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J. Biochem, 1998, Vol. 123, No. 1 24-27
© 1998 Japanese Biochemical Society

other

Long-Range Effect of Mutation of Calcium Binding Asparates on the Catalytic Activity of Alkaline Protease from Pseudomonas aeruginosa1

Yoshiro Miyajima*, Yasuo Hata{dagger}, Jun Fukushima{ddagger}, Susumu Kawamoto{ddagger}, Kenji Okuda{ddagger}, Yuji Shibano§ and Kazuyuki Morihara*,2

*Institute for Applied Life Science, Graduate School of University of East Asia 2-1, Ichinomiya-Gakuen-cho, Shimonoseki, Yamaguchi 751
{dagger}Institute for Chemical Research, Kyoto University Uji, Kyoto 611
{ddagger}Department of Bacteriology, Yokohama City University School of Medicine 3-9, Fukuura, Kanazawa-ku, Yokohama 236
§Department of Molecular Biology, Biomolecular Engineering Research Institute 6-2-3, Furuedai, Suita, Osaka 565

2To whom correspondence should be addressed.

Apart from a catalytic domain, the alkaline protease of Pseudomonas aeruginosa has a novel parallel ß-helix domain stabilized through Ca2+ binding. In order to clarify the importance of the ß-helix structure in maturation of the enzyme, aspartic residue D-356 or D-365 in the Ca2+ binding sequence motif was replaced with L-alanine, and the catalytic activity of each mutant was assayed. These mutants did not show any proteolytic activity, although the composition of their polypeptide chains was the same as that of the wild type except for the mutated alanine residue. These results suggest that D-356 and D-365 are important in control of the ß-helix folding induced by Ca2+ binding and that incomplete ß-helix folding due to the lack of their side-chains affects the maturation of the enzyme in the long-range order.

1This research was partly supported by Grants-in-Aid for Scientific Research (C; No. 07660126 to K.M.) and Scientific Research on Priority Areas, Molecular Biometallics (No. 09235214 to Y.H.) from the Ministry of Education, Science, Sports and Culture of Japan.


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