Information on EC 1.14.13.182 - 2-heptyl-3-hydroxy-4(1H)-quinolone synthase

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The expected taxonomic range for this enzyme is: Pseudomonas aeruginosa

EC NUMBER
COMMENTARY hide
1.14.13.182
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RECOMMENDED NAME
GeneOntology No.
2-heptyl-3-hydroxy-4(1H)-quinolone synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-heptyl-4(1H)-quinolone + NADH + H+ + O2 = 2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-heptyl-3-hydroxy-4(1H)-quinolone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
2-heptyl-4(1H)-quinolone,NADH:oxygen oxidoreductase (3-hydroxylating)
The enzyme from the bacterium Pseudomonas aeruginosa catalyses the terminal step in biosynthesis of the signal molecule 2-heptyl-3,4-dihydroxyquinoline that plays a role in regulation of virulence genes.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
PqsH catalyzes the terminal step in biosynthesis of the Pseudomonas quinolone signal molecule 2-heptyl-3,4-dihydroxyquinoline. Under anaerobic conditions 2-heptyl-3-hydroxy-4(1H)-quinolone is not produced. The enzyme is a biochemical regulator of Pseudomonas Quinolone Signal controlled social behaviors in Pseudomonas aeruginosa
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-heptyl-4(1H)-quinolone + NADH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
show the reaction diagram
2-heptyl-4(1H)-quinolone + NADPH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NADP+ + H2O
show the reaction diagram
kcat/KM for NADH is 20fold higher than kcat/Km for NADPH
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?
2-nonyl-4(1H)-quinolone + NADH + H+ + O2
3-hydroxy-2-nonyl-4(1H)-quinolone + NAD+ + H2O
show the reaction diagram
the alkyl side chain of 2-heptyl-4-quinolone is critical for PqsH activity with the highest activity observed for alkyl chain lengths of 7 and 9 carbons
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2-pentyl-4(1H)-quinolone + NADH + H+ + O2
3-hydroxy-2-pentyl-4(1H)-quinolone + NAD+ + H2O
show the reaction diagram
the alkyl side chain of 2-heptyl-4-quinolone is critical for PqsH activity with the highest activity observed for alkyl chain lengths of 7 and 9 carbons
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2-propyl-4(1H)-quinolone + NADH + H+ + O2
3-hydroxy-2-propyl-4(1H)-quinolone + NAD+ + H2O
show the reaction diagram
the alkyl side chain of 2-heptyl-4-quinolone is critical for PqsH activity with the highest activity observed for alkyl chain lengths of 7 and 9 carbons
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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
2-heptyl-4(1H)-quinolone + NADH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
show the reaction diagram
Q9I0Q0
PqsH catalyzes the terminal step in biosynthesis of the Pseudomonas quinolone signal molecule 2-heptyl-3-hydroxy-4(1H)-quinolone. Under anaerobic conditions 2-heptyl-3-hydroxy-4(1H)-quinolone is not produced. The enzyme is a biochemical regulator of Pseudomonas quinolone signal controlled social behaviors in Pseudomonas aeruginosa
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
kcat/KM for NADH is 20fold higher than kcat/Km for NADPH
NADPH
kcat/KM for NADH is 20fold higher than kcat/Km for NADPH
riboflavin
flavin-dependent monooxygenase, riboflavin is included in the assay
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00011
2-heptyl-4(1H)-quinolone
pH 8.0, 25C
0.00013
2-nonyl-4(1H)-quinolone
pH 8.0, 25C
0.0016
2-pentyl-4(1H)-quinolone
pH 8.0, 25C
0.014
2-propyl-4(1H)-quinolone
pH 8.0, 25C
0.032
NADH
pH 8.0, 25C, cosubstrate: 2-heptyl-4(1H)-quinolone
0.74
NADPH
pH 8.0, 25C, cosubstrate: 2-heptyl-4(1H)-quinolone
0.00052
O2
pH 8.0, 25C, cosubstrate: 2-heptyl-4(1H)-quinolone
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.7
2-heptyl-4(1H)-quinolone
Pseudomonas aeruginosa
Q9I0Q0
pH 8.0, 25C
2.5
2-nonyl-4(1H)-quinolone
Pseudomonas aeruginosa
Q9I0Q0
pH 8.0, 25C
3
2-pentyl-4(1H)-quinolone
Pseudomonas aeruginosa
Q9I0Q0
pH 8.0, 25C
2.3
2-propyl-4(1H)-quinolone
Pseudomonas aeruginosa
Q9I0Q0
pH 8.0, 25C
3.2
NADH
Pseudomonas aeruginosa
Q9I0Q0
pH 8.0, 25C, cosubstrate: 2-heptyl-4(1H)-quinolone
3.8
NADPH
Pseudomonas aeruginosa
Q9I0Q0
pH 8.0, 25C, cosubstrate: 2-heptyl-4(1H)-quinolone
1.2
O2
Pseudomonas aeruginosa
Q9I0Q0
pH 8.0, 25C, cosubstrate: 2-heptyl-4(1H)-quinolone
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2455
2-heptyl-4(1H)-quinolone
Pseudomonas aeruginosa
Q9I0Q0
pH 8.0, 25C
12235
1900
2-nonyl-4(1H)-quinolone
Pseudomonas aeruginosa
Q9I0Q0
pH 8.0, 25C
42404
190
2-pentyl-4(1H)-quinolone
Pseudomonas aeruginosa
Q9I0Q0
pH 8.0, 25C
42405
17
2-propyl-4(1H)-quinolone
Pseudomonas aeruginosa
Q9I0Q0
pH 8.0, 25C
28935
100
NADH
Pseudomonas aeruginosa
Q9I0Q0
pH 8.0, 25C, cosubstrate: 2-heptyl-4(1H)-quinolone
8
5.1
NADPH
Pseudomonas aeruginosa
Q9I0Q0
pH 8.0, 25C, cosubstrate: 2-heptyl-4(1H)-quinolone
5
2308
O2
Pseudomonas aeruginosa
Q9I0Q0
pH 8.0, 25C, cosubstrate: 2-heptyl-4(1H)-quinolone
9
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 86000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, purified fusion protein can be stored for one week without loss of enzymatic activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression of recombinant enzyme in Escherichia coli both with and without a N-terminal fusion with the maltose binding protein
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is influenced by the las/rhl systems. Pseudomonas quinolone signal synthesis might be regulated by the balance between the expression of the pqsA-D/phnAB, pqsH, antABC, and catBCA gene loci
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