| Title: | Biochemical and structural characterization of benzenoid carboxyl methyltransferases involved in floral scent production in Stephanotis floribunda and Nicotiana suaveolens |
| Author(s): | Pott MB; Hippauf F; Saschenbrecker S; Chen F; Ross J; Kiefer I; Slusarenko A; Noel JP; Pichersky E; Effmert U; Piechulla B; |
| Address: | "Department of Biological Sciences, University of Rostock, 18059 Rostock, Germany" |
| ISSN/ISBN: | 0032-0889 (Print) 1532-2548 (Electronic) 0032-0889 (Linking) |
| Abstract: | "Flower-specific benzenoid carboxyl methyltransferases from Stephanotis floribunda and Nicotiana suaveolens were biochemically and structurally characterized. The floral scents of both these species contain higher levels of methyl benzoate and lower levels of methyl salicylate. The S. floribunda enzyme has a 12-fold lower K(m) value for salicylic acid (SA) than for benzoic acid (BA), and results of in silico modeling of the active site of the S. floribunda enzyme, based on the crystal structure of Clarkia breweri salicylic acid methyltransferase (SAMT), are consistent with this functional observation. The enzyme was therefore designated SAMT. The internal concentration of BA in S. floribunda flowers is three orders of magnitude higher than the SA concentration, providing a rationale for the observation that these flowers synthesize and emit more methyl benzoate than methyl salicylate. The N. suaveolens enzyme has similar K(m) values for BA and SA, and the in silico modeling results are again consistent with this in vitro observation. This enzyme was therefore designated BSMT. However, the internal concentration of BA in N. suaveolens petals was also three orders of magnitude higher than the concentration of SA. Both S. floribunda SAMT and N. suaveolens BSMT are able to methylate a range of other benzenoid-related compounds and, in the case of S. floribunda SAMT, also several cinnamic acid derivatives, an observation that is consistent with the larger active site cavity of each of these two enzymes compared to the SAMT from C. breweri, as shown by the models. Broad substrate specificity may indicate recent evolution or an adaptation to changing substrate availability" |
| Keywords: | "Amino Acid Sequence Asteraceae/classification/*enzymology Benzoates/metabolism Conserved Sequence Flowers/enzymology Models, Molecular Molecular Sequence Data *Odorants Protein Conformation Protein Methyltransferases/chemistry/genetics/*metabolism Salicyl;" |
| Notes: | "MedlinePott, Marcella B Hippauf, Frank Saschenbrecker, Sandra Chen, Feng Ross, Jeannine Kiefer, Ingrid Slusarenko, Alan Noel, Joseph P Pichersky, Eran Effmert, Uta Piechulla, Birgit eng Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. 2004/08/18 Plant Physiol. 2004 Aug; 135(4):1946-55. doi: 10.1104/pp.104.041806. Epub 2004 Aug 13" |
