Information on EC 1.6.2.6 - leghemoglobin reductase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.6.2.6
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RECOMMENDED NAME
GeneOntology No.
leghemoglobin reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NAD(P)H + H+ + 2 ferrileghemoglobin = NAD(P)+ + 2 ferroleghemoglobin
show the reaction diagram
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-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
-
-
-
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reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
NAD(P)H:ferrileghemoglobin oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
60440-35-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bean
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-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ferricytochrome c + NAD(P)H
2 ferrocytochrome c + NAD(P)+ + H+
show the reaction diagram
-
reduced at 53% of leghemoglobin rate
-
?
2,6-dichloroindophenol + NADH
reduced 2,6-dichloroindophenol + NAD+
show the reaction diagram
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
NAD(P)H + ferrimyoglobin
NAD(P)+ + ferromyoglobin
show the reaction diagram
-
-
-
?
NADH + ferrileghemoglobin
NAD+ + ferroleghemoglobin
show the reaction diagram
-
-
-
?
NADH + H+ + ferrileghemoglobin
NAD+ + ferroleghemoglobin
show the reaction diagram
NADH + H+ + oxidized ferric rice non-symbiotic Hb1
NAD+ + + reduced ferric rice non-symbiotic Hb1
show the reaction diagram
-
-
-
-
?
NADH + lipoamide
NAD+ + ?
show the reaction diagram
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-
-
?
NADH + lipoamide
NAD+ + lipoamide
show the reaction diagram
-
recombinant enzyme, lipoamide-dependent NADH oxidation
-
?
NADPH + H+ + ferrileghemoglobin
NADP+ + ferroleghemoglobin
show the reaction diagram
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-
-
-
?
additional information
?
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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
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
show the reaction diagram
NADH + H+ + ferrileghemoglobin
NAD+ + ferroleghemoglobin
show the reaction diagram
-
-
-
-
?
NADPH + H+ + ferrileghemoglobin
NADP+ + ferroleghemoglobin
show the reaction diagram
-
-
-
-
?
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
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acetate
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slight
Amobarbital
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1 mM, 35% after 0.5-1 h, 80% after 4 h
arsenic acid
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arsenic trioxide
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catalase
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possibly H2O2 as reaction intermediate
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CdSO4
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Cu(NO3)2
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iodoacetamide
nicotinate
p-chloromercuribenzoate
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p-hydroxymercuribenzoate
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0.5 mM, slight inhibition
Phenylarsine oxide
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Quinacrine
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0.5 mM, 30-40% inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0063 - 0.088
ferrileghemoglobin
0.716 - 3.381
Lipoamide
0.0188 - 0.058
NADH
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6 - 6.2
ferrileghemoglobin
31 - 392
Lipoamide
137
NADH
recombinant FLbR-2
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.215
-
reduction of ferrileghemoglobin
0.216
-
reduction of ferrileghemoglobin
0.218
-
reduction of ferrileghemoglobin
0.388
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reduction of ferrileghemoglobin in the presence of O2
0.486
-
recombinant enzyme, reduction of ferrileghemoglobin
0.5
-
reduction of ferrileghemoglobin
1.85
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oxidation of NADH in the presence of O2, 30fold higher than in the absence of O2
2
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reduction of 2,6-dichlorophenolindophenol
2.565
-
reduction of 2,6-dichloroindophenol
4.47
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recombinant enzyme, reduction of 2,6-dichloroindophenol
4.5
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reduction of 2,6-dichloroindophenol in the presence of O2
4.89
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reduction of 2,6-dichlorophenolindophenol
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
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decrease of activity from 100% at pH 5.2, to 30% at pH 6.7, no measurements below 5.2
6.5
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reduction of ferrileghemoglobin
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 8.5
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no activity below and above
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
isoelectric focusing, pH-range 4.0-6.5
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
high mRNA level
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50030
electrospray mass spectrometry
54000
-
2 * 54000, SDS-PAGE
56000
-
2 * 56000, deduced from amino acid sequence
83000
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equilibrium ultracentrifugation
100000
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gel filtration
110000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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heat labile
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C
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0°C, 37 days, 96% activity retains
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, hydroxylapatite, ion exchange, gel filtration
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His Trap HP Ni-chelating resin column chromatography
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recombinant enzyme, Sepharose 6B, Probond
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recombinant FLbR2
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of cDNA
expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
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overexpression in Escherichia coli BL21
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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.6.2.6)
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)