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Information on EC 1.11.1.1 - NADH peroxidase and Organism(s) Enterococcus faecalis and UniProt Accession P37062
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1.11.1.1 NADH peroxidaseIUBMB Comments
A flavoprotein (FAD). Ferricyanide, quinones, etc., can replace H2O2.
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Word Map
- 1.11.1.1
- succinate
- naproxen
- dismutase
- flavoproteins
- catalase
- streptococcus
- fad
- flavin
-
submitochondrial
- oxidases
- rotenone
- ubiquinone
- peroxidases
-
nadh-dependent
- faecalis
- ferricyanide
- ibuprofen
- capsaicin
- antimycin
-
uninephrectomized
-
rotenone-sensitive
-
nephrectomy
- diclofenac
-
nephrectomized
-
flavoenzyme
- aif
-
nadh-ubiquinone
-
two-electron
- acetoin
-
succinate-supported
-
nadh-oxidase
- rubrerythrins
- guaiacol
-
1.6.99.3
-
drug-responsive
- dnazyme
- 2,3-butanediol
- hyodysenteriae
- diacetyl
-
nadh-ferricyanide
- brachyspira
-
aptasensors
-
sulfenic
- synthesis
The taxonomic range for the selected organisms is: Enterococcus faecalis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
nadh oxidase, npx, nadh peroxidase, apoplastic peroxidase, nadh-peroxidase, nigerythrin, npxase, revrbr, nadh-px, nadh:o2 oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
diphosphopyridine nucleotide peroxidase
-
-
-
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DPN peroxidase
-
-
-
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DPNH peroxidase
-
-
-
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NAD peroxidase
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-
-
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NADH-peroxidase
-
-
-
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NADH2 peroxidase
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-
-
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nicotinamide adenine dinucleotide peroxidase
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-
-
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Npx
NPXase
-
-
-
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peroxidase, nicotinamide adenine dinucleotide
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-
-
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Npx
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
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reduction
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
NADH:hydrogen-peroxide oxidoreductase
A flavoprotein (FAD). Ferricyanide, quinones, etc., can replace H2O2.
CAS REGISTRY NUMBER
COMMENTARY
9032-24-0
-
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
NADH + H2O2
NAD+ + H2O
-
H2O2 can be replaced by 1,4-naphthoquinone which is one third as effective as H2O2
-
?
NADH + H2O2
NAD+ + H2O
-
elimination of toxic H2O2, regeneration of oxidized pyridine nucleotide which is essential to the strictly fermentative metabolism
-
-
?
additional information
?
-
-
NADH cannot be replaced by reduced cytochrome c, H2O2 cannot be replaced by Cu2+, Fe3+, SeO32+, NO3-, NO2-, oxidized glutathione, cystine, lipoic acid disulfide, dehydroascorbic acid, cytochrome c, FAD, flavin mononucleotide, riboflavin, 2,6-dichlorophenolindophenol, methylene blue, brilliant cresyl blue
-
-
?
additional information
?
-
-
Npr is absolutely required for aerobic growth on glycerol and optimal growth on the other substrates
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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
?
-
-
Npr is absolutely required for aerobic growth on glycerol and optimal growth on the other substrates
-
-
?
NADH + H2O2
NAD+ + H2O
-
elimination of toxic H2O2, regeneration of oxidized pyridine nucleotide which is essential to the strictly fermentative metabolism
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
enzyme contains flavin and non-flavin redox centers
FAD
-
2 mol flavin and 1 mol of a non-flavin electron acceptor at the active site
FAD
-
flavoprotein. The resonance Raman (RR) modes of the oxidized and twoelectron reduced (EH2) forms of Npx are related to very tight flavin-protein interactions maintaining a nearly planar conformation of the isoalloxazine tricycle, a low level of H-bonding at the N1/N5 and O2/O4 sites, and a strong H-bond at N3H. Minimal changes in FAD structure and environment upon either NAD(H) binding or reduction of the sulfinic redox center
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
NADH converts the enzyme to an unstable intermediate that decays to inactive enzyme at suboptimal H2O2 concentrations
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
prevents formation of unstable intermediate of the enzyme and lowers Km for H2O2
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km values over a pH range from pH 5.5 to pH 8.5
-
additional information
additional information
-
Km values at different pH
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pH dependence of kcat from pH 5 to pH 9
-
additional information
additional information
-
kcat at different pH values
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
8500-9000 U/ml, calculated as change of 0.01 of optical density
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8.5
-
90% of maximal activity at pH 5.0, 32% of maximal activity at pH 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
an Enterococcus faecalis npr mutant has similar growth to the wild-type under normal growth conditions, but is more susceptible to killing by H2O2 as well as macrophages
physiological function
-
Npx is a key factor that allows Group B Streptococcus to survive oxidative and phagosomal stress, and contributes to the inhibition of the ROS burst in human macrophages
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
-
wild type, C42A and C42S mutants are tetramers, concluded from crystal structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the resonance Raman modes of the oxidized and two-electron reduced forms of Npx are related to very tight flavin-protein interactions maintaining a nearly planar conformation of the isoalloxazine tricycle, a low level of H-bonding at the N1/N5 and O2/O4 sites, and a strong H-bond at N3H. They indicate minimal changes in FAD structure and environment upon either NAD(H) binding or reduction of the sulfinic redox center
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C42A
C42S
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
low concentrations of urea stabilize an intermediate state in the transition between native and denatured form
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cox, C.; Camus, P.; Buret, J.; Duvivier, J.
An enzymatic cycling procedure for NAD+ using an irreversible reaction with NAD+-peroxidase
Anal. Biochem.
119
185-193
1982
Enterococcus faecalis
Dolin, M.I.
Reduced diphosphopyridine nucleotide peroxidase. Intermediates formed on reduction of the enzyme with dithionite or reduced diphosphopyridine nucleotide
J. Biol. Chem.
250
310-317
1975
Enterococcus faecalis, Enterococcus faecalis 10C1
Dolin, M.I.
The Streptococcus faecalis oxidase for reduced diphosphopyridine nucleotide. III. Isolation and properties of a flavin peroxidase for reduced diphosphopyridine nucleotide
J. Biol. Chem.
225
557-573
1957
Enterococcus faecalis
Dolin, M.I.
DPNH peroxidase: effector activities of DPN
Biochem. Biophys. Res. Commun.
78
393-400
1977
Enterococcus faecalis
Yeh, J.I.; Claiborne, A.; Hol, W.G.J.
Structure of the native cysteinesulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8.ANG. resolution
Biochemistry
35
9951-9957
1996
Enterococcus faecalis (P37062)
Miller, H.; Poole, L.B.; Claiborne, A.
Heterogeneity among the flavin-containing NADH peroxidases of group D streptococci. Analysis of the enzyme from Streptococcus faecalis ATCC 9790
J. Biol. Chem.
265
9857-9863
1990
Enterococcus faecalis
Schiering, N.; Stoll, V.S.; Blanchart, J.S.; Pai, E.F.
Crystallization and preliminary x-ray diffraction study of the flavoprotein NADH peroxidase from Streptococcus faecalis 10C1
J. Biol. Chem.
264
21144-21145
1989
Enterococcus faecalis, Enterococcus faecalis 10C1
Claiborne, A.; Ahmed, S.A.; Ross, P.; Miller, H.
The Streptococcal NADH peroxidase and NADH oxidase: structural and mechanistic aspects
Flavins and Flavoproteins (Proc. Int. Symp. , 10th, Meeting Date 1990, Curti, B. , Ronchi S. , Zanetti, G. , eds. ) de Gruyter, Berlin, New York
667-670
1991
Enterococcus faecalis
-
Stehle, T.; Ahmed, S.A.; Claiborne, A.; Schulz, G.E.
Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 A resolution
J. Mol. Biol.
221
1325-1344
1991
Enterococcus faecalis
Stehle, T.; Schulz, G.E.; Ahmed, S.A.; Claiborne, A.
The structure of NADH peroxidase from Streptococcus faecalis
Flavins and Flavoproteins (Proc. Int. Symp. , 10th, Meeting Date 1990, Curti, B. , Ronchi S. , Zanetti, G. , eds. ) de Gruyter, Berlin, New York
651-654
1991
Enterococcus faecalis
-
Poole, L.B.; Claiborne, A.
The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid
J. Biol. Chem.
264
12330-12338
1989
Enterococcus faecalis
Ahmed, A.S.; Ross, P.; Miller, H.; Claiborne, A.
Sequence fingerprints for the disulfide reductases: application to the streptococcal NADH peroxidase
Flavins and Flavoproteins (Proc. Int. Symp. , 10th, Meeting Date 1990, Curti, B. , Ronchi S. , Zanetti, G. , eds. ) de Gruyter, Berlin, New York
647-650
1991
Enterococcus faecalis
-
Crane, E.J.; Parsonage, D.; Poole, L.B.; Claiborne, A.
Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme forms
Biochemistry
34
14114-14124
1995
Enterococcus faecalis
Crane, E.J.; Yeh, J.I.; Luba, J.; Claiborne, A.
Analysis of the kinetic and redox properties of the NADH peroxidase R303M mutant: correlation with the crystal structure
Biochemistry
39
10353-10364
2000
Enterococcus faecalis (P37062)
Mande, S.S.; Parsonage, D.; Claiborne, A.; Hol, W.G.J.
Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg303
Biochemistry
34
6985-6992
1995
Enterococcus faecalis
Parsonage, D.; Claiborne, A.
Analysis of the kinetic and redox properties of NADH peroxidase C42S and C42A mutants lacking the cysteine-sulfenic acid redox center
Biochemistry
34
435-441
1995
Enterococcus faecalis, Enterococcus faecalis 10C1
Parsonage, D.; Miller, H.; Ross, R.P.; Claiborne, A.
Purification and analysis of streptococcal NADH peroxidase expressed in Escherichia coli
J. Biol. Chem.
268
3161-3167
1993
Enterococcus faecalis, Enterococcus faecalis 10C1
Yeh, J.I.; Claiborne, A.
Crystal structures of oxidized and reduced forms of NADH peroxidase
Methods Enzymol.
353
44-54
2002
Enterococcus faecalis
La Carbona, S.; Sauvageot, N.; Giard, J.C.; Benachour, A.; Posteraro, B.; Auffray, Y.; Sanguinetti, M.; Hartke, A.
Comparative study of the physiological roles of three peroxidases (NADH peroxidase, alkyl hydroperoxide reductase and thiol peroxidase) in oxidative stress response, survival inside macrophages and virulence of Enterococcus faecalis
Mol. Microbiol.
66
1148-1163
2007
Enterococcus faecalis
Keirsse-Haquin, J.; Picaud, T.; Bordes, L.; de Gracia, A.G.; Desbois, A.
Modulation of the flavin-protein interactions in NADH peroxidase and mercuric ion reductase a resonance Raman study
Eur. Biophys. J.
47
205-223
2017
Enterococcus faecalis
Keirsse-Haquin, J.; Picaud, T.; Bordes, L.; de Gracia, A.G.; Desbois, A.
Modulation of the flavin-protein interactions in NADH peroxidase and mercuric ion reductase a resonance Raman study
Eur. Biophys. J.
47
205-223
2018
Enterococcus faecalis
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