BRENDA - Enzyme Database show
show all sequences of 1.14.19.64

Efficient microbial production of stylopine using a Pichia pastoris expression system

Hori, K.; Okano, S.; Sato, F.; Sci. Rep. 6, 22201 (2016)

Data extracted from this reference:

Application
Application
Commentary
Organism
pharmacology
a microbial system is established for producing a protoberberine-type alkaloid (stylopine) in Pichia cells
Eschscholzia californica
synthesis
a microbial system is established for producing a protoberberine-type alkaloid (stylopine) in Pichia cells
Eschscholzia californica
Cloned(Commentary)
Commentary
Organism
coexpression of cheilanthifoline synthase (CYP719A5), and stylopine synthase (CYP719A2) in Pichia pastoris. Biosynthetic enzyme expression is examined in a consolidated system with all genes expressed in one cell and a coculture system with three cell lines that each express a single gene were examined. Although both systems efficiently converted reticuline to stylopine, the consolidated system is more rapid and efficient than the co-culture system. However, substrate-feeding experiments reveal a decrease in the conversion efficiency in the consolidated system during successive cultures, whereas the conversion efficiency in the co-culture system remains constant. Thus, the final amount of stylopine produced from reticuline after successive feedings in the co-culture system is more than 150 nmoles from 750 nmoles of (R,S)-reticuline (375 nmoles of (S)-reticuline)
Eschscholzia californica
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Eschscholzia californica
Q50LH3
-
-
Application (protein specific)
Application
Commentary
Organism
pharmacology
a microbial system is established for producing a protoberberine-type alkaloid (stylopine) in Pichia cells
Eschscholzia californica
synthesis
a microbial system is established for producing a protoberberine-type alkaloid (stylopine) in Pichia cells
Eschscholzia californica
Cloned(Commentary) (protein specific)
Commentary
Organism
coexpression of cheilanthifoline synthase (CYP719A5), and stylopine synthase (CYP719A2) in Pichia pastoris. Biosynthetic enzyme expression is examined in a consolidated system with all genes expressed in one cell and a coculture system with three cell lines that each express a single gene were examined. Although both systems efficiently converted reticuline to stylopine, the consolidated system is more rapid and efficient than the co-culture system. However, substrate-feeding experiments reveal a decrease in the conversion efficiency in the consolidated system during successive cultures, whereas the conversion efficiency in the co-culture system remains constant. Thus, the final amount of stylopine produced from reticuline after successive feedings in the co-culture system is more than 150 nmoles from 750 nmoles of (R,S)-reticuline (375 nmoles of (S)-reticuline)
Eschscholzia californica
Other publictions for EC 1.14.19.64
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
746047
Yahyazadeh
-
Cloning and characterization ...
Chelidonium majus
Plant Cell Physiol.
58
1421-1430
2017
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1
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1
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1
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1
1
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746447
Hori
Efficient microbial productio ...
Eschscholzia californica
Sci. Rep.
6
22201
2016
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2
1
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3
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728446
Takemura
Molecular cloning and characte ...
Eschscholzia californica
Phytochemistry
91
100-108
2013
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-
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-
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2
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4
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711025
Diaz Chavez
Characterization of two methyl ...
Argemone mexicana
Arch. Biochem. Biophys.
507
186-193
2011
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-
1
-
-
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1
-
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1
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5
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4
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2
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1
1
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1
1
1
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1
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1
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4
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2
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1
1
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1
1
1
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1
1
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673579
Ikezawa
Molecular cloning and characte ...
Eschscholzia californica
FEBS J.
274
1019-1035
2007
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1
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2
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3
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7
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3
2
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8
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1
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3
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8
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395597
Bauer
-
Two methylenedioxy bridge form ...
Eschscholzia californica
Phytochemistry
30
2953-2961
1991
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1
1
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