Information on EC 2.3.1.18 - galactoside O-acetyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.18
-
RECOMMENDED NAME
GeneOntology No.
galactoside O-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + a beta-D-galactoside = CoA + a 6-acetyl-beta-D-galactoside
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:beta-D-galactoside 6-acetyltransferase
Acts on thiogalactosides and phenylgalactoside.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-94-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
A324-5
-
-
Manually annotated by BRENDA team
K12
-
-
Manually annotated by BRENDA team
subsp. COL, methicillin-resistant strain, gene SACOL2570
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme is a member of the galactoside acetyltransferase superfamily from methicillin-resistant Staphylococcus aureus
physiological function
the enzyme SACOL2570 is a putative galactoside O-acetyltransferase (GAT) protein and may act as a detoxifying enzyme, acetylating nonmetabolizable carbohydrates to prevent their reentry into the cell. It is potentially involved in the cellular processes of toxin production and antibiotic resistance
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl beta-D-galactopyranoside + acetyl-CoA
4-nitrophenyl 6-O-acetyl-beta-D-galactopyranoside + CoA
show the reaction diagram
-
-
-
-
?
acetyl-CoA + a beta-D-galactoside
CoA + a 6-acetyl-beta-D-galactoside
show the reaction diagram
acetyl-CoA + beta-D-galactoside
CoA + 6-acetyl-beta-D-galactoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + beta-D-methylgalactoside
CoA + 6-O-acetyl-beta-D-methylgalactoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + beta-D-phenylgalactoside
CoA + 6-O-acetyl-beta-D-phenylgalactoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + beta-D-phenylglucoside
CoA + 6-O-acetyl-beta-D-phenylglucoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + beta-D-thiodigalactoside
CoA + 6-O-acetyl-beta-D-thiodigalactoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + beta-D-thiophenylglucoside
CoA + 6-O-acetyl-beta-D-thiophenylglucoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + butyl beta-D-thiogalactoside
CoA + butyl 6-O-acetyl-beta-D-thiogalactoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + isopropyl beta-D-thiogalactoside
CoA + isopropyl 6-O-acetyl-beta-D-thiogalactoside
show the reaction diagram
acetyl-CoA + methyl beta-D-thiogalactoside
CoA + methyl 6-O-acetyl-beta-D-thiogalactoside
show the reaction diagram
acetyl-CoA + o-nitrophenyl-beta-D-galactopyranoside
CoA + o-nitrophenyl 6-O-acetyl-beta-D-galactoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + o-nitrophenyl-beta-D-galactoside
CoA + o-nitrophenyl 6-O-acetyl-beta-D-galactoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + o-nitrophenyl-beta-D-thiogalactoside
CoA + o-nitrophenyl 6-O-acetyl-beta-D-thiogalactoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-galactopyranoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-galactopyranoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-galactoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-galactoside
show the reaction diagram
acetyl-CoA + p-nitrophenyl-beta-D-glucopyranoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-glucopyranoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-glucoside
CoA + p-nitrophenyl-6-O-acetyl-beta-D-glucoside
show the reaction diagram
acetyl-CoA + p-nitrophenyl-beta-D-lactopyranoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-lactopyranoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-lactoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-lactoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-thiogalactoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-thiogalactoside
show the reaction diagram
-
-
-
-
?
acetyl-CoA + phenyl beta-D-thiogalactoside
CoA + 6-O-acetyl-beta-D-thiophenylgalactoside
show the reaction diagram
-
-
-
-
?
butyryl-CoA + p-nitrophenyl-beta-D-galactopyranoside
CoA + p-nitrophenyl 6-O-butyryl-beta-D-galactopyranoside
show the reaction diagram
-
-
-
-
?
isopropyl-thio-beta-D-galactopyranoside
?
show the reaction diagram
-
-
-
-
?
isopropyl-thio-beta-D-galactopyranoside + acetyl-CoA
6-acetyl-isopropyl-thio-beta-D-galactopyranoside + CoA
show the reaction diagram
-
-
-
-
?
isopropyl-thio-beta-D-galactopyranoside + acetyl-CoA
isopropyl 6-O-acetyl-1-thio-beta-D-galactopyranoside + CoA
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-galactopyranoside
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + acetyl-CoA
p-nitrophenyl 6-O-acetyl-beta-D-galactopyranoside + CoA
show the reaction diagram
-
-
-
-
?
propionyl-CoA + p-nitrophenyl-beta-D-galactopyranoside
CoA + p-nitrophenyl 6-O-propionyl-beta-D-galactopyranoside
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 + a beta-D-galactoside
CoA + a 6-acetyl-beta-D-galactoside
show the reaction diagram
acetyl-CoA + beta-D-galactoside
CoA + 6-acetyl-beta-D-galactoside
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MgSO4
-
1 mM, addition to 5,5'-dithiobis(2-nitrobenzoic acid) assay mixture lacking EDTA inhibits, preincubation of transacetylase (2 mg/ml in 0.05 M Tris, pH 7.8) with MgSO4 for 1 h at 30°C and subsequent dilution of the enzyme 1000-fold in 5,5'-dithiobis(2-nitrobenzoic acid) assay mixture lacking both EDTA and the metal ion stimulates
Mn2+
-
stimulates when enzyme is initially incubated with the ion in Tris buffer but has no effect if initially incubated in phosphate or if added to the standard assay medium containing 0.05 M phosphate
additional information
-
no requirement for divalent cation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
weak
acetyl-CoA
-
-
Co2+
-
slight
iodoacetamide
-
complete inactivation
MgSO4
-
1 mM, addition to 5,5'-dithiobis(2-nitrobenzoic acid) assay mixture lacking EDTA inhibits, preincubation of transacetylase (2 mg/ml in 0.05 M Tris, pH 7.8) with MgSO4 for 1 h at 30°C and subsequent dilution of the enzyme 1000fold in 5,5'-dithiobis(2-nitrobenzoic acid) assay mixture lacking both EDTA and the metal ion stimulates
Mn2+
-
slight
MnSO4
-
40% inhibition
p-chloromercuribenzoate
-
-
Zn2+
-
slight
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24.1 - 97
4-nitrophenyl-beta-D-galactopyranoside
0.04 - 0.266
acetyl-CoA
0.221
butyryl-CoA
-
p-nitrophenyl-beta-D-galactopyranoside
360 - 1500
isopropyl beta-D-thiogalactoside
629 - 2720
isopropyl-thio-beta-D-galactopyranoside
67.9
o-nitrophenyl-beta-D-galactopyranoside
-
acetyl donor: acetyl-CoA
57.9
p-nitrophenyl-alpha-D-galactopyranoside
-
acetyl donor: acetyl-CoA
12 - 97
p-nitrophenyl-beta-D-galactopyranoside
63.4
phenyl-beta-D-galactopyranoside
-
acetyl donor: acetyl-CoA
0.098
propionyl-CoA
-
p-nitrophenyl-beta-D-galactopyranoside
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006 - 11.1
4-nitrophenyl-beta-D-galactopyranoside
0.175 - 168
isopropyl-thio-beta-D-galactopyranoside
8.9
o-nitrophenyl-beta-D-galactopyranoside
Escherichia coli
-
acetyl donor: acetyl-CoA
1.42
p-nitrophenyl-alpha-D-galactopyranoside
Escherichia coli
-
acetyl donor: acetyl-CoA
0.006 - 14.7
p-nitrophenyl-beta-D-galactopyranoside
1.84
p-nitrophenyl-beta-D-glucopyranoside
Escherichia coli
-
acetyl donor: acetyl-CoA
1.84
p-nitrophenyl-beta-D-lactopyranoside
Escherichia coli
-
acetyl donor: acetyl-CoA
13
phenyl-beta-D-galactopyranoside
Escherichia coli
-
acetyl donor: acetyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.057
acetyl-CoA
-
-
0.068
CoA
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35.3
-
isopropyl 6-O-acetyl-beta-D-thiogalactoside produced
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
phosphate buffer
8.2
-
Tris buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
activity assay; assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22671
-
2 * 22671, amino acid sequence analysis
24800
-
2 * 24800, strain K12 and ML308, SDS-PAGE
28000
-
determined by SDS-PAGE and gel filtration, monomer, containing a hexahistidine tag
45340
-
amino acid sequence analysis
47900
-
strain K12, high-speed equilibrium centrifugation using meniscus depletion technique
49900
-
strain ML308, high-speed equilibrium centrifugation using meniscus depletion technique
80000
-
determined by SDS-PAGE and gel filtration, trimer, containing hexahistidine tags; recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotrimer
in solution, small-angle X-ray scattering and dynamic light scattering. The protein subunit consists of an N-terminal alpha-helical domain connected to a C-terminal LbetaH domain
homotrimer
-
-
trimer
-
3 * 28000, recombinant enzyme, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme bound with CoA, hanging drop vapor diffusion method, mixing f 0.001 ml of protein solution containing 2.6 mg/ml Se-Met-labeled enzyme in 10 mM HEPES buffer, pH 7.5 and 500 mM NaCl, with 0.001 ml of reervoir solution containing 200 mM di-ammonium hydrogen citrate, 20% w/v PEG 3350, pH 5.0, 22°C, X-ray diffraction structure determination and analysis at 1.6 A resolution, molecular dynamics and mechanics simulation, modeling
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56
-
30 min, about 25% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
frozen, in salt solution of low ionic strength, stable
-
in ammonium sulfate suspension, stable for months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
-
K12 strain H30000; strain ML308
-
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)RIPL by nickel affinity chromatography, tag cleavage with TEV protease, another step of nickel affinity chromatography, and gel filtration
recombinant His6-tagged wild-type and mutant enzymes by nickel affinity chromatography, ion exchange chromatography, and gel filtration; using a HiTrap metal-chelating affinity chromatography column, a HiTrap desalting, and a Superdex 200 column
-
wild-type and mutant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
gene lacA, overexpression of His6-tagged wild-type and mutant enzymes in Escherichia coli TOP10 cells; into the pTrcHisB vector
-
gene SACOL2570, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)RIPL
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is downregulated by fusidic acid
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G149Ac3c
glycine is substituted by the constrained amino acids 1-aminocyclopropane-1-carboxylic acid, from protein chain A peptide from residues 131-165 are synthetical produced and investigated, the mutated peptide has a reduce conformational flexibility
G149Ac5c
glycine is substituted by the constrained amino acids 1-aminocyclopentane-1-carboxylic acid, from protein chain A peptide from residues 131-165 are synthetical produced and investigated, the mutated peptide has a reduce conformational flexibility
H115A
-
kcat highly decreased, histidyl residue has an important catalytic role
S162A
-
kcat increased, Ser162 not catalytically important
W139F
-
kcat 10fold decreased
Y83F
-
site-directed mutagenesis, the mutant shows highy reduced activity compared to the wild-type enzyme; tyrosine83 is essential for the activity of galactoside transacetylase
Y83L
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme; tyrosine83 is essential for the activity of galactoside transacetylase
Y83V
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme; tyrosine83 is essential for the activity of galactoside transacetylase
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