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Information on EC 2.3.1.253 - phloroglucinol synthase
for references in articles please use BRENDA:EC2.3.1.253
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.253 phloroglucinol synthase
IUBMB Comments
The enzyme, characterized from the bacterium Pseudomonas protegens Pf-5, is a type III polyketide synthase. The mechanism involves the cyclization of an activated 3,5-dioxoheptanedioate intermediate. The enzyme exhibits broad substrate specificity, and can accept C4-C12 aliphatic acyl-CoAs and phenylacetyl-CoA as the starter molecules, forming 6-(polyoxoalkyl)-α-pyrones by sequential condensation with malonyl-CoA.
The expected taxonomic range for this enzyme is: Pseudomonas
showSynonyms
phloroglucinol synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PhlD
phloroglucinol synthase
type III polyketide synthase
PhlD
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 malonyl-CoA = phloroglucinol + 3 CO2 + 3 CoA
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:malonyl-CoA malonyltransferase (decarboxylating, phloroglucinol-forming)
The enzyme, characterized from the bacterium Pseudomonas protegens Pf-5, is a type III polyketide synthase. The mechanism involves the cyclization of an activated 3,5-dioxoheptanedioate intermediate. The enzyme exhibits broad substrate specificity, and can accept C4-C12 aliphatic acyl-CoAs and phenylacetyl-CoA as the starter molecules, forming 6-(polyoxoalkyl)-alpha-pyrones by sequential condensation with malonyl-CoA.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetoacetyl-CoA
phloroglucinol + 4-hydroxy-6-methyl-2H-pyran-2-one + CO2 + CoA
Substrates: 1.6% activity compared to malonyl-CoA
Products: -
Products: -
?
decanoyl-CoA
4-hydroxy-6-octyl-2H-pyran-2-one + 4-hydroxy-6-(2-oxoundecyl)-2H-pyran-2-one + 4-hydroxyl-6-(2',4',6'-trioxopentadecyl)-2-pyrone + CO2 + CoA
Substrates: 18% activity compared to malonyl-CoA
Products: -
Products: -
?
hexanoyl-CoA
4-hydroxy-6-pentyl-2H-pyran-2-one + 4-hydroxy-6-(2-oxoheptyl)-2H-pyran-2-one + CO2 + CoA
lauroyl-CoA
6-decyl-4-hydroxy-2H-pyran-2-one + 4-hydroxy-6-(2-oxotridecyl)-2H-pyran-2-one + CO2 + CoA
Substrates: 7.6% activity compared to malonyl-CoA
Products: -
Products: -
?
octanoyl-CoA
6-heptyl-4-hydroxy-2H-pyran-2-one + 4-hydroxy-6-(2-oxononyl)-2H-pyran-2-one + 4-hydroxyl-6-(2',4',6'-trioxotridecyl)-2-pyrone + 4-hydroxyl-6-(2',4',6',8'-tetraoxopentadecyl)-2-pyrone + CO2 + CoA
phenylacetyl-CoA
6-(cyclohepta-1,3,6-trien-1-yl)-4-hydroxy-2H-pyran-2-one + 6-[2-(cyclohepta-1,3,6-trien-1-yl)-2-oxoethyl]-4-hydroxy-2H-pyran-2-one + CO2 + CoA
Substrates: 3.3% activity compared to malonyl-CoA
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
-
Substrates: -
Products: phloroglucinol is 1,3,5-trihydroxylbenzene
Products: phloroglucinol is 1,3,5-trihydroxylbenzene
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: preferred substrate
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: preferred substrate
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
-
Substrates: -
Products: phloroglucinol is 1,3,5-trihydroxylbenzene
Products: phloroglucinol is 1,3,5-trihydroxylbenzene
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA
monoacetylphloroglucinol + ?
-
Substrates: -
Products: -
Products: -
?
acetoacetyl-CoA
monoacetylphloroglucinol + ?
-
Substrates: -
Products: -
Products: -
?
butyryl-CoA
phloroglucinol + 4-hydroxy-6-propyl-2H-pyran-2-one + CO2 + CoA
Substrates: 0.2% activity compared to malonyl-CoA
Products: -
Products: -
?
butyryl-CoA
phloroglucinol + 4-hydroxy-6-propyl-2H-pyran-2-one + CO2 + CoA
Substrates: 0.2% activity compared to malonyl-CoA
Products: -
Products: -
?
hexanoyl-CoA
4-hydroxy-6-pentyl-2H-pyran-2-one + 4-hydroxy-6-(2-oxoheptyl)-2H-pyran-2-one + CO2 + CoA
Substrates: 8% activity compared to malonyl-CoA
Products: -
Products: -
?
hexanoyl-CoA
4-hydroxy-6-pentyl-2H-pyran-2-one + 4-hydroxy-6-(2-oxoheptyl)-2H-pyran-2-one + CO2 + CoA
Substrates: 8% activity compared to malonyl-CoA
Products: -
Products: -
?
octanoyl-CoA
6-heptyl-4-hydroxy-2H-pyran-2-one + 4-hydroxy-6-(2-oxononyl)-2H-pyran-2-one + 4-hydroxyl-6-(2',4',6'-trioxotridecyl)-2-pyrone + 4-hydroxyl-6-(2',4',6',8'-tetraoxopentadecyl)-2-pyrone + CO2 + CoA
Substrates: 7% activity compared to malonyl-CoA
Products: -
Products: -
?
octanoyl-CoA
6-heptyl-4-hydroxy-2H-pyran-2-one + 4-hydroxy-6-(2-oxononyl)-2H-pyran-2-one + 4-hydroxyl-6-(2',4',6'-trioxotridecyl)-2-pyrone + 4-hydroxyl-6-(2',4',6',8'-tetraoxopentadecyl)-2-pyrone + CO2 + CoA
Substrates: 7% activity compared to malonyl-CoA
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows barely detectable activity toward acetyl-CoA, isobutyryl-CoA, benzoyl-CoA, and crotonyl-CoA. No activity with myristoyl-CoA and palmitoyl-CoA
Products: -
Products: -
?
additional information
?
-
Substrates: acetate is successfully transformed into phloroglucinol by the combined activity of recombinant acetyl-CoA carboxylase (ACC) from Acinetobacter calcoaceticus strain CGMCC 1.6186 and recombinant phloroglucinol synthase (PhlD) from Pseudomonas fluorescens strain Pf-5 in an in vitro system, synthetic pathway of phloroglucinol and in vitro synthesis of phloroglucinol from acetate, method optimization, overview
Products: -
Products: -
?
additional information
?
-
Substrates: acetate is successfully transformed into phloroglucinol by the combined activity of recombinant acetyl-CoA carboxylase (ACC) from Acinetobacter calcoaceticus strain CGMCC 1.6186 and recombinant phloroglucinol synthase (PhlD) from Pseudomonas fluorescens strain Pf-5 in an in vitro system, synthetic pathway of phloroglucinol and in vitro synthesis of phloroglucinol from acetate, method optimization, overview
Products: -
Products: -
?
additional information
?
-
Substrates: acetate is successfully transformed into phloroglucinol by the combined activity of recombinant acetyl-CoA carboxylase (ACC) from Acinetobacter calcoaceticus strain CGMCC 1.6186 and recombinant phloroglucinol synthase (PhlD) from Pseudomonas fluorescens strain Pf-5 in an in vitro system, synthetic pathway of phloroglucinol and in vitro synthesis of phloroglucinol from acetate, method optimization, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows barely detectable activity toward acetyl-CoA, isobutyryl-CoA, benzoyl-CoA, and crotonyl-CoA. No activity with myristoyl-CoA and palmitoyl-CoA
Products: -
Products: -
?
additional information
?
-
Substrates: acetate is successfully transformed into phloroglucinol by the combined activity of recombinant acetyl-CoA carboxylase (ACC) from Acinetobacter calcoaceticus strain CGMCC 1.6186 and recombinant phloroglucinol synthase (PhlD) from Pseudomonas fluorescens strain Pf-5 in an in vitro system, synthetic pathway of phloroglucinol and in vitro synthesis of phloroglucinol from acetate, method optimization, overview
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
-
Substrates: -
Products: phloroglucinol is 1,3,5-trihydroxylbenzene
Products: phloroglucinol is 1,3,5-trihydroxylbenzene
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: preferred substrate
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: preferred substrate
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
-
Substrates: -
Products: phloroglucinol is 1,3,5-trihydroxylbenzene
Products: phloroglucinol is 1,3,5-trihydroxylbenzene
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
-
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
Substrates: -
Products: -
Products: -
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0056
malonyl-CoA
-
pH and temperature not specified in the publication
0.0101
malonyl-CoA
mutant enzyme A289R, pH and temperature not specified in the publication
0.0103
malonyl-CoA
mutant enzyme Y256R/A289R, pH and temperature not specified in the publication
0.0112
malonyl-CoA
mutant enzyme Y256R, pH and temperature not specified in the publication
0.0119
malonyl-CoA
mutant enzyme K210L, pH and temperature not specified in the publication
0.0131
malonyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.0135
malonyl-CoA
mutant enzyme K210L/Y256R, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
malonyl-CoA
mutant enzyme Y256R/A289R, pH and temperature not specified in the publication
0.11
malonyl-CoA
mutant enzyme K210L/Y256R, pH and temperature not specified in the publication
0.12
malonyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.13
malonyl-CoA
mutant enzyme A289R, pH and temperature not specified in the publication
0.17
malonyl-CoA
-
pH and temperature not specified in the publication
0.2
malonyl-CoA
mutant enzyme Y256R, pH and temperature not specified in the publication
0.21
malonyl-CoA
mutant enzyme K210L, pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.5
malonyl-CoA
mutant enzyme Y256R/A289R, pH and temperature not specified in the publication
8.3
malonyl-CoA
mutant enzyme K210L/Y256R, pH and temperature not specified in the publication
9.3
malonyl-CoA
wild type enzyme, pH and temperature not specified in the publication
12.8
malonyl-CoA
mutant enzyme A289R, pH and temperature not specified in the publication
17.5
malonyl-CoA
mutant enzyme K210L, pH and temperature not specified in the publication
17.7
malonyl-CoA
mutant enzyme Y256R, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PHLD_PSEF5
Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
349
0
38617
Swiss-Prot
Mitochondrion (Reliability: 4)
Q9REM4_PSEFL
235
0
25776
TrEMBL
Mitochondrion (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A289R
the mutant shows 1.4fold improved catalytic efficiency compared to the wild type enzyme
A60L
the mutant still retains the wild type activity to react with lauroyl-CoA
H24L
the mutant shows reduced reactivity toward lauroyl-CoA and has lost the ability to produce phloroglucinol
H24V
the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
K210L
the mutant shows 1.9fold improved catalytic efficiency compared to the wild type enzyme
K210L/Y256R
the mutant shows 0.9fold improved catalytic efficiency compared to the wild type enzyme
L59M
the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
M21I
the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
M21T
M21T/L54V/A82T/S96R/A181S
-
the mutant shows 110% of wild type specific activity
M21T/N27D/A82T/A181S
-
the mutant shows 90% of wild type specific activity
M21T/N27D/L54V/A82T/A181S/S243T
-
the mutant shows wild type specific activity
M21T/N27D/L54V/A82T/L136M/A181S/S243T
-
the mutant shows 110% of wild type specific activity
Y256R
the mutant shows 1.9fold improved catalytic efficiency compared to the wild type enzyme
Y256R/A289R
the mutant shows 0.8fold improved catalytic efficiency compared to the wild type enzyme
A289R
-
the mutant shows 1.4fold improved catalytic efficiency compared to the wild type enzyme
-
H24L
-
the mutant shows reduced reactivity toward lauroyl-CoA and has lost the ability to produce phloroglucinol
-
H24V
-
the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
-
K210L
-
the mutant shows 1.9fold improved catalytic efficiency compared to the wild type enzyme
-
K210L/Y256R
-
the mutant shows 0.9fold improved catalytic efficiency compared to the wild type enzyme
-
L59M
-
the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
-
M21I
-
the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
-
Y256R
-
the mutant shows 1.9fold improved catalytic efficiency compared to the wild type enzyme
-
Y256R/A289R
-
the mutant shows 0.8fold improved catalytic efficiency compared to the wild type enzyme
-
M21T
the mutant still retains the wild type activity to react with lauroyl-CoA
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 37
the times required to reduce the activity of the enzyme by 50% at 25, 30, and 37°C are 128, 74, and 7.2 min, respectively
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
codon-optimized gene phlD, functional recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), method optimization
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
the enzyme can be used for production of important industrial chemicals from acetate in in vitro systems
synthesis
production of 2,4-diacetylphloroglucinol from glucose is achieved in Escherichia coli by expression of the the phlACBD gene cluster. Yield is increased by expressing the acc, marA and phlE genes in shake-flasks cultivation. Under optimum condition, the concentration of 2,4-diacetylphloroglucinol reaches 179 mg/l after induction for 36 h by fed-batch fermentation
synthesis
Escherichia coli expressing PhlD and acetyl-CoA carboxylase can produce 1107 mg/l phloroglucinol from glucose. When E. coli is engineered to utilize acetate as main carbon source the endogenous citrate synthase is knocked down in order to enhance the carbon flux for phloroglucinol production, the titer can be improved to 284 mg/l
synthesis
production of PhlD by overexpression in Yarrowia lipolyticy gives a concentration of 107.4 mg/l. When the prokaryotic nanocompartment is introduced to assist the intracellular catalytic activity and fermentations with xylose and lignocellulosic hydrolysates as the carbon source are performed , total concentrations of 580.2 mg/l and 328.9 mg/l, respectively, can be achieved
synthesis
-
the enzyme can be used for production of important industrial chemicals from acetate in in vitro systems
-
synthesis
-
production of 2,4-diacetylphloroglucinol from glucose is achieved in Escherichia coli by expression of the the phlACBD gene cluster. Yield is increased by expressing the acc, marA and phlE genes in shake-flasks cultivation. Under optimum condition, the concentration of 2,4-diacetylphloroglucinol reaches 179 mg/l after induction for 36 h by fed-batch fermentation
-
synthesis
-
the enzyme can be used for production of important industrial chemicals from acetate in in vitro systems
-
synthesis
-
the enzyme can be used for production of important industrial chemicals from acetate in in vitro systems
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cao, Y.; Jiang, X.; Zhang, R.; Xian, M.
Improved phloroglucinol production by metabolically engineered Escherichia coli
Appl. Microbiol. Biotechnol.
91
1545-1552
2011
Pseudomonas fluorescens, Pseudomonas fluorescens Pf-5
brenda
Rao, G.; Lee, J.K.; Zhao, H.
Directed evolution of phloroglucinol synthase PhlD with increased stability for phloroglucinol production
Appl. Microbiol. Biotechnol.
97
5861-5867
2013
Pseudomonas fluorescens, Pseudomonas fluorescens Pf-5
brenda
Achkar, J.; Xian, M.; Zhao, H.; Frost, J.W.
Biosynthesis of phloroglucinol
J. Am. Chem. Soc.
127
5332-5333
2005
Pseudomonas fluorescens, Pseudomonas fluorescens Pf-5
brenda
Bangera, M.G.; Thomashow, L.S.
Identification and characterization of a gene cluster for synthesis of the polyketide antibiotic 2,4-diacetylphloroglucinol from Pseudomonas fluorescens Q2-87
J. Bacteriol.
181
3155-3163
1999
Pseudomonas fluorescens, Pseudomonas fluorescens Q2-87
brenda
Zha, W.; Rubin-Pitel, S.B.; Zhao, H.
Characterization of the substrate specificity of PhlD, a type III polyketide synthase from Pseudomonas fluorescens
J. Biol. Chem.
281
32036-32047
2006
Pseudomonas fluorescens (Q4K418), Pseudomonas fluorescens Pf-5 (Q4K418)
brenda
Zha, W.; Rubin-Pitel, S.B.; Zhao, H.
Exploiting genetic diversity by directed evolution: molecular breeding of type III polyketide synthases improves productivity
Mol. Biosyst.
4
246-248
2008
Pseudomonas fluorescens (Q4K418), Pseudomonas fluorescens Pf-5 (Q4K418)
brenda
Ramette, A.; Moenne-Loccoz, Y.; Defago, G.
Polymorphism of the polyketide synthase gene phID in biocontrol fluorescent pseudomonads producing 2,4-diacetylphloroglucinol and comparison of PhID with plant polyketide synthases
Mol. Plant Microbe Interact.
14
639-652
2001
Pseudomonas fluorescens (Q9REZ9), Pseudomonas fluorescens (Q9REM4), Pseudomonas fluorescens (Q9REL5), Pseudomonas fluorescens (Q9REL4), Pseudomonas fluorescens (Q9REZ8), Pseudomonas fluorescens CHA0 (Q9REL5), Pseudomonas fluorescens M1-96 (Q9REZ9), Pseudomonas fluorescens Pf-5 (Q9REL4), Pseudomonas fluorescens Q8r1-96 (Q9REZ8), Pseudomonas fluorescens UP61 (Q9REM4)
brenda
Zhang, R.; Liu, W.; Cao, Y.; Xu, X.; Xian, M.; Liu, H.
An in vitro synthetic biosystem based on acetate for production of phloroglucinol
BMC Biotechnol.
17
66
2017
Pseudomonas fluorescens (Q4K418), Pseudomonas fluorescens ATCC BAA-477 (Q4K418), Pseudomonas fluorescens NRRL B-23932 (Q4K418), Pseudomonas fluorescens Pf-5 (Q4K418)
brenda
Yu, S.; Guo, L.; Zhao, L.; Chen, Z.; Huo, Y.
Metabolic engineering of E. coli for producing phloroglucinol from acetate
Appl. Microbiol. Biotechnol.
104
7787-7799
2020
Pseudomonas fluorescens (Q9FCR3)
brenda
Tu, Z.; Zhou, L.; Wu, Y.; Wen, Z.; Li, Y.; Huang, H.
Construction of prokaryotic nanocompartment in Yarrowia lipolytica to assist phloroglucinol production
Appl. Microbiol. Biotechnol.
107
5341-5349
2023
Pseudomonas fluorescens (Q9FCR3)
brenda
Liu, W.; Zhang, R.; Xian, M.
Biosynthesis of 2,4-diacetylphloroglucinol from glucose using engineered Escherichia coli
World J. Microbiol. Biotechnol.
36
130
2020
Pseudomonas fluorescens (Q9FCR3), Pseudomonas fluorescens CHA0 (Q9FCR3)
brenda
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