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- W2080456846 abstract "The regulatory protein B of soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath), exists as a mixture of the full-length active form and truncated forms, B′ and B″. Electrospray ionisation mass spectrometry (ESI-MS) was used to identify a cleavage site between Met12 and Gly13, such that 12 amino acids were lost from the N-terminus of protein B. This truncate was designated B′ and molecular masses were assigned to proteins B and B′ of 15 852.6 ± 0.4 Da and 14629.5 ± 0.3 Da, respectively. A cleavage site between Gln29 and Val30 was also identified such that 29 amino acids were lost from the N-terminus of protein B. This truncate was designated B″ and had a molecular mass of 12 709.93 ± 0.02 Da. Proteins B′ and B″ were found to be inactive in the sMMO system. Addition of protease inhibitors or the heterologous expression of protein B in various strains of lon-deficient or ompT-deficient Escherichia coli, did not inhibit B′ formation. Expression of protein B as a glutathione S-transferase fusion protein and subsequent purification of protein B from E. coli using affinity chromatography resulted in preparations of protein B with higher enzyme activities than that of wild-type protein B. However, ESI-MS confirmed that protein B′ was still present. Alteration of the Met12-Gly13 cleavage site to Met12-Gln13 revealed that the stability of G13Q at 20°C and 37°C was higher than that of wild-type preparations. ESI-MS indicated that protein B′ was absent and could only be identified after prolonged incubation at room temperature. The amount of active protein B present in the cell may be controlled by protein B cleavage, thereby regulating electron transfer. Alternatively, it may allow protein B to maintain a certain conformation necessary for enzyme activity and this may control the activity of sMMO in response to the supply of methane to the cell." @default.
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- W2080456846 date "1997-08-15" @default.
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- W2080456846 title "Inactivation of the Regulatory Protein B of Soluble Methane Monooxygenase from Methylococcus Capsulatus (Bath) by Proteolysis can be Overcome by a Gly to Gin Modification" @default.
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- W2080456846 doi "https://doi.org/10.1111/j.1432-1033.1997.t01-1-00072.x" @default.
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