Corrigendum to “Structure determinants and substrate recognition of serine carboxypeptidase‐like acyltransferases from plant secondary metabolism” [FEBS Lett. 580 (2006) 6366–6374]

An unfortunate error occurred in Fig. 2 . This figure, which appears in black/white, should have been printed in colour. The correct Fig. 2 is as follows: Fig. 2 Alignment of amino acid sequences of SCPL acyltransferases with those of serine carboxypeptidases used as templates for structure modeling. N-terminal leader peptides are removed. Fully conserved residues are shaded in black. Amino acid residues forming the catalytic triad are depicted in yellow. Residues are marked that are involved in substrate recognition (hydrogen bond network, blue crosses) and stabilization of the transition state (oxyanion hole, green asterisks in SMT/SCT above and in CPY below the sequences). Secondary structure elements are shown for AtSMT and CPY. Endopeptides cleaved out during enzyme maturation are crossed out. AtSMT (Arabidopsis thaliana SMT; GenBank accession number AF275313) was aligned with BnSCT (Brassica napus SCT; GenBank accession number AY383718), AtSCT (Arabidopsis thaliana SCT; GenBank accession number AY033947), HPP (human protective protein; NM000308.1), Kex1p (NC001139.7) and CPY (Saccharomyces carboxypeptidase Y; NC001145.2) by CLUSTALW using the BLOSUM62 matrix.