Structure of the thermophilic l-Arabinose isomerase from Geobacillus kaustophilus reveals metal-mediated intersubunit interactions for activity and thermostability

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• 作者：Jin Myung Choi^a ; ¹ ; Yong-Jik Lee^b ; ¹ ; Thinh-Phat Cao^a ; Sun-Mi Shin^b ; Min-Kyu Park^b ; Han-Seung Lee^c ; Eric di Luccio^d ; Seong-Bo Kim^e ; Sang-Jae Lee^c ; Sang Jun Lee^f ; Sung Haeng Lee^a ; ^{sunglee@chosun.ac.kr" class="auth_mail" title="E-mail the corresponding author} ; Dong-Woo Lee^b ; ^{leehicam@knu.ac.kr" class="auth_mail" title="E-mail the corresponding author}
• 关键词：l-arabinose isomerase ; Crystal structure ; Intersubunit interaction ; Substrate specificity ; Thermostability
• 刊名：Archives of Biochemistry and Biophysics
• 出版年：2016
• 出版时间：15 April 2016
• 年：2016
• 卷：596
• 期：Complete
• 页码：51-62
• 全文大小：4247 K

文摘

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d="p0010">Thermophilic AI is an enzyme that catalyzes the isomerization of aldose to ketose.

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d="p0015">The first crystal structures of the apo and holo forms of thermophilic GKAI were determined at high resolutions.

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d="p0020">Hexameric GKAI forms the substrate-binding pockets through metal-mediated intersubunit interactions.

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d="p0025">The l-arabitol-Mn²⁺-GKAI complex structure suggests a metal-mediated isomerization reactions at elevated temperatures.

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