Structure of the flavoprotein tryptophan 2-monooxygenase, a key enzyme in the formation of galls in plants.

ABSTRACT: The flavoprotein tryptophan 2-monooxygenase catalyzes the oxidative decarboxylation of tryptophan to yield indole-3-acetamide. This is the initial step in the biosynthesis of the plant growth hormone indole-acetic acid by bacterial pathogens that cause crown gall and related diseases. The structure of the enzyme from Pseudomonas savastanoi has been determined by X-ray diffraction methods to a resolution of 1.95 Å. The overall structure of the protein shows that it has the same fold as members of the monoamine oxidase family of flavoproteins, with the greatest similarities to the l-amino acid oxidases. The location of bound indole-3-acetamide in the active site allows identification of residues responsible for substrate binding and specificity. Two residues in the enzyme are conserved in al

SUBMITTER: Gaweska HM 

PROVIDER: S-EPMC3635830 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature