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Literature summary extracted from

  • Zabin, I.; Kepes, A.; Monod, J.
    Thiogalactoside transacetylase (1962), J. Biol. Chem., 237, 253-257.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.18 Co2+ slight Escherichia coli
2.3.1.18 Cu2+
-
Escherichia coli
2.3.1.18 Mn2+ slight Escherichia coli
2.3.1.18 p-chloromercuribenzoate
-
Escherichia coli
2.3.1.18 Zn2+ slight Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.18 0.04
-
acetyl-CoA
-
Escherichia coli
2.3.1.18 360
-
isopropyl beta-D-thiogalactoside
-
Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.18 additional information activity present in supernatant solution Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.1.18 additional information no requirement for divalent cation Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.18 Escherichia coli
-
ML308
-
2.3.1.18 Escherichia coli ML308
-
ML308
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.18 strain ML308 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.18 additional information
-
-
Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.18 acetyl-CoA + beta-D-methylgalactoside
-
Escherichia coli CoA + 6-O-acetyl-beta-D-methylgalactoside
-
?
2.3.1.18 acetyl-CoA + beta-D-phenylgalactoside
-
Escherichia coli CoA + 6-O-acetyl-beta-D-phenylgalactoside
-
?
2.3.1.18 acetyl-CoA + beta-D-phenylglucoside
-
Escherichia coli CoA + 6-O-acetyl-beta-D-phenylglucoside
-
?
2.3.1.18 acetyl-CoA + beta-D-thiodigalactoside
-
Escherichia coli CoA + 6-O-acetyl-beta-D-thiodigalactoside
-
?
2.3.1.18 acetyl-CoA + beta-D-thiophenylglucoside
-
Escherichia coli CoA + 6-O-acetyl-beta-D-thiophenylglucoside
-
?
2.3.1.18 acetyl-CoA + butyl beta-D-thiogalactoside
-
Escherichia coli CoA + butyl 6-O-acetyl-beta-D-thiogalactoside
-
?
2.3.1.18 acetyl-CoA + isopropyl beta-D-thiogalactoside
-
Escherichia coli CoA + isopropyl 6-O-acetyl-beta-D-thiogalactoside
-
?
2.3.1.18 acetyl-CoA + isopropyl beta-D-thiogalactoside
-
Escherichia coli ML308 CoA + isopropyl 6-O-acetyl-beta-D-thiogalactoside
-
?
2.3.1.18 acetyl-CoA + methyl beta-D-thiogalactoside
-
Escherichia coli CoA + methyl 6-O-acetyl-beta-D-thiogalactoside
-
?
2.3.1.18 acetyl-CoA + methyl beta-D-thiogalactoside
-
Escherichia coli ML308 CoA + methyl 6-O-acetyl-beta-D-thiogalactoside
-
?
2.3.1.18 acetyl-CoA + phenyl beta-D-thiogalactoside
-
Escherichia coli CoA + 6-O-acetyl-beta-D-thiophenylgalactoside
-
?
2.3.1.18 additional information palmitoyl-CoA Escherichia coli ?
-
?
2.3.1.18 additional information inactive: succinyl-CoA Escherichia coli ?
-
?
2.3.1.18 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 Escherichia coli ?
-
?
2.3.1.18 additional information palmitoyl-CoA Escherichia coli ML308 ?
-
?
2.3.1.18 additional information inactive: succinyl-CoA Escherichia coli ML308 ?
-
?
2.3.1.18 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 Escherichia coli ML308 ?
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.18 7
-
phosphate buffer Escherichia coli
2.3.1.18 8.2
-
Tris buffer Escherichia coli