Protein Variants | Comment | Organism |
---|---|---|
F321Y | mutation in the alpha-subunit of hydrolase component, in presence of 10 mM propanoate, 61% residual activity | Thauera butanivorans |
G113N | mutation in the alpha-subunit of hydrolase component, loss of inhibition by propanoate | Thauera butanivorans |
L279F | mutation in the alpha-subunit of hydrolase component, in presence of 10 mM propanoate, 56% residual activity | Thauera butanivorans |
Q320K | mutation in the alpha-subunit of hydrolase component, in presence of 10 mM propanoate, 28% residual activity | Thauera butanivorans |
T148C | mutation in the alpha-subunit of hydrolase component, in presence of 10 mM propanoate, 15% residual activity | Thauera butanivorans |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Butanoate | incubation of alkane-grown cells with butanoate or propanoate leads to irreversible time- and O2-dependent loss of butane monooxygenase activity | Thauera butanivorans | |
propanoate | 10 mM, 41% residual activity. Incubation of alkane-grown cells with butanoate or propanoate leads to irreversible time- and O2-dependent loss of butane monooxygenase activity. Propanoate-dependent inactivation involves interaction with the catalytic site. Butane monooxygenase is protected from propanoate-dependent inactivation by the presence of its natural substrate, butane | Thauera butanivorans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thauera butanivorans | Q8KQF0 and Q8KQE9 and Q8KQE7 and Q8KQE6 and Q8KQE8 | Q8KQF0 i.e. alpha-subunit BmoX, Q8KQE9 i.e. beta-subunit BmoY, Q8KQE7 i.e. gamma-subunit BmoZ of hydrolase component, respectively. Q8KQE6 i.e. oxidoreductase BmoC, Q8KQE8 i.e. regulatory protein BmoB | - |
Thauera butanivorans ATCC 43655 | Q8KQF0 and Q8KQE9 and Q8KQE7 and Q8KQE6 and Q8KQE8 | Q8KQF0 i.e. alpha-subunit BmoX, Q8KQE9 i.e. beta-subunit BmoY, Q8KQE7 i.e. gamma-subunit BmoZ of hydrolase component, respectively. Q8KQE6 i.e. oxidoreductase BmoC, Q8KQE8 i.e. regulatory protein BmoB | - |