Origin of the enantioselectivity of alcohol dehydrogenase.
Journal
Physical chemistry chemical physics : PCCP
ISSN: 1463-9084
Titre abrégé: Phys Chem Chem Phys
Pays: England
ID NLM: 100888160
Informations de publication
Date de publication:
22 Nov 2023
22 Nov 2023
Historique:
medline:
27
11
2023
pubmed:
13
11
2023
entrez:
13
11
2023
Statut:
epublish
Résumé
Alcohol dehydrogenases (ADH) are a family of enzymes that catalyse the interconversion between ketones/aldehydes and alcohols in the presence of NADPH cofactor. It is challenging to desymmetrise the substituted cyclopentane-1,3-dione by engineering an ADH, while the reaction mechanism of the metal independent ADH remains elusive. Here we measured the conversion of a model substrate 2-benzyl-2-methylcyclopentane-1,3-dione by
Substances chimiques
Alcohol Dehydrogenase
EC 1.1.1.1
Alcohols
0
Aldehydes
0
Ketones
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM