EC Number | Cloned (Comment) | Organism |
---|---|---|
6.3.1.2 | expression in Escherichia coli | Mycolicibacterium smegmatis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
6.3.1.2 | L-methionine sulfoximine | no inhibition of the acetyltransferase activity | Mycolicibacterium smegmatis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.3.1.2 | Mg2+ | - |
Escherichia coli | |
6.3.1.2 | Mg2+ | - |
Mycolicibacterium smegmatis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
6.3.1.2 | 58000 | - |
x * 58000, SDS-PAGE | Mycolicibacterium smegmatis |
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 | ? | - |
? |
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 | - |
- |
- |
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 |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
6.3.1.2 | commercial preparation | - |
Escherichia coli | - |
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 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
6.3.1.2 | ? | x * 58000, SDS-PAGE | Mycolicibacterium smegmatis |
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 |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.3.1.2 | ATP | - |
Escherichia coli | |
6.3.1.2 | ATP | - |
Mycolicibacterium smegmatis |