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Escherichia colifatty acid cyclopropane synthase (CFAS)was overproduced and purified as a His6-tagged protein.This recombinant enzyme is as active as the native enzymewith aKmof 90lMforS-AdoMet and a specific activity of5·10)2lmolÆmin)1Æmg)1. The enzyme is devoid of organicor metal cofactors and is unable to catalyze the wash-out ofthemethyl protons ofS-AdoMet to the solvent, data that donot support the ylidemechanism. Inactivationof the enzymeby 5,5¢-dithiobis-(2-nitrobenzoic acid) (DTNB), a pseudofirst-order process with a rate constant of 1.2M)1Æs)1, is notprotected by substrates. Graphical analysis of the inactiva-tion byDTNB revealed that only one cysteine is responsiblefor the inactivation of the enzyme. ...
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Escherichia coli cyclopropane fatty acid synthase Mechanistic and site-directed mutagenetic studies
