate specificity and feedback control by cysteine
Biochem. J.
375
745-752
2003
Escherichia coli
Manually annotated by BRENDA team
Pye, V.E.; Tingey, A.P.; Robson, R.L.; Moody, P.C.
The structure and mechanism of serine acetyltransferase from Escherichia coli
J. Biol. Chem.
279
40729-40736
2004
Escherichia coli (P0A9D4), Escherichia coli
Manually annotated by BRENDA team
Zhao, C.; Moriga, Y.; Feng, B.; Kumada, Y.; Imanaka, H.; Imamura, K.; Nakanishi, K.
On the interaction site of serine acetyltransferase in the cysteine synthase complex from Escherichia coli
Biochem. Biophys. Res. Commun.
341
911-916
2006
Escherichia coli
Manually annotated by BRENDA team
Kai, Y.; Kashiwagi, T.; Ishikawa, K.; Ziyatdinov, M.K.; Redkina, E.I.; Kiriukhin, M.Y.; Gusyatiner, M.M.; Kobayashi, S.; Takagi, H.; Suzuki, E.
Engineering of Escherichia coli L-serine O-acetyltransferase on the basis of crystal structure: desensitization to feedback inhibition by L-cysteine
Protein Eng. Des. Sel.
19
163-167
2006
Escherichia coli (P0A9D4), Escherichia coli
Manually annotated by BRENDA team
Agarwal, S.; Jain, R.; Bhattacharya, A.; Azam, A.
Inhibitors of Escherichia coli serine acetyltransferase block proliferation of Entamoeba histolytica trophozoites
Int. J. Parasitol.
38
137-141
2008
Mus musculus, Escherichia coli (P0A9D4), Escherichia coli, Entamoeba histolytica (Q9U8X2), Entamoeba histolytica, Escherichia coli DH5-alpha (P0A9D4), Entamoeba histolytica HMM1:IMSS (Q9U8X2)
Manually annotated by BRENDA team