Cation-π Interactions Contribute to Substrate Recognition in γ-Butyrobetaine Hydroxylase Catalysis.
Chemistry
; 22(4): 1270-6, 2016 Jan 22.
Article
em En
| MEDLINE
| ID: mdl-26660433
ABSTRACT
γ-Butyrobetaine hydroxylase (BBOX) is a non-heme Fe(II) - and 2-oxoglutarate-dependent oxygenase that catalyzes the stereoselective hydroxylation of an unactivated C-H bond of γ-butyrobetaine (γBB) in the final step of carnitine biosynthesis. BBOX contains an aromatic cage for the recognition of the positively charged trimethylammonium group of the γBB substrate. Enzyme binding and kinetic analyses on substrate analogues with P and As substituting for N in the trimethylammonium group show that the analogues are good BBOX substrates, which follow the efficiency trend N(+) >P(+) >As(+). The results reveal that an uncharged carbon analogue of γBB is not a BBOX substrate, thus highlighting the importance of the energetically favorable cation-π interactions in productive substrate recognition.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Betaína
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Carnitina
/
Cátions
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Gama-Butirobetaína Dioxigenase
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Compostos de Amônio Quaternário
Idioma:
En
Revista:
Chemistry
Ano de publicação:
2016
Tipo de documento:
Article