Department of Biomolecular Science, Faculty of Science, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan.
Multidisciplinary Science Cluster, Research and Education Faculty, Kochi University, B200 Monobe, Nankoku, Kochi 783-8502, Japan.
Acta Crystallogr F Struct Biol Commun. 2023 Feb 1;79(Pt 2):31-37. doi: 10.1107/S2053230X23000304. Epub 2023 Feb 2.
D-Threonine aldolase (DTA) is a pyridoxal-5'-phosphate-dependent enzyme which catalyzes the reversible aldol reaction of glycine with a corresponding aldehyde to yield the D-form β-hydroxy-α-amino acid. This study produced and investigated the crystal structure of DTA from Chlamydomonas reinhardtii (CrDTA) at 1.85 Å resolution. To our knowledge, this is the first report on the crystal structure of eukaryotic DTA. Compared with the structure of bacterial DTA, CrDTA has a similar arrangement of active-site residues. On the other hand, we speculated that some non-conserved residues alter the affinity for substrates and inhibitors. The structure of CrDTA could provide insights into the structural framework for structure-guided protein engineering studies to modify reaction selectivity.
D-苏氨酸醛缩酶（DTA）是一种依赖吡哆醛-5'-磷酸的酶，它催化甘氨酸与相应醛的可逆醛缩反应，生成 D 型β-羟基-α-氨基酸。本研究产生并研究了莱茵衣藻（CrDTA）的 DTA 的晶体结构，分辨率为 1.85Å。据我们所知，这是真核 DTA 晶体结构的首次报道。与细菌 DTA 的结构相比，CrDTA 的活性位点残基排列相似。另一方面，我们推测一些非保守残基改变了对底物和抑制剂的亲和力。CrDTA 的结构可以为基于结构的蛋白质工程研究提供结构框架，以改变反应选择性。
