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Catalytic roles of lysines (K9, K27, K31) in the N-terminal domain in human adenylate kinase by random site-directed mutagenesis



Catalytic roles of lysines (K9, K27, K31) in the N-terminal domain in human adenylate kinase by random site-directed mutagenesis



Biochemistry and Molecular Biology International 40(5): 897-906



To elucidate lysine residues in the N-terminal domain of human cytosolic adenylate kinase (hAK1, EC 2.7.4.3), random site-directed mutagenesis of K9, K27, and K31 residues was performed, and six mutants were analyzed by steady-state kinetics. K9 residue may play an important role in catalysis by interacting with AMP-2-. K27 and K31 residues appear to play a functional role in catalysis by interacting with MgATP-2-. In human AK, the epsilon-amino group in the side chain of these lysine residues would be essential for phosphoryl transfer between MgATp-2- and AMP-2- during transition state.

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Accession: 008270203

Download citation: RISBibTeXText

PMID: 8955878

DOI: 10.1080/15216549600201513


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