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KMID : 0545120010110040709
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Journal of Microbiology and Biotechnology
2001 Volume.11 No. 4 p.709 ~ p.711
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Mutagenic Characterization of a Conserved Functional Amino Acid in Fuculose-1-Phosphate Aldolase from Methanococcus jannaschii, a Hyperthermophic Archaea
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Yoon, Hye Sook/Yoon, Hye Sook
Kwon, Si Joong/Han, Myung Soo/Yu, Yeon Gyu/Yoon, Moon Young/Kwon, Si Joong/Han, Myung Soo/Yu, Yeon Gyu/Yoon, Moon Young
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Abstract
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To elucidate the putative role of the amido group in the metal binding of the fuculose-l-phosphate aldolase from Methanococcus jannaschii, we have examined a potential target using site-directed mutagenesis. The replacement of asparagine 25 with leucine or threonine was shown to have a negative effect, not only on catalytic efficiency, but also on substrate recognition as well. The Hill coefficient values yielded a value of 1. All metals used with the wild-type aldolases exhibited higher activity than that of the mutants. The spectra of the mutants were quite different from the wildtype aldolase. A highly conserved amino acid of asparagine 25 in a related family of aldolase does not appear to provide sufficient evidence for evolution.
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