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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. Issue 38 (18th April 2016)
Record Type:
Journal Article
Title:
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. Issue 38 (18th April 2016)
Main Title:
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
Abstract : The contributions of Lys370α and Asp298α to the critical Co–C bond cleavage trigger and open–closed cycle transitions of lysine 5, 6-aminomutase. 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.