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The Nitrilase ZmNIT2 converts indole-3-acetonitrile to indole-3-acetic acid.
Plant Physiol. 2003 Oct; 133(2):794-802.PP

Abstract

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 beta-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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Authors+Show Affiliations

Park WJ
Lehrstuhl für Genetik, Technische Universität München, D-85350 Freising, Germany.
Kriechbaumer V
No affiliation info available
Möller A
No affiliation info available
Piotrowski M
No affiliation info available
Meeley RB
No affiliation info available
Gierl A
No affiliation info available
Glawischnig E
No affiliation info available

MeSH

AminohydrolasesCloning, MolecularIndoleacetic AcidsIndolesIsoenzymesRecombinant ProteinsSeedsSubstrate SpecificityZea mays

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

12972653

Citation

Park, Woong June, et al. "The Nitrilase ZmNIT2 Converts Indole-3-acetonitrile to Indole-3-acetic Acid." Plant Physiology, vol. 133, no. 2, 2003, pp. 794-802.
Park WJ, Kriechbaumer V, Möller A, et al. The Nitrilase ZmNIT2 converts indole-3-acetonitrile to indole-3-acetic acid. Plant Physiol. 2003;133(2):794-802.
Park, W. J., Kriechbaumer, V., Möller, A., Piotrowski, M., Meeley, R. B., Gierl, A., & Glawischnig, E. (2003). The Nitrilase ZmNIT2 converts indole-3-acetonitrile to indole-3-acetic acid. Plant Physiology, 133(2), 794-802.
Park WJ, et al. The Nitrilase ZmNIT2 Converts Indole-3-acetonitrile to Indole-3-acetic Acid. Plant Physiol. 2003;133(2):794-802. PubMed PMID: 12972653.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The Nitrilase ZmNIT2 converts indole-3-acetonitrile to indole-3-acetic acid. AU - Park,Woong June, AU - Kriechbaumer,Verena, AU - Möller,Axel, AU - Piotrowski,Markus, AU - Meeley,Robert B, AU - Gierl,Alfons, AU - Glawischnig,Erich, Y1 - 2003/09/04/ PY - 2003/9/16/pubmed PY - 2004/1/24/medline PY - 2003/9/16/entrez SP - 794 EP - 802 JF - Plant physiology JO - Plant Physiol VL - 133 IS - 2 N2 - 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 beta-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. SN - 0032-0889 UR - https://www.unboundmedicine.com/medline/citation/12972653/The_Nitrilase_ZmNIT2_converts_indole_3_acetonitrile_to_indole_3_acetic_acid_ DB - PRIME DP - Unbound Medicine ER -