Volume 60, Issue 1 pp. 193-194

Purification, crystallization and preliminary X-ray diffraction studies on pyruvate phosphate dikinase from maize

Pyruvate phosphate dikinase

Tsugumi Nakanishi

Tsugumi Nakanishi

Kinetic Crystallography Research Team, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan

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Yasushi Ohki

Yasushi Ohki

Kinetic Crystallography Research Team, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan

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Jun'ichi Oda

Jun'ichi Oda

Kinetic Crystallography Research Team, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan

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Makoto Matsuoka

Makoto Matsuoka

Kinetic Crystallography Research Team, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan

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Kanzo Sakata

Kanzo Sakata

Kinetic Crystallography Research Team, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan

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Hiroaki Kato

Hiroaki Kato

Kinetic Crystallography Research Team, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan

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First published: 09 March 2004
Citations: 1
Hiroaki Kato, Kinetic Crystallography Research Team, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan. E-mail: [email protected]

Abstract

Pyruvate phosphate dikinase (PPDK) from maize catalyzes the reversible conversion of ATP, orthophosphate and pyruvate to AMP, pyrophosphate and PEP. In higher plants, this enzyme is believed to be involved in the C4 dicarboxylic acid pathway. PPDK was crystallized by the vapour-diffusion method using polyethylene glycol as a precipitant. The crystals belong to the orthorhombic space group C2, with unit-cell parameters a = 108.2, b = 100.2, c = 108.4 Å, β = 96.5°, and diffract to 2.3 Å using SPring-8 synchrotron radiation.

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