Information on EC 1.11.1.1 - NADH peroxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.11.1.1
-
RECOMMENDED NAME
GeneOntology No.
NADH peroxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NADH + H+ + H2O2 = NAD+ + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
non-pathway related
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-
SYSTEMATIC NAME
IUBMB Comments
NADH:hydrogen-peroxide oxidoreductase
A flavoprotein (FAD). Ferricyanide, quinones, etc., can replace H2O2.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-24-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
NADH-peroxidase activity in stationary cells is higher than in exponential cells
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
subsp. cornyformis
-
-
Manually annotated by BRENDA team
subsp. delbrueckii und lactis
-
-
Manually annotated by BRENDA team
subsp. yamanashiensis
-
-
Manually annotated by BRENDA team
effect of growth conditions on enzyme formation
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
subsp. cremoris und mesenteroides
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
role for NADH-PX in the stress response, crucial function of the cell wall-bound NADH-PX in the oxidative burst-mediated cell death and DNA damage in plants under Al3+ stress
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ferricyanide + H2O2
ferrocyanide + H2O
show the reaction diagram
NAD+ + H2O
NADH + H2O2
show the reaction diagram
NADH + H+ + H2O2
NAD+ + 2 H2O
show the reaction diagram
-
-
-
-
?
NADH + H+ + H2O2
NAD+ + H2O
show the reaction diagram
NADH + H2O2
NAD+ + H2O
show the reaction diagram
reduced o-dianisidine + H2O2
oxidised o-dianisidine + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
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+ + H2O
NADH + H2O2
show the reaction diagram
NADH + H+ + H2O2
NAD+ + 2 H2O
show the reaction diagram
-
-
-
-
?
NADH + H+ + H2O2
NAD+ + H2O
show the reaction diagram
NADH + H2O2
NAD+ + H2O
show the reaction diagram
additional information
?
-
-
Npr is absolutely required for aerobic growth on glycerol and optimal growth on the other substrates
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-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
rubredoxin
rubredoxin-like Fe(SCys)4-domain
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe
-
small amounts, significance unknown
additional information
-
no Mo, Cu, Mn, Zn
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
-
98% inhibition at 0.01 mM
Cl-
-
strong inhibitor
Co2+
-
25% inhibition at 1 mM
Cu2+
-
85% inhibition at 1 mM
Ethyl hydroperoxide
-
-
H2O2
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43% inhibition at 16.5 mM
Hg2+
-
21% inhibition at 0.01 mM
N-ethylmaleimide
-
50% inhibition at 1 mM
NAD+
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at pH 5.5 in millimolar range
NADH
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NADH converts the enzyme to an unstable intermediate that decays to inactive enzyme at suboptimal H2O2 concentrations
NaN3
-
15% inhibition at 50 mM
p-chloromercuribenzoate
-
20% inhibition at 0.33 mM
p-hydroxymercuribenzoate
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100% inhibition at 1 mM
Pb2+
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49% inhibition at 0.33 mM
phenylmercuric acetate
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70% loss of activity after 24 h
potassium cyanide
-
-
Salicylhydroxamic acid
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-
SO42-
-
strong inhibitor
Sodium azide
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Benzoic acid
-
enhances NADH-peroxidase activity in the presence of Mn2+
ferulic acid
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enhances NADH-peroxidase activity in the presence of Mn2+
NAD+
-
prevents formation of unstable intermediate of the enzyme and lowers Km for H2O2
p-coumaric acid
vanillic acid
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enhances NADH-peroxidase activity in the presence of Mn2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
ferricyanide
-
-
0.00069 - 0.08
H2O2
0.001 - 0.0068
NADH
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
66.7
H2O2
Enterococcus faecalis
-
calculated per flavin
0.000167 - 83.3
NADH
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
NAD+
-
at pH 5.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000064
-
with FAD
0.00001
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with FAD
0.000012
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with FAD
0.00002
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with FAD
0.000021
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with FAD
0.000022
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with FAD
0.000024
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with FAD
0.000028
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with FAD
0.0000296
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with FAD
0.000032
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with FAD
0.000044
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with FAD
0.000049
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with FAD
0.000081
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subspecies cremoris with FAD
0.000082
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subspecies lactis with FAD
0.000083
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subspecies mesenteroides with FAD
0.00011
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subspecies delbrueckii with FAD
0.017
Clostridium acetobutylicum wild-type cell lysate
0.024
Clostridium acetobutylicum pTrbr3B cell lysate
0.66
NADH:rubredoxin oxidoreductase, revRbr
0.993
NADH:rubredoxin oxidoreductase, rubredoxin, revRbr
additional information
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8500-9000 U/ml, calculated as change of 0.01 of optical density
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
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ferricyanide
5.2 - 5.4
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substrate H2O2 in acetate or phosphate buffer
6
-
activity assay
6.4 - 7.4
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
-
90% of maximal activity at pH 5.0, 32% of maximal activity at pH 8.5
5.5 - 6.5
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four peroxidase isoenzymes
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
activity assay at room temperature
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
40% of enzyme activity in cytoplam and membrane fraction
Manually annotated by BRENDA team
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60% of enzyme activity
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
determined by SDS-PAGE
47000
-
SDS-PAGE
49000
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4 * 49000, SDS-PAGE
49700
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2 * 49700, Superdex 200 gel filtration
49730
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MALDI-TOF
60000
-
2 * 60000, calculation from FAD content
80000
determined by gel filtration
100000
-
Superdex 200 gel filtration
120000
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calculation from FAD content
201300
-
gel filtration
201400
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 49700, Superdex 200 gel filtration
homotetramer
4 * 21000
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.8
-
complete loss of activity after 2 h
395332
3
-
19% of enzyme activity after 2 h
395332
3.25
-
86% of enzyme activity after 2 h
395332
3.5
-
no loss of enzyme activity after 2 h
395332
5.4
-
45 min stable
395334
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28 - 47
-
fully active after 5 h
60
-
5 min, 20% loss of activity
70
-
complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
25°C, without H2O2 in assay system 85% loss of activity in 30 min
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low concentrations of urea stabilize an intermediate state in the transition between native and denatured form
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The presence of the peptergents V6K, A6D, and a 40:60 mixture of A6D:A6K all extends the enzymatic half-life to over 3-5 times longer than in its absence.
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Npx is labile, rapidly losing activity under aerobic conditions via spontaneous oxidation of its secondary redox center. The enzyme is oxidized over a period of several weeks at 4 °C or –20°C.
-
672012
Npx is labile, rapidly losing activity under aerobic conditions via spontaneous oxidation of its secondary redox center. The enzyme is oxidized over a period of several weeks at 4°C or –20°C.
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672012
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM phosphate buffer pH 7.0
-
5°C, pH 7.0, 1 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial, peroxidase activity cannot be separated from oxidase acitivity
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separation of proteins on a 1D blue-native gel followed by electroelution, four isoenzymes elutes from the blue-native gels
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the crude extract is loaded onto columns containing a Strep-Tactin-Sepharose matrix
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the rbr3B gene is cloned into a pThydA vector for expression of the protein in Escherichia coli DH5alpha cells and in Clostridium acetobutylicum ATCC 824
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
aluminium induces the cell wall-bound NADH-PX, which contributes to the oxidative burst through the generation of Rreactive oxygen species that lead to cell death and DNA damage in the root cells
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revRbr is massively up-regulated in response to oxidative stress
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H10Q
lower Km for H2O2
R303M
significant conformational change, lower Km and kcat
C42A
-
mutation leads to an almost inactive enzyme
-
C42S
-
mutation leads to an almost inactive enzyme
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