Any feedback?
Literature summary extracted from
- Oxygen levels rapidly modulate Pseudomonas aeruginosa social behaviours via substrate limitation of PqsH (2010), Mol. Microbiol., 77, 1527-1538.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.13.182 | overexpression of recombinant enzyme in Escherichia coli both with and without a N-terminal fusion with the maltose binding protein | Pseudomonas aeruginosa |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.13.182 | 0.00011 | - |
2-heptyl-4(1H)-quinolone | pH 8.0, 25°C | Pseudomonas aeruginosa |  |
| 1.14.13.182 | 0.00013 | - |
2-nonyl-4(1H)-quinolone | pH 8.0, 25°C | Pseudomonas aeruginosa | |
| 1.14.13.182 | 0.00052 | - |
O2 | pH 8.0, 25°C, cosubstrate: 2-heptyl-4(1H)-quinolone | Pseudomonas aeruginosa | |
| 1.14.13.182 | 0.0016 | - |
2-pentyl-4(1H)-quinolone | pH 8.0, 25°C | Pseudomonas aeruginosa | |
| 1.14.13.182 | 0.014 | - |
2-propyl-4(1H)-quinolone | pH 8.0, 25°C | Pseudomonas aeruginosa | |
| 1.14.13.182 | 0.032 | - |
NADH | pH 8.0, 25°C, cosubstrate: 2-heptyl-4(1H)-quinolone | Pseudomonas aeruginosa | |
| 1.14.13.182 | 0.74 | - |
NADPH | pH 8.0, 25°C, cosubstrate: 2-heptyl-4(1H)-quinolone | Pseudomonas aeruginosa | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.182 | 86000 | - |
x * 86000, SDS-PAGE | Pseudomonas aeruginosa |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.13.182 | 2-heptyl-4(1H)-quinolone + NADH + H+ + O2 | Pseudomonas aeruginosa | 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 | 2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.13.182 | Pseudomonas aeruginosa | Q9I0Q0 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.13.182 | - |
Pseudomonas aeruginosa |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.14.13.182 | -80°C, purified fusion protein can be stored for one week without loss of enzymatic activity | Pseudomonas aeruginosa |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.13.182 | 2-heptyl-4(1H)-quinolone + NADH + H+ + O2 | 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 | Pseudomonas aeruginosa | 2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O | - |
? | |
| 1.14.13.182 | 2-heptyl-4(1H)-quinolone + NADH + H+ + O2 | 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 | Pseudomonas aeruginosa | 2-heptyl-3-hydroxy-4(1H)-quinolone + NAD+ + H2O | - |
? | |
| 1.14.13.182 | 2-heptyl-4(1H)-quinolone + NADPH + H+ + O2 | kcat/KM for NADH is 20fold higher than kcat/Km for NADPH | Pseudomonas aeruginosa | 2-heptyl-3-hydroxy-4(1H)-quinolone + NADP+ + H2O | - |
? | |
| 1.14.13.182 | 2-nonyl-4(1H)-quinolone + NADH + H+ + O2 | 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 | Pseudomonas aeruginosa | 3-hydroxy-2-nonyl-4(1H)-quinolone + NAD+ + H2O | - |
? | |
| 1.14.13.182 | 2-pentyl-4(1H)-quinolone + NADH + H+ + O2 | 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 | Pseudomonas aeruginosa | 3-hydroxy-2-pentyl-4(1H)-quinolone + NAD+ + H2O | - |
? | |
| 1.14.13.182 | 2-propyl-4(1H)-quinolone + NADH + H+ + O2 | 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 | Pseudomonas aeruginosa | 3-hydroxy-2-propyl-4(1H)-quinolone + NAD+ + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.13.182 | ? | x * 86000, SDS-PAGE | Pseudomonas aeruginosa |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.13.182 | 2-heptyl-3,4-dihydroxyquinoline synthase | - |
Pseudomonas aeruginosa |
| 1.14.13.182 | PqsH | - |
Pseudomonas aeruginosa |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.182 | 25 | - |
assay at | Pseudomonas aeruginosa |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.13.182 | 1.2 | - |
O2 | pH 8.0, 25°C, cosubstrate: 2-heptyl-4(1H)-quinolone | Pseudomonas aeruginosa | |
| 1.14.13.182 | 2.3 | - |
2-propyl-4(1H)-quinolone | pH 8.0, 25°C | Pseudomonas aeruginosa | |
| 1.14.13.182 | 2.5 | - |
2-nonyl-4(1H)-quinolone | pH 8.0, 25°C | Pseudomonas aeruginosa | |
| 1.14.13.182 | 2.7 | - |
2-heptyl-4(1H)-quinolone | pH 8.0, 25°C | Pseudomonas aeruginosa | |
| 1.14.13.182 | 3 | - |
2-pentyl-4(1H)-quinolone | pH 8.0, 25°C | Pseudomonas aeruginosa | |
| 1.14.13.182 | 3.2 | - |
NADH | pH 8.0, 25°C, cosubstrate: 2-heptyl-4(1H)-quinolone | Pseudomonas aeruginosa | |
| 1.14.13.182 | 3.8 | - |
NADPH | pH 8.0, 25°C, cosubstrate: 2-heptyl-4(1H)-quinolone | Pseudomonas aeruginosa | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.182 | 8 | - |
assay at | Pseudomonas aeruginosa |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.182 | NADH | kcat/KM for NADH is 20fold higher than kcat/Km for NADPH | Pseudomonas aeruginosa | |
| 1.14.13.182 | NADPH | kcat/KM for NADH is 20fold higher than kcat/Km for NADPH | Pseudomonas aeruginosa | |
| 1.14.13.182 | riboflavin | flavin-dependent monooxygenase, riboflavin is included in the assay | Pseudomonas aeruginosa | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.13.182 | 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 | Pseudomonas aeruginosa |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.13.182 | 5.1 | - |
NADPH | pH 8.0, 25°C, cosubstrate: 2-heptyl-4(1H)-quinolone | Pseudomonas aeruginosa | |
| 1.14.13.182 | 17 | - |
2-propyl-4(1H)-quinolone | pH 8.0, 25°C | Pseudomonas aeruginosa | |
| 1.14.13.182 | 100 | - |
NADH | pH 8.0, 25°C, cosubstrate: 2-heptyl-4(1H)-quinolone | Pseudomonas aeruginosa | |
| 1.14.13.182 | 190 | - |
2-pentyl-4(1H)-quinolone | pH 8.0, 25°C | Pseudomonas aeruginosa | |
| 1.14.13.182 | 1900 | - |
2-nonyl-4(1H)-quinolone | pH 8.0, 25°C | Pseudomonas aeruginosa | |
| 1.14.13.182 | 2308 | - |
O2 | pH 8.0, 25°C, cosubstrate: 2-heptyl-4(1H)-quinolone | Pseudomonas aeruginosa | |
| 1.14.13.182 | 2455 | - |
2-heptyl-4(1H)-quinolone | pH 8.0, 25°C | Pseudomonas aeruginosa | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
