INDOLEPYRUVATE DECARBOXYLASE OF M. extorquens AM1
1443
Nadalig, T., Pagni, M., Penny, C., Peyraud, R., Robinson,
D. G., Roche, D., Rouy, Z., Saenampechek, C., Salvignol,
G., Vallenet, D., Wu, Z., Marx, C. J., Vorholt, J. A., Olson,
M. V., Kaul, R., Weissenbach, J., Medigue, C., and
Lidstrom, M. E. (2009) PLoS ONE, 4, e5584;
doi:10.1371/journal.pone.0005584.
thase large subunit (ACS42655, ACS42922), pyruvate
decarboxylase/oxidase (ACS39317), and oxalylꢀCoA
decarboxylase (ACS38885) that can be involved in IAA
biosynthesis. Eventually, other key enzymes of auxin
biosynthesis (tryptophan decarboxylase, tryptophan 2ꢀ
monooxygenase) in the M. extorquens AM1 genome were
not detected and, respectively, alternative IAA biosynthetꢀ
ic pathways in M. extorquens are not known yet.
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707ꢀ735.
Thus, for the first time for methylotrophs we have
showed that the ipdC gene encodes indolepyruvate decarꢀ
boxylase by using the recombinant enzyme IpdC as well
as the mutant with deletion in the ipdC gene and the comꢀ
plemented strain. Although the protein from
Methylobacterium phylogenetically belongs to the benꢀ
zoylformate decarboxylases, the enzyme has catalytic
properties of indolepyruvate decarboxylase, which was
first demonstrated for this group of enzymes. Finally,
mutational analysis also implied an alternative pathway of
IAA biosynthesis operates in M. extorquens AM1, which is
a subject of our further investigation.
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The authors are grateful to V. I. Tishkov (Chemical
Enzymology Department, Chemistry Faculty, M. V.
Lomonosov Moscow State University) for useful advice
in the kinetic data interpretation.
This work was supported by grants of the Ministry of
Education and Science of the Russian Federation (RNP
2.1.1/605) and the Russian Foundation for Basic
Research (10ꢀ04ꢀ00808ꢀa).
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BIOCHEMISTRY (Moscow) Vol. 75 No. 12 2010