title: Floral benzenoid carboxyl methyltransferases: from in vitro to in planta function.
abstract: Benzenoid carboxyl methyltransferases synthesize methyl esters (e.g., methyl benzoate and methyl salicylate), which are constituents of aromas and scents of many plant species and play important roles in plant communication with the surrounding environment. Within the past five years, eleven such carboxyl methyltransferases were isolated and most of them were comprehensively investigated at the biochemical, molecular and structural level. Two types of enzymes can be distinguished according to their substrate preferences: the SAMT-type enzymes isolated from Clarkia breweri, Stephanotis floribunda, Antirrhinum majus, Hoya carnosa, and Petunia hybrida, which have a higher catalytic efficiency and preference for salicylic acid, while BAMT-type enzymes from A. majus, Arabidopsis thaliana, Arabidopsis lyrata, and Nicotiana suaveolens prefer benzoic acid. The elucidation of C. breweri SAMT's three-dimensional structure allowed a detailed modelling of the active sites of the carboxyl methyltransferases and revealed that the SAM binding pocket is highly conserved among these enzymes while the methyl acceptor binding site exhibits some variability, allowing a classification into SAMT-type and BAMT-type enzymes. The analysis of expression patterns coupled with biochemical characterization showed that these carboxyl methyltransferases are involved either in floral scent biosynthesis or in plant defense responses. While the latter can be induced by biotic or abiotic stress, the genes responsible for floral scent synthesis exhibit developmental and rhythmic expression pattern. The nature of the product and efficiency of its formation in planta depend on the availability of substrates, the catalytic efficiency of the enzyme toward benzoic acid and/or salicylic acid, and the transcriptional, translational, and post-translational regulation at the enzyme level. The biochemical properties of benzenoid carboxyl methyltransferases suggest that the genes involved in plant defenses might represent the ancestor for the presently existing floral genes which during evolution gained different expression profiles and encoded enzymes with the ability to accept structurally similar substrates.
authors.affiliation: Department of Biological Sciences, University of Rostock, Albert-Einstein-Str. 3, D-18059 Rostock, Germany.
authors.forename: Uta
authors.initials: U
authors.lastname: Effmert
authors.forename: Sandra
authors.initials: S
authors.lastname: Saschenbrecker
authors.forename: Jeannine
authors.initials: J
authors.lastname: Ross
authors.forename: Florence
authors.initials: F
authors.lastname: Negre
authors.forename: Chris M
authors.initials: CM
authors.lastname: Fraser
authors.forename: Joseph P
authors.initials: JP
authors.lastname: Noel
authors.forename: Natalia
authors.initials: N
authors.lastname: Dudareva
authors.forename: Birgit
authors.initials: B
authors.lastname: Piechulla
mesh_terms: D000595:Amino Acid Sequence; D001565:Benzoates / Q000378:metabolism; D035264:Flowers / Q000201:enzymology*; D015870:Gene Expression; D008780:Methyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D010802:Phylogeny; D010944:Plants / Q000201:enzymology* / Q000235:genetics; D012459:Salicylates / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D001565:Benzoates; D012459:Salicylates; C044605:methyl benzoate; D008780:Methyltransferases; C033069:methyl salicylate