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Issue 38, 2016
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The molecular mechanism of the open–closed protein conformational cycle transitions and coupled substrate binding, activation and product release events in lysine 5,6-aminomutase

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Abstract

How a protein domain motion is coupled to the catalytic cycle is a current subject in enzymology. We render down a complicated domain motion in the 5′-deoxyadenosylcobalamin and pyridoxal-5′-phosphate codependent radical enzyme, lysine 5,6-aminomutase, into dominant contributions from Lys370α and Asp298α to the critical Co–C bond cleavage trigger and open–closed cycle transitions.

Graphical abstract: The molecular mechanism of the open–closed protein conformational cycle transitions and coupled substrate binding, activation and product release events in lysine 5,6-aminomutase

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Publication details

The article was received on 02 Mar 2016, accepted on 05 Apr 2016 and first published on 05 Apr 2016


Article type: Communication
DOI: 10.1039/C6CC01888B
Citation: Chem. Commun., 2016,52, 6399-6402
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    The molecular mechanism of the open–closed protein conformational cycle transitions and coupled substrate binding, activation and product release events in lysine 5,6-aminomutase

    H. Lo, H. Lin, A. N. Maity and S. Ke, Chem. Commun., 2016, 52, 6399
    DOI: 10.1039/C6CC01888B

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