The Biocatalytic Potential of Aromatic Ammonia–Lyase from <i>Loktanella atrilutea</i>
作者:R. B. Tomoiaga、G. Ágoston、K. Boros、L. C. Nagy、M. I. Toşa、C. Paizs、L. C. Bencze
DOI:10.1002/cbic.202400011
日期:——
The aromatic ammonia–lyase from Loktanella atrilutea (LaAAL) displays a high activity towards 3,4-dimethoxy trans–cinnamic acid, with a surprisingly diminished activity towards natural AAL substrates. Under the optimal reaction conditions LaAAL exhibited versatility for the transformation of various cinnamic acids. While LaAAL might be classified as a tyrosine ammonia-lyase (TAL, E.C. 4.3.1.23), its
来自Loktanella atrirudea ( La AAL) 的芳香氨裂解酶对 3,4-二甲氧基反式肉桂酸表现出高活性,而对天然 AAL 底物的活性却出人意料地降低。在最佳反应条件下, La AAL 表现出多种肉桂酸转化的多功能性。虽然La AAL 可能被归类为酪氨酸氨裂解酶(TAL,EC 4.3.1.23),但其强烈独特的属性表明其在非天然苯丙氨酸的转化中发挥着重要作用。