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Applied Microbiology and Biotechnology (2021) 105:5433–5447
/10.1007/s00253-021-11401-z
BIOTECHNOLOGICAL PRODUCTS AND PROCESS ENGINEERING
Selection of the optimal tyrosine hydroxylation enzyme for (S)
-reticuline production in Escherichia coli
Akira Nakagawa 1 & Shinya Nakamura2 & Eitaro Matsumura 1 & Yurino Yashima 1 & Mizuki Takao 1 & Sachiyo Aburatani3 &
Katsuro Yaoi3 & Takane Katayama 4 & Hiromichi Minami 1
Received: 30 November 2020 /Revised: 31 May 2021 /Accepted: 8 June 2021 / Published online: 28 June 2021
# The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2021
Abstract
We have constructed an Escherichia coli-based platform producing (S)-reticuline, an important intermediate of benzylisoquinoline
alkaloids (BIAs), using up to 14 genes. (S)-reticuline was produced from a simple carbon source such as glucose and glycerol via L-
DOPA, which is synthesized by hydroxylation of L-tyrosine, one of the rate-limiting steps of the reaction. There are three kinds of
enzymes catalyzing tyrosine hydroxylation: tyrosinase (TYR), tyrosine hydroxylase (TH), and 4-hydroxyphenylacetate 3-
monooxygenase (HpaBC). Here, to further improve (S)-reticuline production, we chose eight from these three kinds of tyrosine
hydroxylation enzymes (two TYRs, four THs, and two HpaBCs) derived from various organisms, and examined which enzyme was
optimal for (S)-reticuline production in E. coli. TH fromDrosophila melanogaster was the most suitable for (S)-reticuline production
under the experimental conditions tested. We improved the productivity by genome integration of a gene set for L-tyrosine
overproduction, introducing the regeneration pathway of BH4, a cofactor of TH, and methionine addition to enhance the S-
adenosylmethionine supply. As a result, the yield of (S)-reticuline reached up to 384 μM from glucose in laboratory-scale shake
flask. Furthermore, we found three inconsistent phenomena: an inhibitory e
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