日本結晶学会誌
Online ISSN : 1884-5576
Print ISSN : 0369-4585
ISSN-L : 0369-4585
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1つの酵素が2つの反応を触媒するしくみ
西増 弘志伏信 進矢若木 高善
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2012 年 54 巻 2 号 p. 113-118

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Unlike ordinary enzymes, fructose-1,6-bisphosphate (FBP) aldolase/phosphatase (FBPA/P) catalyzes two distinct reactions : (1) the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate to FBP, and (2) the dephosphorylation of FBP to fructose-6-phosphate. We solved the crystal structures of FBPA/P in complex with DHAP (its aldolase form) and FBP (its phosphatase form). The crystal structures revealed that FBPA/P exhibits the dual activities through a dramatic conformational change in the active-site architecture. Our findings expand the conventional concept that one enzyme catalyzes one reaction.

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© 2012 日本結晶学会
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