Abstract:
:Previous studies have utilized monoamine oxidase (MAO) and L-3,4-dihydroxyphenylalanine decarboxylase (DDC) for microbe-based production of tetrahydropapaveroline (THP), a benzylisoquinoline alkaloid (BIA) precursor to opioid analgesics. In the current study, a phylogenetically distinct Bombyx mori 3,4-dihydroxyphenylacetaldehyde synthase (DHPAAS) is identified to bypass MAO and DDC for direct production of 3,4-dihydroxyphenylacetaldehyde (DHPAA) from L-3,4-dihydroxyphenylalanine (L-DOPA). Structure-based enzyme engineering of DHPAAS results in bifunctional switching between aldehyde synthase and decarboxylase activities. Output of dopamine and DHPAA products is fine-tuned by engineered DHPAAS variants with Phe79Tyr, Tyr80Phe and Asn192His catalytic substitutions. Balance of dopamine and DHPAA products enables improved THP biosynthesis via a symmetrical pathway in Escherichia coli. Rationally engineered insect DHPAAS produces (R,S)-THP in a single enzyme system directly from L-DOPA both in vitro and in vivo, at higher yields than that of the wild-type enzyme. However, DHPAAS-mediated downstream BIA production requires further improvement.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Vavricka CJ,Yoshida T,Kuriya Y,Takahashi S,Ogawa T,Ono F,Agari K,Kiyota H,Li J,Ishii J,Tsuge K,Minami H,Araki M,Hasunuma T,Kondo Adoi
10.1038/s41467-019-09610-2subject
Has Abstractpub_date
2019-05-01 00:00:00pages
2015issue
1issn
2041-1723pii
10.1038/s41467-019-09610-2journal_volume
10pub_type
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