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Literature summary for 1.14.13.235 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
Search for more literature for 1.14.13.235

Organism

Organism UniProt Comment Textmining
Pseudomonas putida B0FXI0
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Pseudomonas putida 1290 B0FXI0
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(indol-3-yl)acetate + NADH + H+ + O2
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 Pseudomonas putida (2-hydroxyindol-3-yl)acetate + NAD+ + H2O
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 ?
(indol-3-yl)acetate + NADH + H+ + O2
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 Pseudomonas putida 1290 (2-hydroxyindol-3-yl)acetate + NAD+ + H2O
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 ?
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 ?
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 ?
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 ?
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 ?

Expression

Organism Comment Expression
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

General Information Comment Organism
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