Information on EC 2.3.1.233 - 1,3,6,8-tetrahydroxynaphthalene synthase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.3.1.233
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RECOMMENDED NAME
GeneOntology No.
1,3,6,8-tetrahydroxynaphthalene synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5 malonyl-CoA = 1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
flaviolin dimer and mompain biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA C-acyl transferase (1,3,6,8-tetrahydroxynaphthalene forming)
Isolated from the fungus Colletotrichum lagenarium [1], and the bacteria Streptomyces coelicolor [2,3] and Streptomyces peucetius [4]. It only uses malonyl-CoA, without invovement of acetyl-CoA.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
show the reaction diagram
acetoacetyl-CoA
4-hydroxy-6-methyl-2-pyrone + CoA + CO2 + H2O
show the reaction diagram
acetoacetyl-CoA + 2 malonyl-CoA
4-hydroxy-6-methyl-2-pyrone + CoA + CO2 + H2O
show the reaction diagram
acetoacetyl-CoA + methylmalonyl-CoA
3,6-dimethyl-4-hydroxy-2-pyrone + CoA + CO2 + H2O
show the reaction diagram
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-
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?
Acetyl-CoA
?
show the reaction diagram
acetyl-CoA
? + CoA + CO2 + H2O
show the reaction diagram
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-
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?
acetyl-CoA + 2 malonyl-CoA
? + CoA + CO2 + H2O
show the reaction diagram
benzoyl-CoA
? + CoA + CO2 + H2O
show the reaction diagram
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-
-
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?
benzoyl-CoA + 2 malonyl-CoA
4-hydroxy-6-phenyl-2H-pyran-2-one + CoA + CO2 + H2O
show the reaction diagram
butyryl-CoA
4-hydroxy-6-propyl-2-pyrone + 4-hydroxy-6-(2'-oxopentyl)-2-pyrone + 1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
show the reaction diagram
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21% activity compared to acetoacetyl-CoA
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-
?
hexanoyl-CoA
4-hydroxy-6-pentyl-2-pyrone + 4-hydroxy-6-(2'-oxoheptyl)-2-pyrone + CoA + CO2 + H2O
show the reaction diagram
hexanoyl-CoA
? + CoA + CO2 + H2O
show the reaction diagram
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-
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?
hexanoyl-CoA + 2 malonyl-CoA
4-hydroxy-6-pentyl-2H-pyran-2-one + CoA + CO2 + H2O
show the reaction diagram
isobutyryl-CoA
4-hydroxy-6-isopropyl-2-pyrone + 4-hydroxy-6-(3'-methyl-2'-oxopropyl)-2-pyrone + CoA + CO2 + H2O
show the reaction diagram
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7% activity compared to acetoacetyl-CoA
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-
?
isovaleryl-CoA
4-hydroxy-6-isobutyl-2-pyrone + 4-hydroxy-6-(4'-methyl-2'-oxopentyl)-2-pyrone + CoA + CO2 + H2O
show the reaction diagram
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13% activity compared to acetoacetyl-CoA
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?
lauroyl-CoA
1-(2,4,6-trihydroxyphenyl)-dodecan-1-one + 4-hydroxy-6-(2-oxotridecyl)-2H-pyran-2-one + CoA + CO2 + H2O
show the reaction diagram
malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
show the reaction diagram
malonyl-CoA
5 1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
show the reaction diagram
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?
octanoyl-CoA
6-heptyl-4-hydroxy-2-pyrone + 4-hydroxy-6-(2'-oxononyl)-2-pyrone + 4-hydroxy-6-(2',4',6'-trioxotridecyl)-2-pyrone + CoA + CO2 + H2O
show the reaction diagram
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6% activity compared to acetoacetyl-CoA
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?
octanoyl-CoA + malonyl-CoA
4-hydroxy-6-(2',4',6'-trioxotridecyl)-2-pyrone + CoA + CO2 + H2O
show the reaction diagram
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?
phenylacetyl-CoA
6-benzyl-4-hydroxy-2-pyrone + 4-hydroxy-6-(2'-oxo-3'-phenylpropyl)-2-pyrone + CoA + CO2 + H2O
show the reaction diagram
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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
5 malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
show the reaction diagram
malonyl-CoA
1,3,6,8-tetrahydroxynaphthalene + CoA + CO2 + H2O
show the reaction diagram
malonyl-CoA
5 1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O
show the reaction diagram
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?
additional information
?
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does not use acetyl-CoA as substrate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0087 - 0.0508
Hexanoyl-CoA
0.0011 - 0.93
malonyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 9
Hexanoyl-CoA
0.0003 - 79.2
malonyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.85 - 574.7
Hexanoyl-CoA
395
0.133 - 44.58
malonyl-CoA
76
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
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x * 40000, SDS-PAGE
58000
x * 58000, SDS-PAGE
230000
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x * 230000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M Bicine, pH 8, and 18% (w/v) polyethylene glycol 6000, at 19C
hanging drop vapor diffusion method, using 14% (w/v) PEG 8000, 200 mM MgCl2, 100 mM Na-MOPSO buffer (pH 7.0), 5 mM dithiothreitol, and 3% (w/v) sucrose
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Co2+ affinity column chromatography
His-binding resin column chromatography
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Ni-nickel tetradentate column chromatography and Sephacryl-200 gel filtration
Ni-NTA column chromatography
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Ni2+-affinity column chromatography
nickel-nitrilotriacetic acid-agarose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Aspergillus oryzae
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expressed in Escherichia coli BL21 (DE3) codon Plus RIPL cells
expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Streptomyces venezuelae strain YJ028
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C106S
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inactive
C138A
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inactive with malonyl-CoA
C138S
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inactive with malonyl-CoA
C171S
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the mutant shows about 4fold reduced catalytic efficiency compared to the wild type enzyme
C184S
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the mutant shows about 2.5fold increased catalytic efficiency compared to the wild type enzyme
Y224A
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the mutant shows 3% activity with malonyl-CoA compared to the wild type enzyme
Y224C
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the mutant shows 50% activity with malonyl-CoA compared to the wild type enzyme
Y224F
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the mutant shows 70% activity with malonyl-CoA compared to the wild type enzyme
Y224G
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inactive with malonyl-CoA but capable of accepting acetoacetyl-CoA and acetyl-CoA
Y224H
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inactive with malonyl-CoA but capable of accepting acetoacetyl-CoA and acetyl-CoA
Y224L
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the mutant shows 65% activity with malonyl-CoA compared to the wild type enzyme
Y224M
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the mutant shows 15% activity with malonyl-CoA compared to the wild type enzyme
Y224S
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inactive with malonyl-CoA but capable of accepting acetoacetyl-CoA and acetyl-CoA
C138A
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inactive with malonyl-CoA
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C138S
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inactive with malonyl-CoA
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Y224A
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the mutant shows 3% activity with malonyl-CoA compared to the wild type enzyme
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Y224F
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the mutant shows 70% activity with malonyl-CoA compared to the wild type enzyme
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Y224S
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inactive with malonyl-CoA but capable of accepting acetoacetyl-CoA and acetyl-CoA
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A305I
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the mutant produces only a triketide pyrone from hexanoyl-CoA as starter substrate
A305S
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the mutant produces a triketide and tetraketide pyrone from hexanoyl-CoA as starter substrate
C138A
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the mutant loses the ability to decarboxylate malonyl-CoA
C138Q
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the mutant loses the ability to decarboxylate malonyl-CoA
C138S
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the mutation does not influence the decarboxylation of malonyl-CoA
F188A
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inactive
F188S
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inactive
F188Y
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the mutant shows reduced catalytic efficiency with hexanoyl-CoA as substrate
H270A
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inactive
H270N
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the mutant produces triacetic acid lactone and flaviolin, an auto-oxidized product of 1,3,6,8-tetrahydroxynaphthalene, at a reduced rate
H270Q
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the mutant retains high activity to catalyse polyketide formation, whereas the derailment products triacetic acid lactone and 6-acetonyl-4-hydroxy-2-pyrone (tetraketide lactone) are observed in increased amounts
N303D
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inactive
N303H
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inactive
N303Q
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inactive
Y224F
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the mutant is able to accept malonyl-CoA as a starter substrate
Y224G
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the mutant shows reduced catalytic efficiency with hexanoyl-CoA as substrate
Y224W
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the mutant is able to accept malonyl-CoA as a starter substrate