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Literature summary extracted from

  • Gupta, G.; Baghel, A.S.; Bansal, S.; Tyagi, T.K.; Kumari, R.; Saini, N.K.; Ponnan, P.; Kumar, A.; Bose, M.; Saluja, D.; Patkar, S.A.; Parmar, V.S.; Raj, H.G.
    Establishment of glutamine synthetase of Mycobacterium smegmatis as a protein acetyltransferase utilizing polyphenolic acetates as the acetyl group donors (2008), J. Biochem., 144, 709-715.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.1.2 expression in Escherichia coli Mycolicibacterium smegmatis

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.1.2 L-methionine sulfoximine no inhibition of the acetyltransferase activity Mycolicibacterium smegmatis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.1.2 Mg2+
-
 Escherichia coli
6.3.1.2 Mg2+
-
 Mycolicibacterium smegmatis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.1.2 58000
-
 x * 58000, SDS-PAGE Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.1.2 ATP + L-glutamate + NH3 Escherichia coli
-
 ADP + phosphate + L-glutamine
-
 ?
6.3.1.2 ATP + L-glutamate + NH3 Mycolicibacterium smegmatis
-
 ADP + phosphate + L-glutamine
-
 ?
6.3.1.2 ATP + L-glutamate + NH3 Mycolicibacterium smegmatis VT301
-
 ADP + phosphate + L-glutamine
-
 ?
6.3.1.2 additional information Escherichia coli the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, overview ?
-
 ?
6.3.1.2 additional information Mycolicibacterium smegmatis the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, substrate specificity, overview. The TAase activity of MTAase is independent of the catalytic activity of the glutamine synthetase ?
-
 ?
6.3.1.2 additional information Mycolicibacterium smegmatis VT301 the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, substrate specificity, overview. The TAase activity of MTAase is independent of the catalytic activity of the glutamine synthetase ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.1.2 Escherichia coli
-
-
-
6.3.1.2 Mycolicibacterium smegmatis
-
-
-
6.3.1.2 Mycolicibacterium smegmatis VT301
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.1.2 recombinant enzyme from Escherichia coli by nickel affinity chromatography, native enzyme 24.2fold to homogeneity by hydrophobic interaction chromatography followed by two different steps of anion exchange chromatography Mycolicibacterium smegmatis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.1.2 commercial preparation
-
 Escherichia coli
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.1.2 ATP + L-glutamate + NH3
-
 Escherichia coli ADP + phosphate + L-glutamine
-
 ?
6.3.1.2 ATP + L-glutamate + NH3
-
 Mycolicibacterium smegmatis ADP + phosphate + L-glutamine
-
 ?
6.3.1.2 ATP + L-glutamate + NH3
-
 Mycolicibacterium smegmatis VT301 ADP + phosphate + L-glutamine
-
 ?
6.3.1.2 additional information the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, overview Escherichia coli ?
-
 ?
6.3.1.2 additional information the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, substrate specificity, overview. The TAase activity of MTAase is independent of the catalytic activity of the glutamine synthetase Mycolicibacterium smegmatis ?
-
 ?
6.3.1.2 additional information the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, substrate specificity, overview. The TAase activity of MTAase is independent of the catalytic activity of the glutamine synthetase Mycolicibacterium smegmatis VT301 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.1.2 ? x * 58000, SDS-PAGE Mycolicibacterium smegmatis

Synonyms

EC Number Synonyms Comment Organism
6.3.1.2 Glutamine synthetase
-
 Escherichia coli
6.3.1.2 Glutamine synthetase
-
 Mycolicibacterium smegmatis
6.3.1.2 protein transacetylase
-
 Escherichia coli
6.3.1.2 protein transacetylase
-
 Mycolicibacterium smegmatis
6.3.1.2 TAase
-
 Escherichia coli
6.3.1.2 TAase
-
 Mycolicibacterium smegmatis

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.1.2 ATP
-
 Escherichia coli
6.3.1.2 ATP
-
 Mycolicibacterium smegmatis