Acyltransferases in plants: a good time to be BAHD

Evolutionarily Distinct BAHD N-acyltransferases are Responsible for Natural Variation of Aromatic Amine Conjugates in Rice

“…Phylogenetic relationships among the BAHD acyltransferases were then investigated by reconstructing the phylogenetic tree ( Figure 4A), using a neighbor-joining algorithm, based on the amino acid sequences of our candidates and a collection of 27 reported plant BAHD acyltransferases (D'Auria, 2006;Grienenberger et al, 2009;Luo et al, 2009;Onkokesung et al, 2012;Chen et al, 2014;Dong et al, 2015). The resulting phylogenetic tree is consistent with that of Tuominen et al (2011), an updated version of that from D'Auria, who sorted biochemically characterized BAHD acyltransferases into eight major clades (A) An unrooted phylogenetic tree was constructed as described in Methods.…”

“…Clade IV, which had only five members in the tree of Tuominen et al (2011), was further expanded into IVa and IVb in following analysis ( Figure 4A). Candidates for four out of the five loci identified grouped in clade IV, which is enriched in monocot genes, while candidates for the remaining locus were grouped into clade Vb, which is mainly made up of enzymes closely related to hydroxycinnamoyl transferases responsible for the biosynthesis of chlorogenic acid and monolignols (D'Auria, 2006). Closer examination of the phylogeny in clade IVa revealed that Os04g56900 lies next to HvACT and Os04g56910, two agmatine coumaroyl transferase from barley and rice, respectively, consistent with the strong association between the Os04g56900 locus and the content of agmatine derivatives (Burhenne et al, 2003;Chen et al, 2014).…”

“…Analysis of their amino acid sequences revealed that all these enzymes belong to the GCN5-related N-acetyltransferases (GNAT) protein family, which also includes mammalian spermidine/spermine acetyltransferase and several microbial antibiotic N-acetyltransferases (Lu et al, 1996;Farmer et al, 1999;Kang et al, 2006). In contrast to the situation where PAs of arylamine moieties are mainly biosynthesized by the GNAT family of enzymes, the biosynthesis of the aliphatic type of phenolamides is exclusively the domain of BAHD acyltransferases (D'Auria, 2006;Bassard et al, 2010). The BAHD acyltransferase family was named according to the first letter of each of the first four biochemically characterized enzymes of this family BEAT (benzoyl alcohol O-acetyltransferase), AHCT (anthocyanin O-hydroxycinnamoyl transferase), HCBT (anthranilate N-hydroxycinnamoyl/benzoyl transferase), and DAT (deacetyl vindoline 4-O-acetyltransferase) (St-Pierre and De Luca, 2000).…”

“…The BAHD acyltransferase family was named according to the first letter of each of the first four biochemically characterized enzymes of this family BEAT (benzoyl alcohol O-acetyltransferase), AHCT (anthocyanin O-hydroxycinnamoyl transferase), HCBT (anthranilate N-hydroxycinnamoyl/benzoyl transferase), and DAT (deacetyl vindoline 4-O-acetyltransferase) (St-Pierre and De Luca, 2000). So far, enzymes involved in the biosynthesis of PAs have been identified from three (I, IV, and V) of the five clades of BAHD acyltransferases (D'Auria, 2006;Yu et al, 2009;Tuominen et al, 2011). ACTs (agmatine coumaroyl transferases) were characterized in barley and in Arabidopsis thaliana (Burhenne et al, 2003;Muroi et al, 2009).…”

Two Herbivore-Induced Cytochrome P450 Enzymes CYP79D6 and CYP79D7 Catalyze the Formation of Volatile Aldoximes Involved in Poplar Defense

“…Terpene synthases, for example, frequently produce many different products from a single substrate (e.g., Degenhardt et al, 2009), while methyltransferases and acyltransferases involved in the formation of volatile esters often accept several alcohols as substrates (Effmert et al, 2005;D'Auria, 2006). Thus, using a limited number of different enzymes, plants are able to produce complex volatile blends comprising dozens of compounds.…”