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Literature summary extracted from

  • Iwaki, H.; Grosse, S.; Bergeron, H.; Leisch, H.; Morley, K.; Hasegawa, Y.; Lau, P.C.
    Camphor pathway redux functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions (2013), Appl. Environ. Microbiol., 79, 3282-3293 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.37 to enable functional assessment of the two-component monooxygenase system in Baeyer-Villiger oxidations, recombinant plasmids expressing Fred (FMN reductase (NADH)) in tandem with the respective 2,5-diketocamphane- and 3,6-diketocamphane 1,2-monooxygenase-encoding genes in Escherichia coli are constructed Pseudomonas putida
1.5.1.42 to enable functional assessment of the two-component monooxygenase system in Baeyer-Villiger oxidations, recombinant plasmids expressing Fred (FMN reductase (NADH)) in tandem with the respective 2,5-diketocamphane- and 3,6-diketocamphane 1,2-monooxygenase-encoding genes in Escherichia coli are constructed Pseudomonas putida
1.14.14.108 to enable functional assessment of the two-component monooxygenase system in Baeyer-Villiger oxidations, a recombinant plasmid expressing Fred (FMN reductase (NADH)) in tandem with 2,5-DKCMO-encoding gene in Escherichia coli is constructed Pseudomonas putida
1.14.14.108 to enable functional assessment of the two-component monooxygenase system in Baeyer-Villiger oxidations, recombinant plasmids expressing Fred (FMN reductase (NADH)) in tandem with the respective 2,5-DKCMO- and 3,6-DKCMO-encoding genes in Escherichia coli are constructed Pseudomonas putida
1.14.14.155 to enable functional assessment of the two-component monooxygenase system in Baeyer-Villiger oxidations, a recombinant plasmid expressing Fred (FMN reductase (NADH)) in tandem with the 3,5-DKCMO-encoding gene in Escherichia coli is constructed Pseudomonas putida

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.37 NAD+ competitive enzyme inhibitor Pseudomonas putida
1.5.1.42 NAD+ competitive enzyme inhibitor Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.37 0.0036
-
 FMN pH 7.5, 25°C Pseudomonas putida
1.5.1.37 0.019
-
 FAD pH 7.5, 25°C Pseudomonas putida
1.5.1.37 0.032
-
 NADH pH 7.5, 25°C Pseudomonas putida
1.5.1.42 0.0036
-
 FMN pH 7.5, 25°C Pseudomonas putida
1.5.1.42 0.019
-
 FAD pH 7.5, 25°C Pseudomonas putida
1.5.1.42 0.032
-
 NADH pH 7.5, 25°C Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.37 37000
-
 gel filtration Pseudomonas putida
1.5.1.42 37200
-
 gel filtration Pseudomonas putida
1.14.14.108 40574
-
 calculated from sequence Pseudomonas putida
1.14.14.108 40702
-
 calculated from sequence Pseudomonas putida
1.14.14.108 41000
-
 SDS-PAGE Pseudomonas putida
1.14.14.108 60000
-
 gel filtration Pseudomonas putida
1.14.14.108 64000
-
 gel filtration Pseudomonas putida
1.14.14.155 42311
-
 calculated from sequence Pseudomonas putida
1.14.14.155 44000
-
 SDS-PAGE Pseudomonas putida
1.14.14.155 85000
-
 gel filtration Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.108 (+)-bornane-2,5-dione + FMNH2 + O2 Pseudomonas putida the enzyme is involved in the degradation of (-)-camphor (+)-5-oxo-1,2-campholide + FMN + H2O
-
 ?
1.14.14.108 (+)-bornane-2,5-dione + FMNH2 + O2 Pseudomonas putida ATCC 17453 the enzyme is involved in the degradation of (-)-camphor (+)-5-oxo-1,2-campholide + FMN + H2O
-
 ?
1.14.14.155 (-)-bornane-2,5-dione + O2 + FMNH2 Pseudomonas putida the enzyme is involved in the degradation of (-)-camphor (-)-5-oxo-1,2-campholide + FMN + H2O
-
 ?
1.14.14.155 (-)-bornane-2,5-dione + O2 + FMNH2 Pseudomonas putida ATCC 17453 the enzyme is involved in the degradation of (-)-camphor (-)-5-oxo-1,2-campholide + FMN + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.37 Pseudomonas putida M4YFG7
-
-
1.5.1.37 Pseudomonas putida ATCC 17453 M4YFG7
-
-
1.5.1.42 Pseudomonas putida M4YFG7
-
-
1.5.1.42 Pseudomonas putida ATCC 17453 M4YFG7
-
-
1.14.14.108 Pseudomonas putida M5AWY0
-
-
1.14.14.108 Pseudomonas putida Q6STM1
-
-
1.14.14.108 Pseudomonas putida ATCC 17453 M5AWY0
-
-
1.14.14.108 Pseudomonas putida ATCC 17453 Q6STM1
-
-
1.14.14.155 Pseudomonas putida D7UER1
-
-
1.14.14.155 Pseudomonas putida ATCC 17453 D7UER1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.37
-
 Pseudomonas putida
1.5.1.42
-
 Pseudomonas putida
1.14.14.108
-
 Pseudomonas putida
1.14.14.155
-
 Pseudomonas putida

Storage Stability

EC Number Storage Stability Organism
1.5.1.37 4°C, stable over several days Pseudomonas putida
1.5.1.42 4°C, stable over several days Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.37 FAD + NADH + H+ FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5 times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate Pseudomonas putida FADH2 + NAD+
-
 ?
1.5.1.37 FAD + NADH + H+ FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5 times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate Pseudomonas putida ATCC 17453 FADH2 + NAD+
-
 ?
1.5.1.37 FMN + NADH + H+ FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5 times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate Pseudomonas putida FMNH2 + NAD+
-
 ?
1.5.1.37 FMN + NADH + H+ FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5 times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate Pseudomonas putida ATCC 17453 FMNH2 + NAD+
-
 ?
1.5.1.42 FAD + NADH + H+ FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate Pseudomonas putida FADH2 + NAD+
-
 ?
1.5.1.42 FAD + NADH + H+ FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate Pseudomonas putida ATCC 17453 FADH2 + NAD+
-
 ?
1.5.1.42 FMN + NADH + H+ FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate Pseudomonas putida FMNH2 + NAD+
-
 ?
1.5.1.42 FMN + NADH + H+ FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate Pseudomonas putida ATCC 17453 FMNH2 + NAD+
-
 ?
1.14.14.108 (+)-bornane-2,5-dione + FMNH2 + O2 the enzyme is involved in the degradation of (-)-camphor Pseudomonas putida (+)-5-oxo-1,2-campholide + FMN + H2O
-
 ?
1.14.14.108 (+)-bornane-2,5-dione + FMNH2 + O2 the enzyme requires a dedicated NADH-FMN reductase (FMN reductase (NADH)), FMN-dependent two-component monooxygenase system Pseudomonas putida (+)-5-oxo-1,2-campholide + FMN + H2O
-
 ?
1.14.14.108 (+)-bornane-2,5-dione + FMNH2 + O2 the enzyme is involved in the degradation of (-)-camphor Pseudomonas putida ATCC 17453 (+)-5-oxo-1,2-campholide + FMN + H2O
-
 ?
1.14.14.108 (+)-bornane-2,5-dione + FMNH2 + O2 the enzyme requires a dedicated NADH-FMN reductase (FMN reductase (NADH)), FMN-dependent two-component monooxygenase system Pseudomonas putida ATCC 17453 (+)-5-oxo-1,2-campholide + FMN + H2O
-
 ?
1.14.14.108 (+)-camphor + FMNH2 + O2 conversion to lactone, no concersion of (-)-camphor Pseudomonas putida ?
-
 ?
1.14.14.108 (+)-camphor + FMNH2 + O2 conversion to lactone, no concersion of (-)-camphor Pseudomonas putida ATCC 17453 ?
-
 ?
1.14.14.155 (-)-bornane-2,5-dione + O2 + FMNH2 the enzyme is involved in the degradation of (-)-camphor Pseudomonas putida (-)-5-oxo-1,2-campholide + FMN + H2O
-
 ?
1.14.14.155 (-)-bornane-2,5-dione + O2 + FMNH2 the enzyme requires a dedicated NADH-FMN reductase (FMN reductase (NADH)), FMN-dependent two-component monooxygenase system Pseudomonas putida (-)-5-oxo-1,2-campholide + FMN + H2O
-
 ?
1.14.14.155 (-)-bornane-2,5-dione + O2 + FMNH2 the enzyme is involved in the degradation of (-)-camphor Pseudomonas putida ATCC 17453 (-)-5-oxo-1,2-campholide + FMN + H2O
-
 ?
1.14.14.155 (-)-bornane-2,5-dione + O2 + FMNH2 the enzyme requires a dedicated NADH-FMN reductase (FMN reductase (NADH)), FMN-dependent two-component monooxygenase system Pseudomonas putida ATCC 17453 (-)-5-oxo-1,2-campholide + FMN + H2O
-
 ?
1.14.14.155 (-)-camphor + FMNH2 + O2 conversion to lactone, no conversion of (+)-camphor Pseudomonas putida ?
-
 ?
1.14.14.155 (-)-camphor + FMNH2 + O2 conversion to lactone, no conversion of (+)-camphor Pseudomonas putida ATCC 17453 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.1.37 homodimer 2 * 18000, SDS-PAGE Pseudomonas putida
1.5.1.42 homodimer 2 * 18000, SDS-PAGE Pseudomonas putida
1.14.14.108 dimer 2 * 41000, SDS-PAGE Pseudomonas putida
1.14.14.155 dimer 2 * 44000, SDS-PAGE Pseudomonas putida

Synonyms

EC Number Synonyms Comment Organism
1.5.1.37 flavin reductase
-
 Pseudomonas putida
1.5.1.37 Fred
-
 Pseudomonas putida
1.5.1.42 flavin reductase
-
 Pseudomonas putida
1.5.1.42 Fred
-
 Pseudomonas putida
1.14.14.108 2,5-diketocamphane monooxygenase
-
 Pseudomonas putida
1.14.14.108 2,5-DKCMO-1
-
 Pseudomonas putida
1.14.14.108 2,5-DKCMO-2
-
 Pseudomonas putida
1.14.14.108 camE25-1 gene name, two isofunctional 2,5-DKCMO genes (camE25-1 for 2,5-DKCMO-1 and camE25-2 for 2,5-DKCMO-2) Pseudomonas putida
1.14.14.108 camE25-2 gene name, two isofunctional 2,5-DKCMO genes (camE25-1 for 2,5-DKCMO-1 and camE25-2 for 2,5-DKCMO-2) Pseudomonas putida
1.14.14.155 3,6-diketocamphane monooxygenase
-
 Pseudomonas putida
1.14.14.155 3,6-DKCMO
-
 Pseudomonas putida
1.14.14.155 camE36
-
 Pseudomonas putida

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.37 30 35
-
 Pseudomonas putida
1.5.1.42 30 35
-
 Pseudomonas putida

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.5.1.37 25
-
 the enzyme irreversibly unfolds with a half-life of about 80 min Pseudomonas putida
1.5.1.37 30 35 the half-life of the enzyme is 5 to 20 min Pseudomonas putida
1.5.1.42 25
-
 the enzyme irreversibly unfolds with a half-life of about 80 min Pseudomonas putida
1.5.1.42 30 35 the half-life of the enzyme is 5 to 20 min Pseudomonas putida
1.14.14.108 56
-
 Tm-value Pseudomonas putida
1.14.14.108 63
-
 Tm-value Pseudomonas putida
1.14.14.155 47
-
 Tm-value Pseudomonas putida

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.1.37 128
-
 FAD pH 7.5, 25°C Pseudomonas putida
1.5.1.37 283
-
 FMN pH 7.5, 25°C Pseudomonas putida
1.5.1.42 128
-
 FAD pH 7.5, 25°C Pseudomonas putida
1.5.1.42 283
-
 FMN pH 7.5, 25°C Pseudomonas putida

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.37 5 6.5 in piperazine-HCl and phosphate buffer Pseudomonas putida
1.5.1.37 7.5
-
 Tris/HCl buffer Pseudomonas putida
1.5.1.42 5 6.5 in piperazine-HCl and phosphate buffer Pseudomonas putida
1.5.1.42 7.5
-
 Tris/HCl buffer Pseudomonas putida
1.14.14.108 7.5
-
-
 Pseudomonas putida
1.14.14.108 8
-
-
 Pseudomonas putida
1.14.14.155 7
-
-
 Pseudomonas putida

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.5.1.37 40
-
 NAD+ pH 7.5, 25°C Pseudomonas putida
1.5.1.42 40
-
 NAD+ pH 7.5, 25°C Pseudomonas putida

General Information

EC Number General Information Comment Organism
1.5.1.37 metabolism the enzyme is involved in the degradation of (-)-camphor Pseudomonas putida
1.5.1.42 metabolism the enzyme is involved in the degradation of (-)-camphor Pseudomonas putida
1.14.14.108 metabolism the enzyme is involved in the degradation of (-)-camphor Pseudomonas putida
1.14.14.155 metabolism the enzyme is involved in the degradation of (-)-camphor Pseudomonas putida

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.5.1.37 6700
-
 FAD pH 7.5, 25°C Pseudomonas putida
1.5.1.37 7900
-
 FMN pH 7.5, 25°C Pseudomonas putida
1.5.1.42 6700
-
 FAD pH 7.5, 25°C Pseudomonas putida
1.5.1.42 7900
-
 FMN pH 7.5, 25°C Pseudomonas putida