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Information on EC 1.14.13.182 - 2-heptyl-3-hydroxy-4(1H)-quinolone synthase
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1.14.13.182 2-heptyl-3-hydroxy-4(1H)-quinolone synthaseIUBMB Comments
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.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
2-heptyl-3,4-dihydroxyquinoline synthase, Aqm, PqsH, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aqm
PqsH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-heptyl-4(1H)-quinolone + NADH + H+ + O2 = 2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-heptyl-1-hydroxyquinolin-4(1H)-one + NADH + H+ + O2
2-heptyl-1,3-dihydroxy-4(1H)-quinolone + NAD+ + H2O
2-heptyl-1-hydroxyquinolin-4(1H)-one one + NADH + H+ + O2
2-heptyl-1,3-dihydroxy-4(1H)-quinolone + NAD+ + H2O
2-heptyl-4(1H)-quinolone + NADPH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NADP+ + H2O
kcat/KM for NADH is 20fold higher than kcat/Km for NADPH
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-
?
2-heptylquinolin-4(1H)-one + NADH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
2-nonyl-4(1H)-quinolone + NADH + H+ + O2
3-hydroxy-2-nonyl-4(1H)-quinolone + NAD+ + H2O
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
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-pentylquinolin-4(1H)-one + NADH + H+ + O2
3-hydroxy-2-pentyl-4(1H)-quinolone + NAD+ + H2O
2-propyl-4(1H)-quinolone + NADH + H+ + O2
3-hydroxy-2-propyl-4(1H)-quinolone + NAD+ + H2O
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-heptyl-1-hydroxyquinolin-4(1H)-one + NADH + H+ + O2
2-heptyl-1,3-dihydroxy-4(1H)-quinolone + NAD+ + H2O
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-
-
?
2-heptyl-1-hydroxyquinolin-4(1H)-one + NADH + H+ + O2
2-heptyl-1,3-dihydroxy-4(1H)-quinolone + NAD+ + H2O
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-
-
?
2-heptyl-1-hydroxyquinolin-4(1H)-one + NADH + H+ + O2
2-heptyl-1,3-dihydroxy-4(1H)-quinolone + NAD+ + H2O
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-
-
?
2-heptyl-1-hydroxyquinolin-4(1H)-one + NADH + H+ + O2
2-heptyl-1,3-dihydroxy-4(1H)-quinolone + NAD+ + H2O
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-
-
?
2-heptyl-1-hydroxyquinolin-4(1H)-one one + NADH + H+ + O2
2-heptyl-1,3-dihydroxy-4(1H)-quinolone + NAD+ + H2O
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-
-
-
?
2-heptyl-1-hydroxyquinolin-4(1H)-one one + NADH + H+ + O2
2-heptyl-1,3-dihydroxy-4(1H)-quinolone + NAD+ + H2O
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-
-
?
2-heptyl-1-hydroxyquinolin-4(1H)-one one + NADH + H+ + O2
2-heptyl-1,3-dihydroxy-4(1H)-quinolone + NAD+ + H2O
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-
-
?
2-heptyl-4(1H)-quinolone + NADH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
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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-
?
2-heptyl-4(1H)-quinolone + NADH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
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
-
-
?
2-heptylquinolin-4(1H)-one + NADH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
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2-heptylquinolin-4(1H)-one and 2-nonylquinolin-4(1H)-one, preferred substrates
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-
?
2-heptylquinolin-4(1H)-one + NADH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
preferred substrate
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-
?
2-heptylquinolin-4(1H)-one + NADH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
preferred substrate
-
-
?
2-heptylquinolin-4(1H)-one + NADH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
2-heptylquinolin-4(1H)-one and 2-nonylquinolin-4(1H)-one, preferred substrates
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-
?
2-heptylquinolin-4(1H)-one + NADH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
2-heptylquinolin-4(1H)-one and 2-nonylquinolin-4(1H)-one, preferred substrates
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-
?
2-heptylquinolin-4(1H)-one + NADH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
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?
2-heptylquinolin-4(1H)-one + NADH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
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-
-
?
2-nonylquinolin-4(1H)-one + NADH + H+ + O2
3-hydroxy-2-nonyl-4(1H)-quinolone + NAD+ + H2O
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2-heptylquinolin-4(1H)-one and 2-nonylquinolin-4(1H)-one, preferred substrates
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-
?
2-nonylquinolin-4(1H)-one + NADH + H+ + O2
3-hydroxy-2-nonyl-4(1H)-quinolone + NAD+ + H2O
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-
-
?
2-nonylquinolin-4(1H)-one + NADH + H+ + O2
3-hydroxy-2-nonyl-4(1H)-quinolone + NAD+ + H2O
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-
-
?
2-nonylquinolin-4(1H)-one + NADH + H+ + O2
3-hydroxy-2-nonyl-4(1H)-quinolone + NAD+ + H2O
2-heptylquinolin-4(1H)-one and 2-nonylquinolin-4(1H)-one, preferred substrates
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-
?
2-nonylquinolin-4(1H)-one + NADH + H+ + O2
3-hydroxy-2-nonyl-4(1H)-quinolone + NAD+ + H2O
2-heptylquinolin-4(1H)-one and 2-nonylquinolin-4(1H)-one, preferred substrates
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-
?
2-nonylquinolin-4(1H)-one + NADH + H+ + O2
3-hydroxy-2-nonyl-4(1H)-quinolone + NAD+ + H2O
preferred substrate
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-
?
2-nonylquinolin-4(1H)-one + NADH + H+ + O2
3-hydroxy-2-nonyl-4(1H)-quinolone + NAD+ + H2O
preferred substrate
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-
?
2-pentylquinolin-4(1H)-one + NADH + H+ + O2
3-hydroxy-2-pentyl-4(1H)-quinolone + NAD+ + H2O
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-
-
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?
2-pentylquinolin-4(1H)-one + NADH + H+ + O2
3-hydroxy-2-pentyl-4(1H)-quinolone + NAD+ + H2O
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-
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?
2-pentylquinolin-4(1H)-one + NADH + H+ + O2
3-hydroxy-2-pentyl-4(1H)-quinolone + NAD+ + H2O
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-
-
?
2-pentylquinolin-4(1H)-one + NADH + H+ + O2
3-hydroxy-2-pentyl-4(1H)-quinolone + NAD+ + H2O
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-
-
?
2-pentylquinolin-4(1H)-one + NADH + H+ + O2
3-hydroxy-2-pentyl-4(1H)-quinolone + NAD+ + H2O
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-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-heptyl-4(1H)-quinolone + NADH + H+ + O2
2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O
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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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
riboflavin
flavin-dependent monooxygenase, riboflavin is included in the assay
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AQDB_MYCA9
Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543)
375
1
39751
Swiss-Prot
-
PQSH_PSEAB
Pseudomonas aeruginosa (strain UCBPP-PA14)
382
0
42054
Swiss-Prot
-
PQSH_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
382
0
42081
Swiss-Prot
-
A0A2P2E895_9PROT
414
0
44815
TrEMBL
-
A0A5K1JUD1_9APHY
611
1
67585
TrEMBL
other Location (Reliability: 2)
A0A346BKD2_9BURK
377
1
40048
TrEMBL
-
A0A6J5FI20_9BURK
375
0
40186
TrEMBL
-
A0A0H3KID8_STAAE
Staphylococcus aureus (strain Newman)
374
0
41890
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified fusion protein can be stored for one week without loss of enzymatic activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression of recombinant enzyme in Escherichia coli both with and without a N-terminal fusion with the maltose binding protein
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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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farnesol suppresses the transcription and protein expression. Farnesol inhibits the expression of PQS signal synthase coding genes (pqsABCDE and pqsH) in the PQS system, but does not inhibit the expression of the PQS signal receptor coding gene pqsR
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Choi, Y.; Park, H.Y.; Park, S.J.; Park, S.J.; Kim, S.K.; Ha, C.; Im, S.J.; Lee, J.H.
Growth phase-differential quorum sensing regulation of anthranilate metabolism in Pseudomonas aeruginosa
Mol. Cells
32
57-65
2011
Pseudomonas aeruginosa
brenda
Schertzer, J.W., Brown, S.A.; Whiteley, M.
Oxygen levels rapidly modulate Pseudomonas aeruginosa social behaviours via substrate limitation of PqsH
Mol. Microbiol.
77
1527-1538
2010
Pseudomonas aeruginosa (Q9I0Q0)
brenda
Ritzmann, N.; Drees, S.; Fetznera, S.
Signal synthase-type versus catabolic monooxygenases retracing 3-hydroxylation of 2-alkylquinolones and their N-oxides by Pseudomonas aeruginosa and other pulmonary pathogens
Appl. Environ. Microbiol.
87
e02241
2021
Microbulbifer sp. HZ11, Mycobacteroides abscessus (B1MFK1), Pseudomonas aeruginosa (Q9I0Q0), Mycobacteroides abscessus DSM 44196 (B1MFK1), Pseudomonas aeruginosa DSM 22644 (Q9I0Q0)
brenda
Ritzmann, N.; Drees, S.; Fetznera, S.
Signal synthase-type versus catabolic monooxygenases retracing 3-hydroxylation of 2-alkylquinolones and their N-oxides by Pseudomonas aeruginosa and other pulmonary pathogens
Appl. Environ. Microbiol.
87
e02241-20
2021
Staphylococcus aureus (A0A0H3KID8), Staphylococcus aureus Newman (A0A0H3KID8)
brenda
Li, W.; Zeng, T.; Xie, X.; Shi, Q.; Li, C.
Inhibition of the pqsABCDE and pqsH in the pqs quorum sensing system and related virulence factors of the Pseudomonas aeruginosa PAO1 strain by farnesol
Int. Biodeter. Biodegrad.
151
104956
2020
Pseudomonas aeruginosa (Q9I0Q0)
-
brenda
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Release 2023.1 (January 2023)
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