Present address: Faculty of Life Science, Toyo University, Izumino 1-1-1, Itakura, Gunma 374-0193, Japan.
Rice CYP734As function as multisubstrate and multifunctional enzymes in brassinosteroid catabolism
Version of Record online: 26 APR 2011
© 2011 The Authors. The Plant Journal © 2011 Blackwell Publishing Ltd
The Plant Journal
Volume 67, Issue 1, pages 1–12, July 2011
How to Cite
Sakamoto, T., Kawabe, A., Tokida-Segawa, A., Shimizu, B.-i., Takatsuto, S., Shimada, Y., Fujioka, S. and Mizutani, M. (2011), Rice CYP734As function as multisubstrate and multifunctional enzymes in brassinosteroid catabolism. The Plant Journal, 67: 1–12. doi: 10.1111/j.1365-313X.2011.04567.x
- Issue online: 27 JUN 2011
- Version of Record online: 26 APR 2011
- Accepted manuscript online: 21 MAR 2011 01:03PM EST
- Received 22 December 2010; revised 25 February 2011; accepted 4 March 2011; published online 26 April 2011.
Figure S1. High-performance LC analysis of the products from the rice CYP734A2 assay with 22,23-hydroxylated brassinosteroid s as substrates.
Figure S2. Total ion chromatogram of products from the CYP734A2 assay with 22-hydroxylated brassinosteroid s as substrates.
Figure S3. Gas chromatography retention time and mass spectrum of products from the CYP734A2 assay with castasterone as substrate.
Figure S4. Multiple alignment of amino acid sequences of the CYP734A subfamily from various plants.
Table S1. Amino acid sequence identities among CYP734A enzymes.
Table S2. Primer sequences used in CYP734A cDNA cloning.
Table S3. Primer sequences used in expression analysis.
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