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J. Biol. Chem., Vol. 269, Issue 51, 32175-32180, 12, 1994
AD Tepper, H Dammann, AA Bominaar and M Veron
Nucleoside-diphosphate kinase (EC 2.7.4.6) catalyzes phosphate exchange
between nucleoside triphosphates and nucleoside diphosphates. Its 17 kDa
subunits are highly conserved throughout evolution in both sequence and
tertiary structure. Using site-directed mutagenesis we investigated the
function of 8 amino acids (Lys16, Tyr56, Arg92, Thr98, Arg109, Asn119,
Ser124, and Glu133) that are totally conserved among all nucleoside
diphosphate kinases known to date. The mutant proteins all show decreased
specific activity and support roles for these residues in catalysis,
substrate binding, or both, as was previously proposed on the basis of the
x-ray structure (Morera, S., Lascu, I., Dumas, C., LeBras, G., Briozzo, P.,
Veron, M., and Janin, J. (1994) Biochemistry 33, 459-467). Furthermore,
residues Lys16, Arg109, and Asn 119 were identified to play important roles
in conformational stability or subunit interactions. We show that Lys16 and
Asn119 form a rigid structure that is important for enzymatic function and
that Arg109, known to interact with the phosphate moiety of the substrate,
also plays an important role in subunit association. The dual roles of
Lys16, Arg109, and Asn119 in both substrate binding and subunit assembly
provide further evidence for a functional coupling between catalytic
activity and quaternary structure in nucleoside diphosphate kinase.
Investigation of the active site and the conformational stability of nucleoside diphosphate kinase by site-directed mutagenesis
Unite de Biochimie Cellulaire, CNRS-URA 1129, Institut Pasteur, Paris, France.
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