EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
    2.3.1.54 | more |
- |
Escherichia coli |
? |
- |
? |
| 2.3.1.54 | more |
phosphate cannot substitute for CoA |
Clostridium butyricum |
? |
- |
? |
| 2.3.1.54 | more |
phosphate cannot substitute for CoA |
Clostridium kluyveri |
? |
- |
? |
| 2.3.1.54 | more |
phosphate cannot substitute for CoA |
Clostridium beijerinckii |
? |
- |
? |
| 2.3.1.54 | more |
not essential for nitrate respiration |
Escherichia coli |
? |
- |
? |
| 2.3.1.54 | more |
analysis of the cytosolic proteome involving the enzyme, proteome profile |
Streptococcus thermophilus |
? |
- |
? |
| 2.3.1.54 | more |
hydrogen is formed from pyruvate by multiple parallel pathways, one pathway involves formate as an intermediate, pyruvate-formate lyase, and formate-hydrogen lyase, comprised of HydA hydrogenase and formate dehydrogenase, and a formate-independent pathway involving pyruvate dehydrogenase, the expression of pflB paralleled the expression of hydA and hyaB |
Shewanella oneidensis |
? |
- |
? |
| 2.3.1.54 | more |
The product of yfiD gene is similar to pyruvate formate-lyase activase and it has been reported to activate PFL by replacing the glycyl radical domain, overview, the YfiD protein contributes to the pyruvate formate-lyase flux in the Escherichia coli arcA mutant strain, but not in the wild-type strain |
Escherichia coli |
? |
- |
? |
| 2.3.1.54 | more |
the enzyme is a glycyl radical enzyme, changes in the active site indicate that the actual substrate of PFL2 is bigger than a glycerol molecule, but sequence and structural homology suggest that PFL2 may be a dehydratase |
Archaeoglobus fulgidus |
? |
- |
? |
| 2.3.1.54 | more |
pyruvate formate-lyase interacts directly with the formate channel FocA to regulate formate translocation, molecular modeling of the FocA-PflB complex, the N-terminus of FocA is important for interaction with enzyme PflB |
Escherichia coli |
? |
- |
? |
