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Literature summary extracted from

  • Scott, J.C.; Greenhut, I.V.; Leveau, J.H.
    Functional characterization of the bacterial iac genes for degradation of the plant hormone indole-3-acetic acid (2013), J. Chem. Ecol., 39, 942-951.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.235 Pseudomonas putida B0FXI0
-
-
1.14.13.235 Pseudomonas putida 1290 B0FXI0
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.235 (indol-3-yl)acetate + NADH + H+ + O2
-
Pseudomonas putida (2-hydroxyindol-3-yl)acetate + NAD+ + H2O
-
?
1.14.13.235 (indol-3-yl)acetate + NADH + H+ + O2
-
Pseudomonas putida 1290 (2-hydroxyindol-3-yl)acetate + NAD+ + H2O
-
?
1.14.13.235 additional information enzyme catalyzes the hydroxylation of position 3 of the indole ring to produce indoxyl, which in the presence of oxygen dimerizes to form indigo Pseudomonas putida ?
-
?
1.14.13.235 additional information enzyme catalyzes the hydroxylation of position 3 of the indole ring to produce indoxyl, which in the presence of oxygen dimerizes to form indigo Pseudomonas putida 1290 ?
-
?

Expression

EC Number Organism Comment Expression
1.14.13.235 Pseudomonas putida with indole-3-acetate as the sole source of carbon and energy, the expression of IacA is more than 2 orders of magnitude greater than with glucose up

General Information

EC Number General Information Comment Organism
1.14.13.235 physiological function enzyme catalyzes the first step in degradation of the plant hormone indole-3-acetate. Transformation of Pseudomonas putida KT2440, which cannot degrade IAA, with the Iac gene cluster confers the ability to grow on indole-3-acetate as a sole source of carbon and energy, but not the ability to chemotaxis towards indole-3-acetate Pseudomonas putida