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Literature summary for 2.3.1.18 extracted from

  • 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 (2013), J. Struct. Funct. Genomics, 14, 97-108.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene SACOL2570, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)RIPL Staphylococcus aureus

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + a beta-D-galactoside Staphylococcus aureus 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 CoA + a 6-acetyl-beta-D-galactoside
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?

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus Q5HCZ5 subsp. COL, methicillin-resistant strain, gene SACOL2570
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Purification (Commentary)

Purification (Comment) Organism
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 Staphylococcus aureus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + a 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 Staphylococcus aureus CoA + a 6-acetyl-beta-D-galactoside
-
?
acetyl-CoA + a 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 Staphylococcus aureus CoA + a 6-acetyl-beta-D-galactoside 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 ?

Subunits

Subunits Comment Organism
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 Staphylococcus aureus

Synonyms

Synonyms Comment Organism
galactoside acetyltransferase
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Staphylococcus aureus
GAT
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Staphylococcus aureus
SACOL2570
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Staphylococcus aureus

Expression

Organism Comment Expression
Staphylococcus aureus the enzyme is downregulated by fusidic acid down

General Information

General Information Comment Organism
evolution the enzyme is a member of the galactoside acetyltransferase superfamily from methicillin-resistant Staphylococcus aureus 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 Staphylococcus aureus