Institut für Pharmazeutische Biologie und Biotechnologie , Philipps-Universität Marburg , Robert-Koch Straße 4 , Marburg 35037 , Germany.
Org Lett. 2019 Jan 18;21(2):498-502. doi: 10.1021/acs.orglett.8b03793. Epub 2019 Jan 2.
Nonribosomal peptide synthetase (NRPS)-like enzymes comprising A-T-TE architectures catalyze the dimerization of α-keto carboxylic acids leading to the formation of hydroxybenzoquinones or lactones. Domain change experiments with five enzymes revealed that A and A-T domains of phenyl or 4-hydroxyphenyl pyruvate-using enzymes can be effectively used by the TE domains of other enzymes. Even the A and A-T domains of an indolyl hydroxybenzoquinone synthase were successfully recombined with TE domains of a phenyl and a 4-hydroxyphenyl pyruvate-activating enzyme.
非核糖体肽合成酶（NRPS）样酶包含 A-T-TE 结构，催化 α-酮羧酸的二聚化，导致羟基苯醌或内酯的形成。对五种酶进行的结构域变化实验表明，苯丙酮酸或 4-羟基苯丙酮酸利用酶的 A 和 A-T 结构域可以被其他酶的 TE 结构域有效地利用。甚至吲哚基羟基苯醌合酶的 A 和 A-T 结构域也成功地与苯丙酮酸和 4-羟基苯丙酮酸激活酶的 TE 结构域重组。
