EC Number | Application | Comment | Organism |
---|---|---|---|
6.2.1.60 | synthesis | the pair acetyltransferase HolE/TmlU can readily ligate pseudomonic acid C to a variety of primary amines including 3-aminocoumarins, but is less effective with a series of aryl amines. An adjacent substrate carbonyl appears useful or important for recognition of the amine donor | Pseudoalteromonas sp. SANK 73390 |
EC Number | Cloned (Comment) | Organism |
---|---|---|
6.2.1.60 | expression in Escherichia coli | Pseudoalteromonas sp. SANK 73390 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.2.1.60 | 0.006 | - |
pseudomonic acid C | pH not specified in the publication, temperature not specified in the publication | Pseudoalteromonas sp. SANK 73390 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.2.1.60 | ATP + marinolic acid C + CoA | Pseudoalteromonas sp. SANK 73390 | - |
AMP + diphosphate + marinoloyl C-CoA | - |
? | |
6.2.1.60 | ATP + octanoic acid + CoA | Pseudoalteromonas sp. SANK 73390 | - |
AMP + diphosphate + octanoyl-CoA | - |
? | |
6.2.1.60 | ATP + pseudomonic acid A + CoA | Pseudoalteromonas sp. SANK 73390 | - |
AMP + diphosphate + pseuodomonoyl A-CoA | - |
? | |
6.2.1.60 | ATP + pseudomonic acid C + CoA | Pseudoalteromonas sp. SANK 73390 | - |
AMP + diphosphate + pseudomonoyl C-CoA | - |
? | |
6.2.1.60 | additional information | Pseudoalteromonas sp. SANK 73390 | at high enzyme concentration, TmlU is capable of activating acetic, octanoic, 2,4-dodecadienoic, and 2,4-decadienoic acids, albeit to a lesser extent | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.2.1.60 | Pseudoalteromonas sp. SANK 73390 | F8J3D9 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.2.1.60 | ATP + marinolic acid C + CoA | - |
Pseudoalteromonas sp. SANK 73390 | AMP + diphosphate + marinoloyl C-CoA | - |
? | |
6.2.1.60 | ATP + octanoic acid + CoA | - |
Pseudoalteromonas sp. SANK 73390 | AMP + diphosphate + octanoyl-CoA | - |
? | |
6.2.1.60 | ATP + pseudomonic acid A + CoA | - |
Pseudoalteromonas sp. SANK 73390 | AMP + diphosphate + pseuodomonoyl A-CoA | - |
? | |
6.2.1.60 | ATP + pseudomonic acid C + CoA | - |
Pseudoalteromonas sp. SANK 73390 | AMP + diphosphate + pseudomonoyl C-CoA | - |
? | |
6.2.1.60 | additional information | at high enzyme concentration, TmlU is capable of activating acetic, octanoic, 2,4-dodecadienoic, and 2,4-decadienoic acids, albeit to a lesser extent | Pseudoalteromonas sp. SANK 73390 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.2.1.60 | tmlU | - |
Pseudoalteromonas sp. SANK 73390 |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.2.1.60 | 3.2 | - |
pseudomonic acid C | pH not specified in the publication, temperature not specified in the publication | Pseudoalteromonas sp. SANK 73390 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
6.2.1.60 | physiological function | TmlU acts as a CoA ligase that activates marinolic acid as its thioester before it is processed by the acetyltransferase HolE to catalyze the amidation. TmlU prefers complex acyl acids as substrates | Pseudoalteromonas sp. SANK 73390 |