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Literature summary for 1.5.1.37 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
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Cloned(Commentary)

Cloned (Comment) Organism
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

Inhibitors

Inhibitors Comment Organism Structure
NAD+ competitive enzyme inhibitor Pseudomonas putida

KM Value [mM]

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37000
-
 gel filtration Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida M4YFG7
-
-
Pseudomonas putida ATCC 17453 M4YFG7
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas putida

Storage Stability

Storage Stability Organism
4°C, stable over several days Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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+
-
 ?
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+
-
 ?
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+
-
 ?
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+
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 18000, SDS-PAGE Pseudomonas putida

Synonyms

Synonyms Comment Organism
flavin reductase
-
 Pseudomonas putida
Fred
-
 Pseudomonas putida

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30 35
-
 Pseudomonas putida

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
 the enzyme irreversibly unfolds with a half-life of about 80 min Pseudomonas putida
30 35 the half-life of the enzyme is 5 to 20 min Pseudomonas putida

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 6.5 in piperazine-HCl and phosphate buffer Pseudomonas putida
7.5
-
 Tris/HCl buffer Pseudomonas putida

Ki Value [mM]

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

General Information

General Information Comment Organism
metabolism the enzyme is involved in the degradation of (-)-camphor Pseudomonas putida

kcat/KM [mM/s]

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