作者: Maria Elena Stroppolo , Alessandra Pesce , Mattia Falconi , Peter O'Neill , Martino Bolognesi
DOI: 10.1016/S0014-5793(00)01967-0
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摘要: The Val28-->Gly single mutant at the subunit interface of Cu,Zn superoxide dismutase from Photobacterium leiognathi displays a k(cat)/K(M) value 1.7x10(10) M(-1) s(-1), twice that native enzyme. Analysis three-dimensional structure indicates active site center is not perturbed, slight structural deviations being only localized in proximity mutation site. enzyme-substrate association rate, calculated by Brownian dynamics simulation, identical for both enzymes, indicating higher catalytic efficiency due to more favorable electrostatic potential distribution. This result demonstrates occurrence an intramolecular communication between and center, about 18 A away new strategy encode extra within other members this enzymatic family.