tailieunhanh - Báo cáo khoa học: Studies on structure–function relationships of indolepyruvate decarboxylase from Enterobacter cloacae, a key enzyme of the indole acetic acid pathway

Enterobacter cloacae, isolated from the rhizosphere of cucumbers, produces large amounts of indole-3-acetic acid. Indolepyruvate decarboxylase, the key enzyme in the biosynthetic pathway of indole-3-acetic acid, catalyses the formation of indole-3-acetaldehyde and carbon dioxide from indole-3-pyruvic acid. The enzyme requires the cofac-tors thiamine diphosphate andmagnesium ions for catalytic activity. Recombinant indolepyruvate decarboxylase was purified from the host Escherichia coli strain JM109 | Eur. J. Biochem. 270 2322-2331 2003 FEBS 2003 doi Studies on structure-function relationships of indolepyruvate decarboxylase from Enterobacter cloacae a key enzyme of the indole acetic acid pathway Anja Schiitz1 Ralph Golbik1 Kai Tittmann1 Dmitri I. Svergun2 3 Michel H. J. Koch2 Gerhard Hiibner1 and Stephan Konig1 1Institut fur Biochemie Fachbereich BiochemiejBiotechnologie Martin-Luther-Universitat Halle-Wittenberg Halle Germany 2European Molecular Biology Laboratory Hamburg Outstation Hamburg Germany 3Institute of Crystallography Russian Academy of Sciences Moscow Russia Enterobacter cloacae isolated from the rhizosphere of cucumbers produces large amounts of indole-3-acetic acid. Indolepyruvate decarboxylase the key enzyme in the biosynthetic pathway of indole-3-acetic acid catalyses the formation of indole-3-acetaldehyde and carbon dioxide from indole-3-pyruvic acid. The enzyme requires the cofactors thiamine diphosphate and magnesium ions for catalytic activity. Recombinant indolepyruvate decarboxylase was purified from the host Escherichia coli strain JM109. Specificity of the enzyme for the substrates indole-3-pyruvic acid pyruvic acid benzoylformic acid and seven benzoylformic acid analogues was investigated using a continuous optical assay. Stopped-flow kinetic data showed no indication for substrate activation in the decarboxylation reaction of indole-3-pyruvic acid pyruvic acid or benzoylformic acid. Size exclusion chromatography and small angle X-ray solution scattering experiments suggested the tetramer as the catalytically active state and a pH-dependent subunit association equilibrium. Analysis of the kinetic constants of the benzoylformic acid analogues according to Hansch et al. Hansch C. Leo A. Unger . Kim . Nikaitani D Lien . 1973 J. Med. Chem. 16 1207-1216 and comparison with indole-3-pyruvic acid conversion by pyruvate decarboxylases from Saccharomyces cerevisiae and Zymomonas mobilis provided some .

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