General Stability | Organism |
---|---|
dithiothreitol stabilizes the enzyme | Salmonella enterica |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + cob(I)alamin | Salmonella enterica | mechanism of adenosylcobalamin biosynthesis | triphosphate + adenosylcob(III)alamin | - |
? | |
additional information | Salmonella enterica | the flavodoxin in vivo reducing agent that serves as the electron donor to the enzyme possesses a reduction potential that is considerably more positive than that of the Co2+/1+ couple of the corrinoid substrate, the enzyme overcomes this challenge by formation of an ATP-activated unique paramagnetic Co2+ corrinoid species by partial conversion, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Salmonella enterica | - |
- |
- |
Oxidation Stability | Organism |
---|---|
enzyme is oxygen-labile | Salmonella enterica |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein | reaction mechanism, substrate structure | Salmonella enterica |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.02 | - |
purified recombinant enzyme | Salmonella enterica |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + cob(I)alamin | mechanism of adenosylcobalamin biosynthesis | Salmonella enterica | triphosphate + adenosylcob(III)alamin | - |
? | |
ATP + cob(I)alamin | formation of the the essential C-Co bond by transferring the adenosyl group from a molecule of ATP to a transient Co1+ corrinoid species generated by the active site | Salmonella enterica | triphosphate + adenosylcob(III)alamin | - |
? | |
additional information | the flavodoxin in vivo reducing agent that serves as the electron donor to the enzyme possesses a reduction potential that is considerably more positive than that of the Co2+/1+ couple of the corrinoid substrate, the enzyme overcomes this challenge by formation of an ATP-activated unique paramagnetic Co2+ corrinoid species by partial conversion, overview | Salmonella enterica | ? | - |
? | |
additional information | enzyme-substrate interactions, intermediate/transition structures, spectroscopic mechanism analysis, computational modeling, overview | Salmonella enterica | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ATP:corrinoid adenosyltransferase | - |
Salmonella enterica |
CobA | - |
Salmonella enterica |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Salmonella enterica |