Literature summary extracted from
Doughty, D.M.; Halsey, K.H.; Vieville, C.J.; Sayavedra-Soto, L.A.; Arp, D.J.; Bottomley, P.J.
Propionate inactivation of butane monooxygenase activity in Pseudomonas butanovora: biochemical and physiological implications (2007), Microbiology, 153, 3722-3729.
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.14.13.230 |
F321Y |
mutation in the alpha-subunit of hydrolase component, in presence of 10 mM propanoate, 61% residual activity |
Thauera butanivorans |
1.14.13.230 |
G113N |
mutation in the alpha-subunit of hydrolase component, loss of inhibition by propanoate |
Thauera butanivorans |
1.14.13.230 |
L279F |
mutation in the alpha-subunit of hydrolase component, in presence of 10 mM propanoate, 56% residual activity |
Thauera butanivorans |
1.14.13.230 |
Q320K |
mutation in the alpha-subunit of hydrolase component, in presence of 10 mM propanoate, 28% residual activity |
Thauera butanivorans |
1.14.13.230 |
T148C |
mutation in the alpha-subunit of hydrolase component, in presence of 10 mM propanoate, 15% residual activity |
Thauera butanivorans |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.14.13.230 |
Butanoate |
incubation of alkane-grown cells with butanoate or propanoate leads to irreversible time- and O2-dependent loss of butane monooxygenase activity |
Thauera butanivorans |
|
1.14.13.230 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.14.13.230 |
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 |
- |
1.14.13.230 |
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 |
- |