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Information on EC 1.5.1.37 - FAD reductase (NADH) and Organism(s) Pseudomonas putida and UniProt Accession M4YFG7

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EC Tree
     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.37 FAD reductase (NADH)
IUBMB Comments
The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. Unlike EC 1.5.1.36, flavin reductase (NADH), the enzyme can not reduce riboflavin. The enzyme does not use NADPH as acceptor.
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This record set is specific for:
Pseudomonas putida
UNIPROT: M4YFG7
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas putida
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
sgce6, nadh-fad reductase, nadh:fad oxidoreductase, fad:nadh reductase, nad(p)h:fad reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
flavin reductase
-
NADH-dependent FAD reductase
-
-
-
-
NADH-FAD reductase
-
-
-
-
NADH:FAD oxidoreductase
-
-
-
-
NADH:flavin adenine dinucleotide oxidoreductase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
FADH2:NAD+ oxidoreductase
The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. Unlike EC 1.5.1.36, flavin reductase (NADH), the enzyme can not reduce riboflavin. The enzyme does not use NADPH as acceptor.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
FAD + NADH + H+
FADH2 + NAD+
show the reaction diagram
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
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
show the reaction diagram
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
competitive enzyme inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019
FAD
pH 7.5, 25°C
0.0036
FMN
pH 7.5, 25°C
0.032
NADH
pH 7.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
128
FAD
pH 7.5, 25°C
283
FMN
pH 7.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6700
FAD
pH 7.5, 25°C
7900
FMN
pH 7.5, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
40
NAD+
pH 7.5, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6.5
in piperazine-HCl and phosphate buffer
7.5
Tris/HCl buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is involved in the degradation of (-)-camphor
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FRED_PSEPU
170
0
18356
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 18000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
the enzyme irreversibly unfolds with a half-life of about 80 min
30 - 35
the half-life of the enzyme is 5 to 20 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable over several days
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Appl. Environ. Microbiol.
79
3282-3293
2013
Pseudomonas putida (M4YFG7), Pseudomonas putida ATCC 17453 (M4YFG7)
Manually annotated by BRENDA team