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Information on EC 1.6.2.6 - leghemoglobin reductase
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1.6.2.6 leghemoglobin reductaseSpecify your search results
Word Map
- 1.6.2.6
- soybean
- nodules
- dihydrolipoamide
-
ferrous
-
nucleotide-disulfide
- pyridine
-
prosthetic
- sativum
- flavin
-
hydroxylapatite
-
enzyme-catalyzed
-
pisum
-
nadh-dependent
- hemoglobins
-
1.8.1.4
-
fad-binding
-
oxido-reductases
-
30-residue
-
sephacryl
The enzyme appears in viruses and cellular organisms
Synonyms
flbr-2, ferric leghemoglobin reductase, flbr2, leghemoglobin reductase, ferric leghemoglobin reductase 2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NAD(P)H + H+ + 2 ferrileghemoglobin = NAD(P)+ + 2 ferroleghemoglobin
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
NAD(P)H:ferrileghemoglobin oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
60440-35-9
-
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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
2 ferricytochrome c + NAD(P)H
2 ferrocytochrome c + NAD(P)+ + H+
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reduced at 53% of leghemoglobin rate
-
?
NADH + H+ + oxidized ferric rice non-symbiotic Hb1
NAD+ + + reduced ferric rice non-symbiotic Hb1
-
-
-
?
NADH + lipoamide
NAD+ + lipoamide
-
recombinant enzyme, lipoamide-dependent NADH oxidation
-
?
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
-
?
2,6-dichloroindophenol + NADH
reduced 2,6-dichloroindophenol + NAD+
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no activity in the absence of
-
?
2,6-dichloroindophenol + NADH
reduced 2,6-dichloroindophenol + NAD+
-
-
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
-
no activity in the absence of O2, formation of H2O2 or peroxide intermediates during NADH oxidation
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
-
31% activity with NADPH
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
-
proposed to be involved in maintaining leghemoglobin in an active form in legume nodules
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
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reduces both cowpea ferrihemoglobin and soybean ferrileghemoglobin
-
?
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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
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
-
-
?
NAD(P)H + ferrileghemoglobin
NAD(P)+ + ferroleghemoglobin
-
proposed to be involved in maintaining leghemoglobin in an active form in legume nodules
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.85
-
oxidation of NADH in the presence of O2, 30fold higher than in the absence of O2
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2
-
decrease of activity from 100% at pH 5.2, to 30% at pH 6.7, no measurements below 5.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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). LEGRE_SOYBN
523
0
55804
Swiss-Prot
Mitochondrion (Reliability: 1)
LEGRE_VIGUN
523
0
55780
Swiss-Prot
Mitochondrion (Reliability: 3)
A0A072V2R0_MEDTR
502
0
53243
TrEMBL
Mitochondrion (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
55000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of cDNA
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moran, J.F.; Sun, Z.; Sarath, G.; Arredondo-Peter, R.; James, E.K.; Becana, M.; Klucas, R.V.
Molecular cloning, functional characterization, and subcellular localization of soybean nodule dihydrolipoamide reductase
Plant Physiol.
128
300-313
2002
Glycine max (O81413), Glycine max
brenda
Saari, L.L.; Klucas, R.V.
Ferric leghemoglobin reductase from soybean root nodules
Arch. Biochem. Biophys.
231
102-113
1984
Glycine max
brenda
Becana, M.; Klucas, R.V.
Enzymatic and nonenzymatic mechanisms for ferric leghemoglobin reduction in legume root nodules
Proc. Natl. Acad. Sci. USA
87
7295-7299
1990
Glycine max, Phaseolus vulgaris, Vigna unguiculata
brenda
Ji, L.; Wood, S.; Becana, M.; Klucas, R.V.
Purification and characterization of soybean root nodule ferric leghemoglobin reductase
Plant Physiol.
96
32-37
1991
Glycine max
brenda
Ji, L.; Becana, M.; Klucas, R.V.
Involvement of molecular oxygen in the enzyme-catalyzed NADH oxidation and ferric leghemoglobin reduction
Plant Physiol.
100
33-39
1992
Glycine max
brenda
Ji, L.; Becana, M.; Sarath, G.; Klucas, R.V.
Cloning and sequence analysis of a cDNA encoding ferric leghemoglobin reductase from soybean nodules
Plant Physiol.
104
453-459
1994
Glycine max
brenda
Ji, L.; Becana, M.; Sarath, G.; Shearman, L.; Klucas, R.V.
Overproduction in Escherichia coli and characterization of a soybean ferric leghemoglobin reductase
Plant Physiol.
106
203-209
1994
Glycine max
brenda
Kim, H.M.
Redox potential of a soybean ferric leghemoglobin reductase
J. Biochem. Mol. Biol.
31
444-452
1998
Glycine max
-
brenda
Luan, P.; Arechaga-Ocampo, E.; Sarath, G.; Arredondo-Peter, R.; Klucas, R.V.
Analysis of a ferric leghemoglobin reductase from cowpea (Vigna unguiculata) root nodules
Plant Sci.
154
161-170
2000
Vigna unguiculata
brenda
Herold, S.; Puppo, A.
Kinetics and mechanistic studies of the reactions of metleghemoglobin, ferrylleghemoglobin, and nitrosylleghemoglobin with reactive nitrogen species
J. Biol. Inorg. Chem.
10
946-957
2005
Glycine max
brenda
Urarte, E.; Auzmendi, I.; Rol, S.; Ariz, I.; Aparicio-Tejo, P.; Arredondo-Peter, R.; Moran, J.F.
A self-induction method to produce high quantities of recombinant functional flavo-leghemoglobin reductase
Methods Enzymol.
436
411-423
2008
Glycine max
brenda
Gopalasubramaniam, S.K.; Kondapalli, K.C.; Millan-Pacheco, C.; Pastor, N.; Stemmler, T.L.; Moran, J.F.; Arredondo-Peter, R.
Soybean dihydrolipoamide dehydrogenase (ferric leghemoglobin reductase 2) interacts with and reduces ferric rice non-symbiotic hemoglobin 1
Sciencejet
2
33
2013
Glycine max
brenda
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