tailieunhanh - Báo cáo khoa học: Crystal structure of thiamindiphosphate-dependent indolepyruvate decarboxylase from Enterobacter cloacae, an enzyme involved in the biosynthesis of the plant hormone indole-3-acetic acid

The thiamindiphosphate-dependent enzyme indolepyruvate decarboxylase catalyses the formationof indoleacetaldehyde from indolepyruvate, one step in the indolepyruvate path-way of biosynthesis of the plant hormone indole-3-acetic acid. The crystal structure of this enzyme fromEnterobacter cloacaehasbeendeterminedat A˚ resolutionandrefined to a crystallographic R-factor of (Rfree ). The subunit of indolepyruvate decarboxylase contains three domains of opena/btopology, whichare similar in structure to that of pyruvate decarboxylase. . | Eur. J. Biochem. 270 2312-2321 2003 FEBS 2003 doi Crystal structure of thiamindiphosphate-dependent indolepyruvate decarboxylase from Enterobacter cloacae an enzyme involved in the biosynthesis of the plant hormone indole-3-acetic acid Anja Schiitz1 Tatyana Sandalova2 Stefano Ricagno2 Gerhard Hiibner1 Stephan Konig1 and Gunter Schneider2 Institute of Biochemistry Department of Biochemistry and Biotechnology Martin-Luther-University Halle-Wittenberg Germany 2Division of Molecular Structural Biology Department of Medical Biochemistry and Biophysics Karolinska Institutet Stockholm Sweden The thiamin diphosphate-dependent enzyme indolepyruvate decarboxylase catalyses the formation of indoleacetaldehyde from indolepyruvate one step in the indolepyruvate pathway of biosynthesis of the plant hormone indole-3-acetic acid. The crystal structure of this enzyme from Enterobacter cloacae has been determined at A resolution and refined to a crystallographic R-factor of Rfree . The subunit of indolepyruvate decarboxylase contains three domains of open a b topology which are similar in structure to that of pyruvate decarboxylase. The tetramer has pseudo 222 symmetry and can be described as a dimer of dimers. It resembles the tetramer of pyruvate decarboxylase from Zymomonas mobilis but with a relative difference of 20 in the angle between the two dimers. Active site residues are highly conserved in indolepyruvate pyruvate decarboxylase suggesting that the interactions with the cofactor thiamin diphosphate and the catalytic mechanisms are very similar. The substrate binding site in indolepyruvate decarboxylase contains a large hydrophobic pocket which can accommodate the bulky indole moiety of the substrate. In pyruvate decarboxylases this pocket is smaller in size and allows discrimination of larger vs. smaller substrates. In most pyruvate decarboxylases restriction of cavity size is due to replacement of residues at three positions

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