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Biosynthesis of plant-specific alkaloids tetrahydroprotoberberines in engineered
Ist Teil von
Green chemistry : an international journal and green chemistry resource : GC, 2021-08, Vol.23 (16), p.5944-5955
Erscheinungsjahr
2021
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
Tetrahydroprotoberberines (THPBs), mainly sourced from the medicinal plants of genus
Stephania
and
Corydalis
, exhibit a variety of pharmacological activities. Plant-sourced THPBs are limited by low yields, and their chemical synthesis faces high cost, low yield, and stereochemical challenges. Since the biosynthesis of THPBs has not yet been fully established, further investigation into their pharmaceutical utility is limited by the product quantity. Here, by reconstructing tailor-made biosynthetic pathways, we provide an alternative strategy for the production of THPBs and related intermediates in
Escherichia coli
(
E. coli
). Firstly, the major obstacle in the reconstruction of the THPBs biosynthetic pathway, berberine bridge enzyme (BBE), a rate-limiting enzyme was functionally expressed in
E. coli
using several new strategies. Next, the corresponding biosynthetic pathway modules for the biosynthesis of (
S
)-scoulerine (compound
3
), (
S
)-tetrahydropalmatine (compound
5
), (
S
)-corydalmine (compound
6
), and their intermediates were reconstituted. We achieved the biosynthesis of compounds
3
,
5
, and
6
and their intermediates in the corresponding engineered
E. coli
strain. Furthermore, we optimized culture conditions to raise the yield of compound
5
to 1.19 mg L
−1
in a flask culture using the engineered strain. Our work provides a green solution for the production of high-value THPBs without environmental consequences.
Tetrahydroprotoberberines (THPBs) exhibit a variety of pharmacological activities however further investigation into their pharmaceutical utility is limited by the product quantity. In this paper, a greener strategy has been developed for the production of high-value THPBs.
Sprache
–
Identifikatoren
ISSN: 1463-9262
eISSN: 1463-9270
DOI: 10.1039/d1gc01670a
Titel-ID: cdi_rsc_primary_d1gc01670a
Format
–
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