An article An L-threonine aldolase for asymmetric synthesis of beta-hydroxy-alpha-amino acids WOS:000573599600004 published article about DYNAMIC KINETIC RESOLUTION; ESCHERICHIA-COLI; SUBSTRATE; MECHANISM in [Wang, Li-Chao; Xu, Lian; Su, Bing-Mei; Lin, Juan] Fuzhou Univ, Coll Chem Engn, Fuzhou 350116, Peoples R China; [Wang, Li-Chao; Xu, Lian; Xu, Xin-Qi; Su, Bing-Mei; Lin, Juan] Fuzhou Univ, Coll Biol Sci & Engn, Fuzhou 350116, Peoples R China in 2020.0, Cited 33.0. Formula: C6H5NO. The Name is 3-Pyridinecarboxaldehyde. Through research, I have a further understanding and discovery of 500-22-1
L-threonine aldolase (LTA) is a PLP-dependent enzyme that can reversibly catalyze aldol reaction of glycine and acetaldehyde to produce beta-hydroxy-alpha-amino acids. In the present work, a putative Ita gene from Actinocorallia herbida (AhLTA) was mined and over-expressed in Escherichia coli BL21 (DE3). The substrate spectrum assay indicated that AhLTA only used glycine as donor substrate and tolerated a wild range of aromatic aldehydes as acceptor substrates. It was found that the type and position of substituents in the aromatic aldehydes exerted a significant impact on the activity and stereoselectivity at beta-carbon of AhLTA. Among those substrates, AhLTA could catalyze glycine and 4-methylsulphonyl benzaldehyde (14a) to produce L-threo-4-methylsulfonylphenylserine ((2S,3R)-14b) with high conversion (94.4%) and moderate stereoselectivity (19% de). By conditional optimization, the de value of (2S, 3R)-14b was improved to 61% and the conversion was 75%. Taken together, our study suggested that AhLTA might be a promising catalyst for producing chiral beta-hydroxy-alpha-amino acids. (C) 2020 Elsevier Ltd. All rights reserved.
Formula: C6H5NO. Bye, fridends, I hope you can learn more about C6H5NO, If you have any questions, you can browse other blog as well. See you lster.
Reference:
Pyridine – Wikipedia,
,Pyridine | C5H5N – PubChem