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Information on EC 2.3.1.18 - galactoside O-acetyltransferase and Organism(s) Staphylococcus aureus and UniProt Accession Q5HCZ5

for references in articles please use BRENDA:EC2.3.1.18
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IUBMB Comments
Acts on thiogalactosides and phenylgalactoside.
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This record set is specific for:
Staphylococcus aureus
UNIPROT: Q5HCZ5
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Word Map
The taxonomic range for the selected organisms is: Staphylococcus aureus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
galactoside acetyltransferase
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acetyltransferase, galactoside
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galactoside acetyltransferase
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GAT
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thiogalactoside acetyltransferase
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thiogalactoside transacetylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 hide
9029-94-1
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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 + a beta-D-galactoside
CoA + a 6-acetyl-beta-D-galactoside
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 + a beta-D-galactoside
CoA + a 6-acetyl-beta-D-galactoside
show the reaction diagram
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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
SUBUNIT
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Luo, H.B.; Knapik, A.A.; Petkowski, J.J.; Demas, M.; Shumilin, I.A.; Zheng, H.; Chruszcz, M.; Minor, W.
Biophysical analysis of the putative acetyltransferase SACOL2570 from methicillin-resistant Staphylococcus aureus
J. Struct. Funct. Genomics
14
97-108
2013
Staphylococcus aureus (Q5HCZ5), Staphylococcus aureus
Manually annotated by BRENDA team