Information on EC 1.5.1.45 - FAD reductase [NAD(P)H]

for references in articles please use BRENDA:EC1.5.1.45
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Geobacillus thermodenitrificans

top print hide
EC NUMBER
COMMENTARY hide
1.5.1.45
-
top print hide
RECOMMENDED NAME
GeneOntology No.
FAD reductase [NAD(P)H]
-
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
FADH2 + NAD(P)+ = FAD + NAD(P)H + H+
show the reaction diagram
-
-
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Riboflavin metabolism
-
-
Metabolic pathways
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
FADH2:NAD(P)+ oxidoreductase
This enzyme, isolated from the bacterium Geobacillus thermodenitrificans, participates in the pathway of tryptophan degradation. The enzyme is part of a system that also includes a bifunctional riboflavin kinase/FMN adenylyltransferase and EC 1.14.14.8, anthranilate 3-monooxygenase (FAD). It can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. The enzyme has a slight preference for NADPH as acceptor. cf. EC 1.5.1.37, FAD reductase (NADH).
top
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
top print hide
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
-
95% activity with NADH relative to NADPH
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
show the reaction diagram
-
higher activity is obtained with FAD than with FMN using NADPH as the cofactor
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
show the reaction diagram
-
higher activity is obtained with FAD than with FMN using NADPH as the cofactor
-
-
?
additional information
?
-
-
anthranilate can also be oxidized to 3-hydroxyanthranilate by GTNG_3158 in the presence of FMN and ATP
-
-
-
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55.47
-
using FMN and NADPH as substrates, in 20 mM glycine/NaOH (pH 9.0), at 60°C
58.2
-
using FAD and NADPH as substrates, in 20 mM glycine/NaOH (pH 9.0), at 60°C
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chelating Sepharose column chromatography
-
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
top
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 1.5.1.45)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)