Multidimensional engineering of Escherichia coli for efficient biosynthesis of cis-3-hydroxypipecolic acid.
Multiple-enzyme expression optimization
NAD(+) regeneration system
Transporter dynamic regulation
cis-3-Hydroxypipecolic acid
l-Lysine
Journal
Bioresource technology
ISSN: 1873-2976
Titre abrégé: Bioresour Technol
Pays: England
ID NLM: 9889523
Informations de publication
Date de publication:
Aug 2023
Aug 2023
Historique:
received:
05
04
2023
revised:
11
05
2023
accepted:
12
05
2023
medline:
5
6
2023
pubmed:
16
5
2023
entrez:
15
5
2023
Statut:
ppublish
Résumé
Cis-3-hydroxypipecolic acid (cis-3-HyPip) is the crucial part of many alkaloids and drugs. However, its bio-based industrial production remains challenging. Here, lysine cyclodeaminase from Streptomyces malaysiensis (SmLCD) and pipecolic acid hydroxylase from Streptomyces sp. L-49973 (StGetF) were screened to achieve the conversion of L-lysine to cis-3-HyPip. Considering the high-cost of cofactors, NAD(P)H oxidase from Lactobacillus sanfranciscensis (LsNox) was further overexpressed in chassis strain Escherichia coli W3110 ΔsucCD (α-ketoglutarate-producing strain) to construct the NAD
Identifiants
pubmed: 37187331
pii: S0960-8524(23)00599-0
doi: 10.1016/j.biortech.2023.129173
pii:
doi:
Substances chimiques
3-hydroxypipecolic acid
0
Ketoglutaric Acids
0
Lysine
K3Z4F929H6
NAD
0U46U6E8UK
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
129173Informations de copyright
Copyright © 2023 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.