Information on EC 2.3.1.253 - phloroglucinol synthase

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The expected taxonomic range for this enzyme is: Pseudomonas fluorescens group

EC NUMBER
COMMENTARY hide
2.3.1.253
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RECOMMENDED NAME
GeneOntology No.
phloroglucinol synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3 malonyl-CoA = phloroglucinol + 3 CO2 + 3 CoA
show the reaction diagram
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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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
show the reaction diagram
acetoacetyl-CoA
monoacetylphloroglucinol + ?
show the reaction diagram
acetoacetyl-CoA
phloroglucinol + 4-hydroxy-6-methyl-2H-pyran-2-one + CO2 + CoA
show the reaction diagram
butyryl-CoA
phloroglucinol + 4-hydroxy-6-propyl-2H-pyran-2-one + CO2 + CoA
show the reaction diagram
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
show the reaction diagram
hexanoyl-CoA
4-hydroxy-6-pentyl-2H-pyran-2-one + 4-hydroxy-6-(2-oxoheptyl)-2H-pyran-2-one + CO2 + CoA
show the reaction diagram
8% activity compared to malonyl-CoA
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-
?
lauroyl-CoA
6-decyl-4-hydroxy-2H-pyran-2-one + 4-hydroxy-6-(2-oxotridecyl)-2H-pyran-2-one + CO2 + CoA
show the reaction diagram
7.6% activity compared to malonyl-CoA
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-
?
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
show the reaction diagram
7% activity compared to malonyl-CoA
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-
?
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
show the reaction diagram
3.3% activity compared to malonyl-CoA
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3 malonyl-CoA
phloroglucinol + 3 CO2 + 3 CoA
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0056 - 0.0135
malonyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 0.4
malonyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.5 - 31.38
malonyl-CoA
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38400
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x * 38400, calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 37
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the times required to reduce the activity of the enzyme by 50% at 25, 30, and 37C are 128, 74, and 7.2 min, respectively
37
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the enzyme has a half-life of 7.2 min at 37C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose resin column chromatography
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Ni-NTA column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A181S
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the mutant shows 110% of wild type specific activity
A185D
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inactive
A289R
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the mutant shows 1.4fold improved catalytic efficiency compared to the wild type enzyme
A60L
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the mutant still retains the wild type activity to react with lauroyl-CoA
A82T
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the mutant shows wild type specific activity
H24L
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the mutant shows reduced reactivity toward lauroyl-CoA and has lost the ability to produce phloroglucinol
H24V
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the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
K210L
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the mutant shows 1.9fold improved catalytic efficiency compared to the wild type enzyme
K210L/Y256R
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the mutant shows 0.9fold improved catalytic efficiency compared to the wild type enzyme
L136M/S243T
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the mutant shows 90% of wild type specific activity
L54V
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the mutant shows 110% of wild type specific activity
L54V/A82T
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the mutant shows wild type specific activity
L59M
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the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
M21I
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the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
M21T/L54V/A82T
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the mutant shows 90% of wild type specific activity
M21T/L54V/A82T/A181S
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the mutant shows wild type specific activity
M21T/L54V/A82T/S96R/A181S
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the mutant shows 110% of wild type specific activity
M21T/N27D/A82T/A181S
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the mutant shows 90% of wild type specific activity
M21T/N27D/L54V/A82T/A181S/S243T
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the mutant shows wild type specific activity
M21T/N27D/L54V/A82T/L136M/A181S/S243T
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the mutant shows 110% of wild type specific activity
N27D
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the mutant shows 90% of wild type specific activity
S96R
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the mutant shows 80% of wild type specific activity
Y256R
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the mutant shows 1.9fold improved catalytic efficiency compared to the wild type enzyme
Y256R/A289R
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the mutant shows 0.8fold improved catalytic efficiency compared to the wild type enzyme
A181S
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the mutant shows 110% of wild type specific activity
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A289R
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the mutant shows 1.4fold improved catalytic efficiency compared to the wild type enzyme
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A82T
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the mutant shows wild type specific activity
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H24L
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the mutant shows reduced reactivity toward lauroyl-CoA and has lost the ability to produce phloroglucinol
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H24V
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the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
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K210L
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the mutant shows 1.9fold improved catalytic efficiency compared to the wild type enzyme
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K210L/Y256R
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the mutant shows 0.9fold improved catalytic efficiency compared to the wild type enzyme
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L136M/S243T
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the mutant shows 90% of wild type specific activity
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L54V
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the mutant shows 110% of wild type specific activity
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L59M
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the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
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M21I
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the mutation significantly reduces the reactivity of the enzyme with lauroyl-CoA while still retaining its physiological activity to synthesize phloroglucinol
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M21T
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the mutant still retains the wild type activity to react with lauroyl-CoA
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N27D
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the mutant shows 90% of wild type specific activity
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Y256R
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the mutant shows 1.9fold improved catalytic efficiency compared to the wild type enzyme
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Y256R/A289R
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the mutant shows 0.8fold improved catalytic efficiency compared to the wild type enzyme
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