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Information on EC 2.3.1.18 - galactoside O-acetyltransferase and Organism(s) Escherichia coli and UniProt Accession P07464
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EC Tree
2.3.1.18 galactoside O-acetyltransferaseIUBMB Comments
Acts on thiogalactosides and phenylgalactoside.
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Word Map
- 2.3.1.18
- lactose
- beta-galactosidase
-
nanostructures
-
beta-helical
-
left-handed
-
permease
-
self-assembly
-
lacy
- melibiose
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
thiogalactoside transacetylase, galactoside acetyltransferase, sacol2570, galactoside transacetylase, galactoside o-acetyltransferase, thiogalactoside acetyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyltransferase, galactoside
-
-
-
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galactoside acetyltransferase
-
-
-
-
GAT
-
-
-
-
thiogalactoside acetyltransferase
-
-
-
-
thiogalactoside transacetylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + a beta-D-galactoside = CoA + a 6-acetyl-beta-D-galactoside
ordered bi-bi reaction mechanism with acetyl-CoA and CoA as the first substrate and final product, respectively
-
acetyl-CoA + a beta-D-galactoside = CoA + a 6-acetyl-beta-D-galactoside
Tyr83 is essential for enzyme activity
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
Acyl group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:beta-D-galactoside 6-acetyltransferase
Acts on thiogalactosides and phenylgalactoside.
CAS REGISTRY NUMBER
COMMENTARY
9029-94-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl alpha-D-galactopyranoside + acetyl-CoA
4-nitrophenyl 6-O-acetyl-alpha-D-galactopyranoside + CoA
-
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + acetyl-CoA
4-nitrophenyl 6-O-acetyl-beta-D-galactopyranoside + CoA
-
-
-
-
?
acetyl-CoA + beta-D-methylgalactoside
CoA + 6-O-acetyl-beta-D-methylgalactoside
-
-
-
-
?
acetyl-CoA + beta-D-phenylgalactoside
CoA + 6-O-acetyl-beta-D-phenylgalactoside
-
-
-
-
?
acetyl-CoA + beta-D-phenylglucoside
CoA + 6-O-acetyl-beta-D-phenylglucoside
-
-
-
-
?
acetyl-CoA + beta-D-thiodigalactoside
CoA + 6-O-acetyl-beta-D-thiodigalactoside
-
-
-
-
?
acetyl-CoA + beta-D-thiophenylglucoside
CoA + 6-O-acetyl-beta-D-thiophenylglucoside
-
-
-
-
?
acetyl-CoA + butyl beta-D-thiogalactoside
CoA + butyl 6-O-acetyl-beta-D-thiogalactoside
-
-
-
-
?
acetyl-CoA + isopropyl beta-D-thiogalactoside
CoA + isopropyl 6-O-acetyl-beta-D-thiogalactoside
acetyl-CoA + methyl beta-D-thiogalactoside
CoA + methyl 6-O-acetyl-beta-D-thiogalactoside
-
-
-
-
?
acetyl-CoA + o-nitrophenyl-beta-D-galactopyranoside
CoA + o-nitrophenyl 6-O-acetyl-beta-D-galactoside
-
-
-
-
?
acetyl-CoA + o-nitrophenyl-beta-D-galactoside
CoA + o-nitrophenyl 6-O-acetyl-beta-D-galactoside
-
-
-
-
?
acetyl-CoA + o-nitrophenyl-beta-D-thiogalactoside
CoA + o-nitrophenyl 6-O-acetyl-beta-D-thiogalactoside
-
-
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-galactopyranoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-galactopyranoside
-
-
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-galactoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-galactoside
-
twice as effective as isopropyl-beta-D-thiogalactoside
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-
?
acetyl-CoA + p-nitrophenyl-beta-D-glucopyranoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-glucopyranoside
-
-
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-glucoside
CoA + p-nitrophenyl-6-O-acetyl-beta-D-glucoside
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-
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-lactopyranoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-lactopyranoside
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-
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-lactoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-lactoside
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-
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-thiogalactoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-thiogalactoside
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-
-
-
?
acetyl-CoA + phenyl beta-D-thiogalactoside
CoA + 6-O-acetyl-beta-D-thiophenylgalactoside
-
-
-
-
?
butyryl-CoA + p-nitrophenyl-beta-D-galactopyranoside
CoA + p-nitrophenyl 6-O-butyryl-beta-D-galactopyranoside
-
-
-
-
?
isopropyl-thio-beta-D-galactopyranoside + acetyl-CoA
6-acetyl-isopropyl-thio-beta-D-galactopyranoside + CoA
-
-
-
-
?
isopropyl-thio-beta-D-galactopyranoside + acetyl-CoA
isopropyl 6-O-acetyl-1-thio-beta-D-galactopyranoside + CoA
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-
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + acetyl-CoA
p-nitrophenyl 6-O-acetyl-beta-D-galactopyranoside + CoA
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-
-
-
?
propionyl-CoA + p-nitrophenyl-beta-D-galactopyranoside
CoA + p-nitrophenyl 6-O-propionyl-beta-D-galactopyranoside
-
-
-
-
?
acetyl-CoA + a beta-D-galactoside
CoA + a 6-acetyl-beta-D-galactoside
-
-
-
-
?
acetyl-CoA + a beta-D-galactoside
CoA + a 6-acetyl-beta-D-galactoside
-
prevents accumulation of methyl-1-thio-beta-D-galactoside, serves as a backup device to avoid metabolic congestion
-
-
?
acetyl-CoA + isopropyl beta-D-thiogalactoside
CoA + isopropyl 6-O-acetyl-beta-D-thiogalactoside
-
-
-
-
?
acetyl-CoA + isopropyl beta-D-thiogalactoside
CoA + isopropyl 6-O-acetyl-beta-D-thiogalactoside
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-
-
?
acetyl-CoA + isopropyl beta-D-thiogalactoside
CoA + isopropyl 6-O-acetyl-beta-D-thiogalactoside
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-
-
-
?
additional information
?
-
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enzyme catalyses transfer of an acetyl group from acetyl-CoA to the 6-hydroxyl group of a beta-D-galactoside
-
-
?
additional information
?
-
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enzyme catalyses transfer of an acetyl group from acetyl-CoA to the 6-hydroxyl group of a beta-D-galactoside
-
-
?
additional information
?
-
-
butyryl-CoA is about 10% as effective as acetyl-CoA, enzyme catalyzes the transfer of acetyl from acetyl-CoA to thiogalactosides but not or at much slower rate to galactosides except when a phenyl group is attached to the oxygen atom at carbon 1, a phenyl group substitution also allows glucosides to react
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-
?
additional information
?
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it is suggested that the enzyme plays an important role in lactose utilization
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
it is suggested that the enzyme plays an important role in lactose utilization
-
-
?
acetyl-CoA + a beta-D-galactoside
CoA + a 6-acetyl-beta-D-galactoside
-
-
-
-
?
acetyl-CoA + a beta-D-galactoside
CoA + a 6-acetyl-beta-D-galactoside
-
prevents accumulation of methyl-1-thio-beta-D-galactoside, serves as a backup device to avoid metabolic congestion
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
629
isopropyl-thio-beta-D-galactopyranoside
-
hexahistidine-tagged wild type enzyme
1150
isopropyl-thio-beta-D-galactopyranoside
-
hexahistidine-tagged Y83V mutant
2440
isopropyl-thio-beta-D-galactopyranoside
-
hexahistidine-tagged Y83L mutant
2720
isopropyl-thio-beta-D-galactopyranoside
-
hexahistidine-tagged Y83F mutant
24.1
p-nitrophenyl-beta-D-galactopyranoside
-
hexahistidine-tagged Y83L mutant
27.2
p-nitrophenyl-beta-D-galactopyranoside
-
hexahistidine-tagged wild type enzyme
29.5
p-nitrophenyl-beta-D-galactopyranoside
-
hexahistidine-tagged Y83F mutant
97
p-nitrophenyl-beta-D-galactopyranoside
-
hexahistidine-tagged Y83V mutant
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.175
isopropyl-thio-beta-D-galactopyranoside
-
hexahistidine-tagged Y83V mutant
0.31
isopropyl-thio-beta-D-galactopyranoside
-
hexahistidine-tagged Y83L mutant
122
isopropyl-thio-beta-D-galactopyranoside
-
hexahistidine-tagged wild type enzyme
168
isopropyl-thio-beta-D-galactopyranoside
-
hexahistidine-tagged Y83F mutant
0.006
p-nitrophenyl-beta-D-galactopyranoside
-
hexahistidine-tagged Y83L mutant
0.022
p-nitrophenyl-beta-D-galactopyranoside
-
hexahistidine-tagged Y83V mutant
4.9
p-nitrophenyl-beta-D-galactopyranoside
-
hexahistidine-tagged Y83F mutant
11.1
p-nitrophenyl-beta-D-galactopyranoside
-
hexahistidine-tagged wild type enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
from chain A residues 131-165 are prepared as synthetical peptide and investigated
UniProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
-
determined by SDS-PAGE and gel filtration, monomer, containing a hexahistidine tag
47900
-
strain K12, high-speed equilibrium centrifugation using meniscus depletion technique
49900
-
strain ML308, high-speed equilibrium centrifugation using meniscus depletion technique
80000
80000
-
determined by SDS-PAGE and gel filtration, trimer, containing hexahistidine tags
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
Y83F
Y83L
Y83V
Y83F
-
site-directed mutagenesis, the mutant shows highy reduced activity compared to the wild-type enzyme
Y83F
-
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
Y83L
-
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
Y83V
-
tyrosine83 is essential for the activity of galactoside transacetylase
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene lacA, overexpression of His6-tagged wild-type and mutant enzymes in Escherichia coli TOP10 cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zabin, I.
Crystalline thiogalactoside transacetylase
J. Biol. Chem.
238
3300-3306
1963
Escherichia coli, Escherichia coli ML308
Zabin, I.; Kepes, A.; Monod, J.
Thiogalactoside transacetylase
J. Biol. Chem.
237
253-257
1962
Escherichia coli, Escherichia coli ML308
Musso, R.E.; Zabin, I.
Substrate specificity and kinetic studies on thiogalactoside transacetylase
Biochemistry
12
553-557
1973
Escherichia coli, Escherichia coli A324-5
Zabin, I.; Fowler, A.V.
Purification of thiogalactoside transacetylase by affinity chromatography
Anal. Biochem.
136
493-496
1984
Escherichia coli
Fried, V.A.
lac Thiogalactoside transacetylase of Escherichia coli K-12 and ML
J. Bacteriol.
143
506-509
1980
Escherichia coli, Escherichia coli ML308
Fowler, A.V.; Hediger, M.A.; Musso, R.E.; Zabin, I.
The amino acid sequence of thiogalactoside transacetylase of Escherichia coli
Biochimie
67
101-108
1985
Escherichia coli
Lewendon, A.; Ellis, J.; Shaw, W.V.
Structural and mechanistic studies of galactoside acetyltransferase, the Escherichia coli LacA gene product
J. Biol. Chem.
270
26326-26331
1995
Escherichia coli
Wang, X.G.; Roderick, S.L.
Expression, purification, crystallization and preliminary x-ray data of Escherichia coli galactoside acetyltransferase
Acta Crystallogr. Sect. D
55
1955-1957
1999
Escherichia coli
Roderick, S.L.
The lac operon galactoside acetyltransferase
C. R. Biol.
328
568-575
2005
Escherichia coli
Radeghieri, A.; Bonoli, M.; Parmeggiani, F.; Hochkoeppler, A.
Tyrosine 83 is essential for the activity of E. coli galactoside transacetylase
Biochim. Biophys. Acta
1774
243-248
2007
Escherichia coli
Ballano, G.; Zanuy, D.; Jimenez, A.I.; Cativiela, C.; Nussinov, R.; Aleman, C.
Structural analysis of a beta-helical protein motif stabilized by targeted replacements with conformationally constrained amino acids
J. Phys. Chem. B
112
13101-13115
2008
Escherichia coli (P07464), Escherichia coli
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