N-Linked Oligosaccharides of Aspergillus awamori Feruloyl Esterase Are Important for Thermostability and Catalysis
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概要
- 論文の詳細を見る
A unique N-linked glycosylation motif (Asn79-Tyr-Thr) was found in the sequence of type-A feruloyl esterases from Aspergillus spp. To clarify the function of the flap, the role of N-linked oligosaccharides located in the flap region on the biochemical properties of feruloyl esterase (AwFAEA) from Aspergillus awamori expressed in Pichia pastoris was analyzed by removing the N-linked glycosylation recognition site by site-directed mutagenesis. N79 was replaced with A or Q. N-glycosylation-free N79A and N79Q mutant enzymes had lower activity than that of the glycosylated recombinant AwFAEA wild-type enzyme toward α-naphthylbutyrate (C4), α-naphthylcaprylate (C8), and phenolic acid methyl esters. Kinetic analysis of the mutant enzymes indicated that the lower catalytic efficiency was due to a combination of increased Km and decreased kcat for N79A, and to a considerably decreased kcat for N79Q. N79A and N79Q mutant enzymes also exhibited considerably reduced thermostability relative to the wild-type.
- 社団法人 日本農芸化学会の論文
- 2006-10-23
著者
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Fushinobu Shinya
Department of Biotechnology, The University of Tokyo
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HASHIZUME Katsumi
National Research Institute of Brewing
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Fushinobu Shinya
Department Of Biotechnology The University Of Tokyo
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Fushinobu Shinya
Department Of Biotechnology Graduate School Of Agricultural And Life Sciences The University Of Toky
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KOSEKI Takuya
National Research Institute of Brewing
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TAKAHASHI Kenji
Graduate School of Biosphere Science, Hiroshima University
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HANDA Takashi
Suishin-Yamane Honten Co., Ltd.
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YAMANE Yuichi
Suishin-Yamane Honten Co., Ltd.
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Yamane Yuichi
Suishin-yamane Honten Co. Ltd.
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Fushinobu Shinya
Dep. Of Biotechnology The Univ. Of Tokyo
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Handa Takashi
Suishin-yamane Honten Co. Ltd.
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Takahashi Kenji
Graduate School Of Biosphere Science Hiroshima University
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Yamane Yuichi
Suishin Yamane Honten Co., Ltd.
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