Crystal Structures of Pyruvate Phosphate Dikinase from Maize Revealed an Alternative Conformation in the Swiveling-Domain Motion,-Reference-Cited by-同舟云学术

Crystal Structures of Pyruvate Phosphate Dikinase from Maize Revealed an Alternative Conformation in the Swiveling-Domain Motion,

Published:2004-12-31 Issue:4 Volume:44 Page:1136-1144
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Nakanishi Tsugumi¹,Nakatsu Toru¹,Matsuoka Makoto¹,Sakata Kanzo¹,Kato Hiroaki¹

Affiliation:

1. Kinetic Crystallography Research Team, Membrane Dynamics Research Group, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan, Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Kyoto University, 46-29 Yoshida-Shimo-Adachi, Kyoto 606-8501, Japan, Institute for Chemical Research, Kyoto University, Gokasyo, Uji, Kyoto 611-0011, Japan, and BioScience Center, Nagoya University, Nagoya, Aichi 464-8601, Japan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi0484522

Reference32 articles.

1. The mode of triple phosphoryl group transfer in pyruvate phosphate dikinase catalysis. Demonstration of the intermediacy of pyrophosphorylated and phosphorylated enzyme species

2. Primary structure of maize pyruvate, orthophosphate dikinase as deduced from cDNA sequence.

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