Structure of the imine reductase from Ajellomyces dermatitidis in three crystal forms.
Acta Crystallogr F Struct Biol Commun
; 79(Pt 9): 224-230, 2023 Sep 01.
Article
em En
| MEDLINE
| ID: mdl-37581897
ABSTRACT
The NADPH-dependent imine reductase from Ajellomyces dermatitidis (AdRedAm) catalyzes the reductive amination of certain ketones with amine donors supplied in an equimolar ratio. The structure of AdRedAm has been determined in three forms. The first form, which belongs to space group P3121 and was refined to 2.01â
Å resolution, features two molecules (one dimer) in the asymmetric unit in complex with the redox-inactive cofactor NADPH4. The second form, which belongs to space group C21 and was refined to 1.73â
Å resolution, has nine molecules (four and a half dimers) in the asymmetric unit, each complexed with NADP+. The third form, which belongs to space group P3121 and was refined to 1.52â
Å resolution, has one molecule (one half-dimer) in the asymmetric unit. This structure was again complexed with NADP+ and also with the substrate 2,2-difluoroacetophenone. The different data sets permit the analysis of AdRedAm in different conformational states and also reveal the molecular basis of stereoselectivity in the transformation of fluorinated acetophenone substrates by the enzyme.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oxirredutases
/
Blastomyces
Idioma:
En
Revista:
Acta Crystallogr F Struct Biol Commun
Ano de publicação:
2023
Tipo de documento:
Article
País de afiliação:
Reino Unido