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Information on EC 2.3.1.18 - galactoside O-acetyltransferase
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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 enzyme appears in viruses and cellular organisms
Synonyms
thiogalactoside transacetylase, galactoside acetyltransferase, sacol2570, galactoside transacetylase, galactoside o-acetyltransferase, thiogalactoside acetyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyltransferase, galactoside
-
-
-
-
galactoside acetyltransferase
GAT
thiogalactoside acetyltransferase
-
-
-
-
thiogalactoside transacetylase
-
-
-
-
galactoside acetyltransferase
-
-
-
-
GAT
-
-
-
-
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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
-
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
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-
acetyl-CoA + a beta-D-galactoside = CoA + a 6-acetyl-beta-D-galactoside
-
-
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9029-94-1
-
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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 + o-nitrophenyl-beta-D-galactopyranoside
CoA + o-nitrophenyl 6-O-acetyl-beta-D-galactoside
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-
-
-
?
acetyl-CoA + o-nitrophenyl-beta-D-galactoside
CoA + o-nitrophenyl 6-O-acetyl-beta-D-galactoside
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-
-
-
?
acetyl-CoA + o-nitrophenyl-beta-D-thiogalactoside
CoA + o-nitrophenyl 6-O-acetyl-beta-D-thiogalactoside
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-
-
-
?
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
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
acetyl-CoA + p-nitrophenyl-beta-D-lactopyranoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-lactopyranoside
-
-
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-lactoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-lactoside
-
-
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-thiogalactoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-thiogalactoside
-
-
-
-
?
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
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-
-
-
?
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
-
-
-
-
?
propionyl-CoA + p-nitrophenyl-beta-D-galactopyranoside
CoA + p-nitrophenyl 6-O-propionyl-beta-D-galactopyranoside
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-
-
-
?
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 + a beta-D-galactoside
CoA + a 6-acetyl-beta-D-galactoside
galactoside acetyltransferases are enzymes that transfer an acetyl group from acetyl coen-zyme A to beta-galactosides. The enzymes have a broad substrate specificity and can acetylate many galactoside derivatives, including thiogalactosides and lactosides
-
-
?
acetyl-CoA + a beta-D-galactoside
CoA + a 6-acetyl-beta-D-galactoside
CoA binds in the active site formed by the residues from adjacent LbetaH domains. After determination of CoA-bound structure, molecular dynamics simulations are performed to model the binding of AcCoA. Binding of both AcCoA and CoA to SACOL2570 is verified by isothermal titration calorimetry
binding of CoA in the 3V4E crystal structure involves residues from two adjacent monomers in the homotrimeric assembly. Residues responsible for CoA binding by SACOL2570 are Asn84, Ala112, Gly141, Lys165, and Arg182
-
?
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
-
-
-
?
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
-
-
-
?
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 + methyl beta-D-thiogalactoside
CoA + methyl 6-O-acetyl-beta-D-thiogalactoside
-
-
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-galactoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-galactoside
-
twice as effective as isopropyl-beta-D-thiogalactoside
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-galactoside
CoA + p-nitrophenyl 6-O-acetyl-beta-D-galactoside
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twice as effective as isopropyl-beta-D-thiogalactoside
-
-
?
acetyl-CoA + p-nitrophenyl-beta-D-glucoside
CoA + p-nitrophenyl-6-O-acetyl-beta-D-glucoside
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-
-
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?
acetyl-CoA + p-nitrophenyl-beta-D-glucoside
CoA + p-nitrophenyl-6-O-acetyl-beta-D-glucoside
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-
-
-
?
additional information
?
-
-
enzyme catalyses transfer of an acetyl group from acetyl-CoA to the 6-hydroxyl group of a beta-D-galactoside
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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
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-
?
additional information
?
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-
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
-
-
?
additional information
?
-
-
it is suggested that the enzyme plays an important role in lactose utilization
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-
?
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
-
-
?
additional information
?
-
-
it is suggested that the enzyme plays an important role in lactose utilization
-
-
?
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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
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 + a beta-D-galactoside
CoA + a 6-acetyl-beta-D-galactoside
galactoside acetyltransferases are enzymes that transfer an acetyl group from acetyl coen-zyme A to beta-galactosides. The enzymes have a broad substrate specificity and can acetylate many galactoside derivatives, including thiogalactosides and lactosides
-
-
?
additional information
?
-
-
it is suggested that the enzyme plays an important role in lactose utilization
-
-
?
additional information
?
-
-
it is suggested that the enzyme plays an important role in lactose utilization
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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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
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Biophysical analysis of the putative acetyltransferase SACOL2570 from methicillin-resistant Staphylococcus aureus.
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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
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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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subsp. COL, methicillin-resistant strain, gene SACOL2570
UniProt
brenda
from chain A residues 131-165 are prepared as synthetical peptide and investigated
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
Show AA Sequence and Transmembrane Helices (902 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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
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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
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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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE