Enhancing enantioselectivity of Candida antarctica lipase B towards chiral sec-alcohols bearing small substituents through hijacking sequence of A homolog

Autor:	Seongsoon Park, Seonghyeon Yi
Rok vydání:	2021
Předmět:	biology 010405 organic chemistry Stereochemistry Chemistry Organic Chemistry Lipase b 010402 general chemistry biology.organism_classification 01 natural sciences Biochemistry 0104 chemical sciences Local sequence Drug Discovery biology.protein Pseudozyma brasiliensis Candida antarctica Lipase
Zdroj:	Tetrahedron Letters. 75:153186
ISSN:	0040-4039
DOI:	10.1016/j.tetlet.2021.153186
Popis:	Candida antarctica lipase B (CAL-B) exhibits extraordinary enantioselectivity towards most chiral sec-alcohols but not towards sec-alcohols bearing substituents smaller than a propyl group (i.e., (±)-but-3-yn-2-ol (E = 4) and (±)-butan-2-ol (E = 7)). Previously, we reported a homologous enzyme (lipase from Pseudozyma brasiliensis GHG001, PBL) of CAL-B, which exhibited high enantioselectivity of CAL-B towards (±)-but-3-yn-2-ol (E > 200). Based on the result, we hypothesized that the comparison of their local sequence or structure would provide a clue for enhancing the enantioselectivity of CAL-B. In this paper, we report enhancing enantioselectivity of CAL-B towards (±)-but-3-yn-2-ol and (±)-butan-2-ol through the substitution of the local sequence of CAL-B with that of PBL. The sequence-substituted mutant of CAL-B exhibited much higher enantioselectivity towards (±)-but-3-yn-2-ol (E > 200) and (±)-butan-2-ol (E > 25).
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::e3edca02bd47c09e141373dcf9961ed9 https://doi.org/10.1016/j.tetlet.2021.153186 Zobrazit plný text záznamu Full Text from ScienceDirect