Exploring Amino Acids Responsible for the Temperature Profile of Glycoside Hydrolase Family 45 Endoglucanase EGL3 from Humicola grisea

Koichiro MURASHIMA; Atsushi SHIMONAKA; Tomoko NISHIMURA; Yuko BABA; Jinichiro KOGA; Hidetoshi KUBOTA; Toshiaki KONO

doi:10.1271/bbb.60149

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Exploring Amino Acids Responsible for the Temperature Profile of Glycoside Hydrolase Family 45 Endoglucanase EGL3 from Humicola grisea

Koichiro MURASHIMA, Atsushi SHIMONAKA, Tomoko NISHIMURA, Yuko BABA, Jinichiro KOGA, Hidetoshi KUBOTA, Toshiaki KONO

著者情報

キーワード: endoglucanase, glycoside hydrolase family 45, temperature profile, Humicola grisea, Rhizopus oryzae

ジャーナルフリー早期公開

論文ID: 60149

DOI https://doi.org/10.1271/bbb.60149

この記事には本公開記事があります。

The final version of this article is now available: Vol. 70 (2006) , No. 9 p.2205

詳細

抄録

EGL3 and RCE1 are glycoside hydrolase family 45 endoglucanases isolated from Humicola grisea and Rhizopus oryzae respectively. The amino acid sequences of the two endoglucanases are homologous; on the other hand, the optimum temperature of EGL3 is higher than that of RCE1. In this study, four chimeric endoglucanases, named ER1, ER2, ER3 and ER4, in which one of four sequential amino acid regions of the EGL3 catalytic domain (CAD) was replaced by the corresponding RCE1 amino acids, were constructed to explore the region responsible for the EGL3 temperature profile. Then their temperature profiles were compared with that of the recombinant EGL3. Replacement of the N-terminal region of EGL3 with that of RCE1 caused the EGL3 temperature profile to shift to a lower temperature. These results suggest that the N-terminal amino acids of the EGL3 are responsible for the EGL3 temperature profile.

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