Information on EC 1.6.2.6 - leghemoglobin reductase

Word Map on EC 1.6.2.6
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:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)
Please login to have access to the AMENDA and FRENDA data

The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
1.6.2.6
-
top print hide
RECOMMENDED NAME
GeneOntology No.
leghemoglobin reductase
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NAD(P)H + H+ + 2 ferrileghemoglobin = NAD(P)+ + 2 ferroleghemoglobin
show the reaction diagram
-
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
NAD(P)H:ferrileghemoglobin oxidoreductase
-
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
60440-35-9
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bean
-
-
Manually annotated by BRENDA team
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
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 + lipoamide
NAD+ + ?
show the reaction diagram
-
-
-
?
NADH + lipoamide
NAD+ + lipoamide
show the reaction diagram
-
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
-
-
-
top print hide
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
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
-
-
-
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
-
CdSO4
-
-
Cu(NO3)2
-
-
iodoacetamide
nicotinate
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
0.5 mM, slight inhibition
Phenylarsine oxide
-
-
Quinacrine
-
0.5 mM, 30-40% inhibition
top print hide
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
top print hide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6 - 6.2
ferrileghemoglobin
31 - 392
Lipoamide
137
NADH
Glycine max
O81413
recombinant FLbR-2
top print hide
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
-
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
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
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
top print hide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 8.5
-
no activity below and above
top print hide
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
isoelectric focusing, pH-range 4.0-6.5
top print hide
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
high mRNA level
Manually annotated by BRENDA team
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
top print hide
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
-
equilibrium ultracentrifugation
100000
-
gel filtration
110000
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
heat labile
top print hide
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C
-
0°C, 37 days, 96% activity retains
-
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, hydroxylapatite, ion exchange, gel filtration
-
recombinant enzyme, Sepharose 6B, Probond
-
recombinant FLbR2
-
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of cDNA
expression in Escherichia coli
-
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
-
top
top
top
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
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)