EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    6.2.1.1 | more |
the enzyme also forms a carbon-nitrogen bond, reaction of EC 6.3.1 acid-ammonia (or amide) ligase, i.e. amide synthase, and EC 6.3.2 acid-amino acid ligase, i.e. peptide synthase, comprising the amino group of the cysteine and the carboxyl group of the acid, overview |
Saccharomyces cerevisiae |
? |
- |
? |
| 6.2.1.1 | more |
the enzyme is a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase, Moorella thermoacetica CODH/ACS contains a very long enzyme channel to allow for intermolecular CO transport, mechanism and reaction steps, overview. Structure-function analysis in comparison to monofunctional Acs, overview |
Moorella thermoacetica |
? |
- |
? |
| 6.2.1.1 | more |
the enzyme performs arsenolysis, the alpha-subunit alone also catalyzes arsenolysis, overview |
Pyrococcus furiosus |
? |
- |
? |
| 6.2.1.1 | more |
activity determination in a coupled assay with myokinase, pyruvate kinase, and lactate dehydrogenase: SeAcs first converts acetate, CoA, and ATP to acetyl-CoA and AMP. Then, myokinase converts AMP to ADP. Pyruvate kinase converts ADP and phosphoenolpyruvate to pyruvate and ATP. Finally, lactate dehydrogenase reduces pyruvate and oxidizes NADH to NAD+ |
Salmonella enterica |
? |
- |
? |
| 6.2.1.1 | more |
activity determination in a coupled assay with myokinase, pyruvate kinase, and lactate dehydrogenase: SeAcs first converts acetate, CoA, and ATP to acetyl-CoA and AMP. Then, myokinase converts AMP to ADP. Pyruvate kinase converts ADP and phosphoenolpyruvate to pyruvate and ATP. Finally, lactate dehydrogenase reduces pyruvate and oxidizes NADH to NAD+ |
Salmonella enterica G2466 |
? |
- |
? |
| 6.2.1.1 | UTP + acetate + CoA |
- |
Penicillium chrysogenum |
UMP + diphosphate + acetyl-CoA |
- |
? |
