The Nitrilase ZmNIT2 Converts Indole-3-Acetonitrile to Indole-3-Acetic Acid | Zendy

Woong June Park | Zendy; Verena Kriechbaumer | Zendy; Axel Müller | Zendy; Markus Piotrowski | Zendy; Robert Meeley | Zendy; Alfons Gierl | Zendy; Erich Glawischnig | Zendy

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The Nitrilase ZmNIT2 Converts Indole-3-Acetonitrile to Indole-3-Acetic Acid

Author(s) -

Woong June Park,

Verena Kriechbaumer,

Axel Müller,

Markus Piotrowski,

Robert Meeley,

Alfons Gierl,

Erich Glawischnig

Publication year - 2003

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.103.026609

Subject(s) - nitrilase , indole test , auxin , biochemistry , arabidopsis , indole 3 acetic acid , chemistry , tryptophan , adenylylation , acetonitrile , gene , biosynthesis , stereochemistry , amino acid , biology , hydrolysis , organic chemistry , mutant

We isolated two nitrilase genes, ZmNIT1 and ZmNIT2, from maize (Zea mays) that share 75% sequence identity on the amino acid level. Despite the relatively high homology to Arabidopsis NIT4, ZmNIT2 shows no activity toward β-cyano-alanine, the substrate of Arabidopsis NIT4, but instead hydrolyzes indole-3-acetonitrile (IAN) to indole-3-acetic acid (IAA). ZmNIT2 converts IAN to IAA at least seven to 20 times more efficiently than AtNIT1/2/3. Quantitative real-time polymerase chain reaction revealed the gene expression of both nitrilases in maize kernels where high concentrations of IAA are synthesized tryptophan dependently. Nitrilase protein and endogenous nitrilase activity are present in maize kernels together with the substrate IAN. These results suggest a role for ZmNIT2 in auxin biosynthesis.

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