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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.
    View publication on PubMed

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
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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
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