Identification of a lysine 4-hydroxylase from the glidobactin biosynthesis and evaluation of its biocatalytic potential.
Org Biomol Chem
; 17(7): 1736-1739, 2019 02 13.
Article
em En
| MEDLINE
| ID: mdl-30320324
ABSTRACT
We present the functional characterization of GlbB, a lysine 4-hydroxylase from the glidobactin biosynthetic gene cluster. Despite its narrow substrate specificity, GlbB is able to catalyze the hydroxylation of l-lysine with excellent total turnover number and complete regio- and diastereoselectivity. The synthetic utility of GlbB is illustrated by its use in the efficient preparation of a key dipeptide fragment of glidobactin.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase
/
Biocatálise
Tipo de estudo:
Diagnostic_studies
Idioma:
En
Revista:
Org Biomol Chem
Assunto da revista:
BIOQUIMICA
/
QUIMICA
Ano de publicação:
2019
Tipo de documento:
Article
País de afiliação:
Estados Unidos