著者

松村 浩由

出版者

The Crystallographic Society of Japan

雑誌

日本結晶学会誌 (ISSN:03694585)

巻号頁・発行日

vol.50, no.4, pp.245-253, 2008-08-29 (Released:2010-09-30)

参考文献数

27

被引用文献数

1

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Phosphoenolpyruvate carboxylase (PEPC) and ribulose 1, 5-bisphosphate carboxylase/oxygenase (Rubisco) play pivotal roles in CO2 fixation. Both of the enzymes are involved in photosynthetic efficiency of plants. Here, we report the crystal structures of PEPC and Rubisco; the inactivated Escherichia coli PEPC complexed with L-aspartate, the activated maize PEPC complexed with a sulfate, the Chlamydomonas Rubisco complexed with transition state analogue, and Galdieria Rubisco complexed with a sulfate. X-ray crystallographic analysis and site-directed mutagenesis studies revealed the allosteric regulation and the reaction mechanism of PEPC. The crystallographic studies on Rubisco provided detailed understanding of activity and regulation in Rubisco.