Information on EC 2.3.1.B38 - heptylquinolone synthase

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The expected taxonomic range for this enzyme is: Pseudomonas aeruginosa

EC NUMBER
COMMENTARY hide
2.3.1.B38
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RECOMMENDED NAME
GeneOntology No.
heptylquinolone synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
octanoyl-CoA + 2-aminobenzoylacetate = 2-heptylquinolin-4(1H)-one + CO2 + H2O
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
octanoyl-CoA:2-aminobenzoylacetate octanoyltransferase |cyclising||
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
A0A0H2Z7A3 i.e. subunit PqsC, and A0A0H2Z7K6, i.e. subunit PqsB
A0A0H2Z7A3 and A0A0H2Z7K6
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
octanoyl-CoA + 2-aminobenzoylacetate
CoA + 2-heptylquinolin-4(1H)-one + CO2 + H2O
show the reaction diagram
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product is a signal molecule in Pseudomonas aeruginosa. The initial product is 1-(2-aminophenyl)decane-1,3-dione which spontaneously rearranges to the product under the elimination of water
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?
additional information
?
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the catalytic His269 residue is not involved in acyl-enzyme formation, but contributes to an acylation-dependent increase in affinity for the second substrate 2-aminobenzoylacetate. Octanoylation of Cys129 of PqsC is independent of His269
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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
octanoyl-CoA + 2-aminobenzoylacetate
CoA + 2-heptylquinolin-4(1H)-one + CO2 + H2O
show the reaction diagram
Q9I4X1
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product is a signal molecule in Pseudomonas aeruginosa. The initial product is 1-(2-aminophenyl)decane-1,3-dione which spontaneously rearranges to the product under the elimination of water
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?
additional information
?
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Q9I4X1
the catalytic His269 residue is not involved in acyl-enzyme formation, but contributes to an acylation-dependent increase in affinity for the second substrate 2-aminobenzoylacetate. Octanoylation of Cys129 of PqsC is independent of His269
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-aminoacetophenone
pathway-inherent competitive inhibitor. EC50 of 46 microM in the in vitro assay
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additional information
2-heptyl-4(1H)-quinolone and 2-heptyl-3-hydroxy-4(1H)-quinolone as well as ,4-dihydroxyquinoline at concentrations up to 50 microM do not affect PqsBC activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.105
2-aminobenzoylacetate
pH 8.2, temperature not specified in the publication
0.006
Octanoyl-CoA
pH 8.2, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.8
Octanoyl-CoA
Pseudomonas aeruginosa
Q9I4X1
pH 8.2, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.054 - 0.056
2-aminoacetophenone
pH 8.2, temperature not specified in the publication
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant C129A, to 2 A resolution, space group P212121. The heterodimer displays a pseudo 2fold symmetry. Subunit PqsC has an active site comprised of Cys129 and His269
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C129A
mutation in catalytic dyad, crystallization data
V299N
substitution leads to significant activity toward the deamino substrate analog benzoylacetate, suggesting that the substrate 2-aminobenzoylacetate itself supplies the asparagine-equivalent amino function that assists in catalysis