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1.11.1.1: NADH peroxidase

This is an abbreviated version!
For detailed information about NADH peroxidase, go to the full flat file.

Word Map on EC 1.11.1.1

Reaction

NADH
+
H+
 +
H2O2
=
NAD+
 + 2 H2O

Synonyms

apoplastic class III peroxidase, apoplastic peroxidase, diphosphopyridine nucleotide peroxidase, DPN peroxidase, DPNH peroxidase, NAD peroxidase, NADH oxidase, NADH peroxidase, NADH-peroxidase, NADH-POD, NADH-PX, NADH2 peroxidase, NADH:H2O2 oxidoreductase, NADH:O2 oxidoreductase, nicotinamide adenine dinucleotide peroxidase, nigerythrin, non-haem diiron protein, NPR, Npx, NPXase, P2, peroxidase, nicotinamide adenine dinucleotide, POD, reverse rubrerythrin, revRbr, ruberythrin

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.1 NADH peroxidase

Reference

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Reference on EC 1.11.1.1 - NADH peroxidase

Please use the Reference Search for a specific query.
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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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Hansson, L.; Häggström, M.H.
Effects of growth conditions on the activities of superoxide dismutase and NADH-oxidase/NADH-peroxidase in Streptococcus lactis
Curr. Microbiol.
10
345-352
1984
Lactococcus lactis
-
Manually annotated by BRENDA team
Dolin, M.I.
DPNH peroxidase: effector activities of DPN
Biochem. Biophys. Res. Commun.
78
393-400
1977
Enterococcus faecalis
Manually annotated by BRENDA team
Walker, G.A.; Kilgour, G.L.
Pyridine nucleotide oxidizing enzymes of Lactobacillus casei. II. Oxidase and peroxidase
Arch. Biochem. Biophys.
111
534-539
1965
Lacticaseibacillus casei
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Thomas, E.L.; Pera, K.A.
Oxygen metabolism of Streptococcus mutans: uptake of oxygen and release of superoxide and hydrogen peroxide
J. Bacteriol.
154
1236-1244
1983
Streptococcus mutans
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
Coulter, E.D.; Shenvi, N.V.; Kurtz, D.M., Jr.
NADH peroxidase activity of rubrerythrin
Biochem. Biophys. Res. Commun.
255
317-323
1999
Clostridium perfringens, Desulfovibrio vulgaris
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Sakamoto, M.; Komagata, K.
Aerobic growth of and activities of NADH oxidase and NADH peroxidase in lactic acid bacteria
J. Ferment. Bioeng.
82
210-216
1996
Leuconostoc mesenteroides, Enterococcus faecium, Lactiplantibacillus plantarum, Levilactobacillus brevis, Lentilactobacillus buchneri, Lacticaseibacillus casei, Loigolactobacillus coryniformis, Lactobacillus delbrueckii, Liquorilactobacillus mali, Lacticaseibacillus rhamnosus, Leuconostoc lactis, Pediococcus acidilactici, Pediococcus pentosaceus, Streptococcus thermophilus
-
Manually annotated by BRENDA team
Yeh, J.I.; Claiborne, A.
Crystal structures of oxidized and reduced forms of NADH peroxidase
Methods Enzymol.
353
44-54
2002
Enterococcus faecalis
Manually annotated by BRENDA team
Davydova, M.N.; Sabirova, R.Z.
Antioxidative enzymes of sulfate-reducing bacterium Desulfovibrio desulfuricans: superoxide dismutase and peroxidases
Biochemistry (Moscow)
67
822-825
2002
Desulfovibrio desulfuricans
Manually annotated by BRENDA team
Simonovicova, M.; Tamas, L.; Huttova, J.; Mistrik, I.
Effect of aluminum on oxidative stress related enzymes activities in barley roots
Biol. Plant.
48
261-266
2004
Hordeum vulgare
-
Manually annotated by BRENDA team
Lin, C.C.; Kao, C.H.
Osmotic stress-induced changes in cell wall peroxidase activity and hydrogen peroxide level in roots of rice seedlings
Plant Growth Regul.
37
177-184
2002
Oryza sativa
-
Manually annotated by BRENDA team
Yeh, J.I.; Du, S.; Tortajada, A.; Paulo, J.; Zhang, S.
Peptergents: peptide detergents that improve stability and functionality of a membrane protein, glycerol-3-phosphate dehydrogenase
Biochemistry
44
16912-16919
2005
Enterococcus casseliflavus
Manually annotated by BRENDA team
Fernandez, R.F.; Kunz, D.A.
Bacterial cyanide oxygenase is a suite of enzymes catalyzing the scavenging and adventitious utilization of cyanide as a nitrogenous growth substrate
J. Bacteriol.
187
6396-6402
2005
Pseudomonas fluorescens
Manually annotated by BRENDA team
Fecht-Christoffers, M.M.; Fuehrs, H.; Braun, H.P.; Horst, W.J.
The role of hydrogen peroxide-producing and hydrogen peroxide-consuming peroxidases in the leaf apoplast of cowpea in manganese tolerance
Plant Physiol.
140
1451-1463
2006
Vigna unguiculata
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Fuehrs, H.; Goetze, S.; Specht, A.; Erban, A.; Gallien, S.; Heintz, D.; Van Dorsselaer, A.; Kopka, J.; Braun, H.P.; Horst, W.J.
Characterization of leaf apoplastic peroxidases and metabolites in Vigna unguiculata in response to toxic manganese supply and silicon
J. Exp. Bot.
60
1663-1678
2009
Vigna unguiculata
Manually annotated by BRENDA team
Riebe, O.; Fischer, R.J.; Wampler, D.A.; Kurtz, D.M.; Bahl, H.
Pathway for H2O2 and O2 detoxification in Clostridium acetobutylicum
Microbiology
155
16-24
2009
Clostridium acetobutylicum (Q97D83), Clostridium acetobutylicum
Manually annotated by BRENDA team
Achary, V.M.; Parinandi, N.L.; Panda, B.B.
Aluminum induces oxidative burst, cell wall NADH peroxidase activity, and DNA damage in root cells of Allium cepa L.
Environ. Mol. Mutagen.
53
550-560
2012
Allium cepa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Wang, S.; Cazelles, R.; Liao, W.C.; Vazquez-Gonzalez, M.; Zoabi, A.; Abu-Reziq, R.; Willner, I.
Mimicking horseradish peroxidase and NADH peroxidase by heterogeneous Cu(2+)-modified graphene oxide nanoparticles
Nano Lett.
17
2043-2048
2017
synthetic construct
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Naraki, S.; Igimi, S.; Sasaki, Y.
NADH peroxidase plays a crucial role in consuming H2O2 in Lactobacillus casei IGM394
Biosci. Microbiota Food Health
39
45-56
2020
Lacticaseibacillus casei, Lacticaseibacillus casei IGM394
Manually annotated by BRENDA team
Korir, M.L.; Flaherty, R.A.; Rogers, L.M.; Gaddy, J.A.; Aronoff, D.M.; Manning, S.D.
Investigation of the role that NADH peroxidase plays in oxidative stress survival in group B Streptococcus
Front. Microbiol.
9
2786
2018
Enterococcus faecalis
Manually annotated by BRENDA team