2.3.1.230: 2-heptyl-4(1H)-quinolone synthase
This is an abbreviated version!
For detailed information about 2-heptyl-4(1H)-quinolone synthase, go to the full flat file.
Word Map on EC 2.3.1.230
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2.3.1.230
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arachidonic
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20-hydroxyeicosatetraenoic
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omega-hydroxylase
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constrictor
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phenylephrine
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microcirculation
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cyp4a2
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clofibrate
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ppars
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lauric
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omega-hydroxylation
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interlobar
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20-hydroxyeicosa-6z,15z-dienoic
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myogenic
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n-methylsulfonyl-12,12-dibromododec-11-enamide
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proliferators
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nafenopin
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arterioles
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vasoconstrictor
- 2.3.1.230
-
arachidonic
-
20-hydroxyeicosatetraenoic
-
omega-hydroxylase
-
constrictor
- phenylephrine
-
microcirculation
- cyp4a2
- clofibrate
-
ppars
-
lauric
-
omega-hydroxylation
-
interlobar
-
20-hydroxyeicosa-6z,15z-dienoic
-
myogenic
- n-methylsulfonyl-12,12-dibromododec-11-enamide
-
proliferators
-
nafenopin
-
arterioles
-
vasoconstrictor
Reaction
Synonyms
2,4-dihydroxyquinoline synthase, PqsBC, PqsD, PsqD
ECTree
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Crystallization
Crystallization on EC 2.3.1.230 - 2-heptyl-4(1H)-quinolone synthase
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molecular dynamics simulations suggest a nucleophilic attack of the deprotonated sulfur of Cys112 at the carbonyl carbon of ACoA and a switch in the protonation pattern of His257 whereby Ndelta is protonated and the proton of Nepsilon is shifted to the sulfur of CoA during the reaction. In the N287A mutant anthraniloyl remains covalently bound to C112, further supporting that N87 does not take part in the cleavage of anthraniloyl-CoA
sitting drop vapor diffusion method, PqsBC(C129A) crystallized in space group P2(1)2(1)2(1) and the structure is determined to 2 A resolution, revealing that PqsB and PqsC have a pseudo-2-fold symmetry
Q9I4X2; Q9I4X1
sitting drop vapor diffusion method. Several crystal structures of the enzyme including that of the PqsD-anthranilate covalent intermediate and the inactive Cys112Ala active site mutant in complex with anthranilate