Information on EC 1.6.2.6 - leghemoglobin reductase

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The expected taxonomic range for this enzyme is: Phaseoleae

EC NUMBER
COMMENTARY
1.6.2.6
-
RECOMMENDED NAME
GeneOntology No.
leghemoglobin reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
NAD(P)H + H+ + 2 ferrileghemoglobin = NAD(P)+ + 2 ferroleghemoglobin
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
NAD(P)H:ferrileghemoglobin oxidoreductase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ferric leghemoglobin reductase
-
-
-
-
FLbR-2
O81413
-
FLbR2
-
-
CAS REGISTRY NUMBER
COMMENTARY
60440-35-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,6-dichloroindophenol + NADH
reduced 2,6-dichloroindophenol + NAD+
show the reaction diagram
-
-
-
?
NAD(P)H + ferricytochrome c
NAD(P)+ + ferrocytochrome c
show the reaction diagram
-
reduced at 53% of leghemoglobin rate
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
-
-
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
-
-
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
-
-
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
-
-
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
-
-
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
-
no activity in the absence of O2, formation of H2O2 or peroxide intermediates during NADH oxidation
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
-
reduces both cowpea ferrihemoglobin and soybean ferrileghemoglobin
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
-
31% activity with NADPH
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
-
proposed to be involved in maintaining leghemoglobin in an active form in legume nodules
-
-
NAD(P)H + ferrimyoglobin
NAD(P)+ + ferromyoglobin
show the reaction diagram
-
-
-
?
NADH + ferrileghemoglobin
NAD+ + ferroleghemoglobin
show the reaction diagram
-, O81413
-
-
-
?
NADH + H+ + ferrileghemoglobin
NAD+ + ferroleghemoglobin
show the reaction diagram
-
-
-
-
-
NADH + lipoamide
NAD+ + lipoamide
show the reaction diagram
-
recombinant enzyme, lipoamide-dependent NADH oxidation
-
?
NADH + lipoamide
NAD+ + ?
show the reaction diagram
-, O81413
-
-
-
?
2,6-dichloroindophenol + NADH
reduced 2,6-dichloroindophenol + NAD+
show the reaction diagram
-
no activity in the absence of
-
?
additional information
?
-
-
reactive nitrogen species are able to react with two inactive forms (in terms of oxygen binding) of leghemoglobin: ferryl-leghemoglobin and nitrosyl-leghemoglobin. In both cases, the product of the reactions is metleghemoglobin. As metleghemoglobin can be reduced by a reductase found in the nodules, reactive nitrogen species could contribute to the recycling of these inactive forms to regenerate deoxyLb, the oxygen-binding form of Lb
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
-
-
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
-
-
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
-
-
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
-
-
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
-
proposed to be involved in maintaining leghemoglobin in an active form in legume nodules
-
-
additional information
?
-
-
reactive nitrogen species are able to react with two inactive forms (in terms of oxygen binding) of leghemoglobin: ferryl-leghemoglobin and nitrosyl-leghemoglobin. In both cases, the product of the reactions is metleghemoglobin. As metleghemoglobin can be reduced by a reductase found in the nodules, reactive nitrogen species could contribute to the recycling of these inactive forms to regenerate deoxyLb, the oxygen-binding form of Lb
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
O81413
not covalently bound to the protein
NADPH
-
31% of NADH activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
acetate
-
slight
Amobarbital
-
1 mM, 35% after 0.5-1 h, 80% after 4 h
arsenic acid
-
-
arsenic trioxide
-
-
catalase
-
possibly H2O2 as reaction intermediate
-
Cu(NO3)2
-
-
iodoacetamide
-
-
iodoacetamide
-
1 mM, 95-100% inhibition
nicotinate
-
-
nicotinate
-
ferrileghemoglobin-nitrite complex
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
0.5 mM, slight inhibition
Phenylarsine oxide
-
-
Quinacrine
-
0.5 mM, 30-40% inhibition
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0063
-
ferrileghemoglobin
-
recombinant enzyme
0.0092
-
ferrileghemoglobin
-
native enzyme
0.0095
-
ferrileghemoglobin
-
-
0.0104
-
ferrileghemoglobin
-
cowpea ferrileghemoglobin
0.0124
-
ferrileghemoglobin
-
soybean ferrileghemoglobin
0.0133
-
ferrileghemoglobin
-
-
0.029
-
ferrileghemoglobin
O81413
recombinant FLbR-2
0.088
-
ferrileghemoglobin
-
-
0.716
-
Lipoamide
-
lipoamide-dependent NADH oxidation
3.381
-
Lipoamide
O81413
recombinant FLbR-2
0.0188
-
NADH
-
-
0.046
-
NADH
-
lipoamide-dependent NADH oxidation
0.051
-
NADH
-
-
0.057
-
NADH
-
-
0.058
-
NADH
O81413
recombinant FLbR-2
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.6
-
ferrileghemoglobin
O81413
recombinant FLbR-2
2.5
-
ferrileghemoglobin
-
soybean ferrileghemoglobin
3.1
-
ferrileghemoglobin
-
cowpea ferrileghemoglobin
6.2
-
ferrileghemoglobin
-
native enzyme; recombinant enzyme
31
-
Lipoamide
-
recombinant enzyme
392
-
Lipoamide
O81413
recombinant FLbR-2
137
-
NADH
O81413
recombinant FLbR-2
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.215
-
-
reduction of ferrileghemoglobin
0.216
-
-
reduction of ferrileghemoglobin
0.218
-
-
reduction of ferrileghemoglobin
0.388
-
-
reduction of ferrileghemoglobin in the presence of O2
0.486
-
-
recombinant enzyme, reduction of ferrileghemoglobin
0.5
-
-
reduction of ferrileghemoglobin
1.85
-
-
oxidation of NADH in the presence of O2, 30fold higher than in the absence of O2
2
-
-
reduction of 2,6-dichlorophenolindophenol
2.565
-
-
reduction of 2,6-dichloroindophenol
4.47
-
-
recombinant enzyme, reduction of 2,6-dichloroindophenol
4.5
-
-
reduction of 2,6-dichloroindophenol in the presence of O2
4.89
-
-
reduction of 2,6-dichlorophenolindophenol
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.2
-
-
decrease of activity from 100% at pH 5.2, to 30% at pH 6.7, no measurements below 5.2
6.5
-
-
reduction of ferrileghemoglobin
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.8
8.5
-
no activity below and above
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.8
-
O81413
isoelectric focusing, pH-range 4.0-6.5
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
high mRNA level
Manually annotated by BRENDA team
-
high mRNA level
Manually annotated by BRENDA team
-
low mRNA level
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50030
-
O81413
electrospray mass spectrometry
83000
-
-
equilibrium ultracentrifugation
100000
-
-
gel filtration
110000
-
-
gel filtration
110000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 55000, SDS-PAGE; 2 * 56000, deduced from amino acid sequence
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
heat labile
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70°C
-
0°C, 37 days, 96% activity retains
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme, Sepharose 6B, Probond
-
recombinant FLbR2
-
ammonium sulfate, hydroxylapatite, ion exchange, gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloning of cDNA
-
expression in Escherichia coli
-
overexpression in Escherichia coli BL21
O81413
production of a recombinant FLbR-2 from Escherichia coli BL21(DE3) by using an overexpression method based on the self-induction of the recombinant Escherichia coli
-
cloning of cDNA
-