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Information on EC 1.5.1.42 - FMN reductase (NADH) and Organism(s) Vibrio harveyi and UniProt Accession P43127
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1.5.1.42 FMN reductase (NADH)IUBMB Comments
The enzyme often forms a two-component system with monooxygenases. Unlike EC 1.5.1.38, FMN reductase (NADPH), and EC 1.5.1.39, FMN reductase [NAD(P)H], this enzyme has a strong preference for NADH over NADPH, although some activity with the latter is observed [1,2].
While FMN is the preferred substrate, FAD can also be used with much lower activity [1,3].
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Word Map
- 1.5.1.42
- luciferase
- monooxygenase
-
desulfurization
-
bioluminescent
- rhodococcus
-
biodesulfurization
- erythropolis
-
photobacterium
- dibenzothiophene
-
fossil
-
instantly
- p-hydroxyphenylacetate
-
cost-competitive
- baumannii
-
sigma54-dependent
-
petroleum
-
fmnh2-dependent
- phosphoreum
The taxonomic range for the selected organisms is: Vibrio harveyi
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
nadh-fmn oxidoreductase, hcba3, nadh:fmn-oxidoreductase, nadh-dependent fmn reductase, nadh-fmn reductase, nadh specific fmn reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NADH-dependent FMN reductase
-
-
-
-
NADH-FMN reductase
-
-
-
-
NADH:flavin oxidoreductase
-
-
-
-
NADH:FMN oxidoreductase
NADH:FMN oxidoreductase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FMNH2 + NAD+ = FMN + NADH + H+
the enzyme exhibits single displacement kinetics
-
SYSTEMATIC NAME
IUBMB Comments
FMNH2:NAD+ oxidoreductase
The enzyme often forms a two-component system with monooxygenases. Unlike EC 1.5.1.38, FMN reductase (NADPH), and EC 1.5.1.39, FMN reductase [NAD(P)H], this enzyme has a strong preference for NADH over NADPH, although some activity with the latter is observed [1,2].
While FMN is the preferred substrate, FAD can also be used with much lower activity [1,3].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
activity with FAD and NADPH is 0.5% of the activity with FMNH2 and NAD+
-
-
?
FAD + NADH + H+
FADH2 + NAD+
-
activity with FADH2 and NAD+ is 5% of the activity with FMNH2 and NAD+
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
activity with NADP+ and FMNH2 is only 10% of the activity with FMNH2 and NAD+
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
the affinity of the NADH-specific reductase is about 60 times greater for NADH than for NADPH
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
the NADH specific FMN reductase does dehydrogenate NADPH with a maximal velocity one-tenth of that for NADH
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
activity with NADP+ and FMNH2 is only 10% of the activity with FMNH2 and NAD+
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
the NADH specific FMN reductase does dehydrogenate NADPH with a maximal velocity one-tenth of that for NADH
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
activity with NADPH and FMNH2 is only 10% of the activity with FMNH2 and NAD+
NADH
-
the affinity of the NADH-specific reductase is about 60 times greater for NADH than for NADPH
NADPH
-
activity with NADPH and FMNH2 is only 10% of the activity with FMNH2 and NAD+
NADPH
-
the NADH specific FMN reductase does does dehydrogenate NADPH with a maximal velocity one-tenth of that for NADH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition by 0.01 mM 2,4-dinitrophenol, 0.2 mM dicoumarol, 0.1 mM rotenone
-
additional information
-
no inhibition by: 0.000325 M dicoumarol, 10 mM KCN, 1% Triton X-100
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
purity was too low to permit estimation of specific activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
bimodal, pH 5: 90% of maximal activity, pH 6.5: about 50% of maximal activity, pH 10: about 70% of maximal activity
5 - 8.6
-
the pH curve is bimodal, with maximal activity exhibited at pH 8.6, a minimum at pH 6.0. and a second maximum at pH 5.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gerlo, E.; Charlier, J.
Identification of NADH-specific and NADPH-specific FMN reductases in Beneckea harveyi
Eur. J. Biochem.
57
461-467
1975
Vibrio harveyi
Jablonski, E.; DeLuca, M.
Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi
Biochemistry
16
2932-2936
1977
Vibrio harveyi, Vibrio harveyi No. 392
Izumoto, Y.; Mori, T.; Yamamoto, K.
Cloning and nucleotide sequence of the gene for NADH:FMN oxidoreductase from Vibrio harveyi
Biochim. Biophys. Acta
1185
243-246
1994
Vibrio harveyi (P43127)
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