An enoate reductase Achr-OYE4 from Achromobacter sp. JA81: characterization and application in asymmetric bioreduction of C=C bonds.
Appl Microbiol Biotechnol
; 98(2): 705-15, 2014 Jan.
Article
en En
| MEDLINE
| ID: mdl-23644746
ABSTRACT
A putative enoate reductase, Achr-OYE4, was mined from the genome of Achromobacter sp. JA81, expressed in Escherichia coli, and was characterized. Sequence analysis and spectral properties indicated that Achr-OYE4 is a typical flavin mononucleotide-dependent protein; it preferred NADH over NADPH as a cofactor. The heterologously expressed protein displayed good activity and excellent stereoselectivity toward some activated alkenes in the presence of NADH, NADPH, or their recycling systems. The glucose dehydrogenase-based recycling system yielded the best results in most cases, with a product yield of up to 99 % and enantiopurity of >99 % ee. Achr-OYE4 is an important addition to the asymmetric reduction reservoir as an "old yellow enzyme" from Achromobacter.
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1
Banco de datos:
MEDLINE
Asunto principal:
Achromobacter
/
Oxidorreductasas actuantes sobre Donantes de Grupo CH-CH
Idioma:
En
Año:
2014
Tipo del documento:
Article