The structure of NADH peroxidase from Enterococcus faecalis. Adapted from PDB: 2NPX.
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EC no.
1.11.1.1
CAS no.
9032-24-0
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In enzymology, a NADH peroxidase (EC 1.11.1.1) is an enzyme that catalyzes the chemical reaction
NADH + H+ + H2O2 NAD+ + 2 H2O
The presumed function of NADH peroxidase is to inactivate H2O2 generated within the cell, for example by glycerol-3-phosphate oxidase during glycerol metabolism or dismutation of superoxide, before the H2O2 causes damage to essential cellular components.[1]
The 3 substrates of this enzyme are NADH, H+, and H2O2, whereas its two products are NAD+ and H2O. It employs one cofactor, FAD, however no discrete FADH2 intermediate has been observed.[2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptor (peroxidases). The systematic name of this enzyme class is NADH:hydrogen-peroxide oxidoreductase. Other names in common use include DPNH peroxidase, NAD peroxidase, diphosphopyridine nucleotide peroxidase, NADH-peroxidase, nicotinamide adenine dinucleotide peroxidase, and NADH2 peroxidase.
^La Carbona S, Sauvageot N, Giard JC, Benachour A, Posteraro B, Auffray Y, Sanguinetti M, Hartke A (December 2007). "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 (5): 1148–63. doi:10.1111/j.1365-2958.2007.05987.x. PMID 17971082. S2CID 40046805.
^Miller H, Poole LB, Claiborne A (June 1990). "Heterogeneity among the flavin-containing NADH peroxidases of group D streptococci. Analysis of the enzyme from Streptococcus faecalis ATCC 9790". J. Biol. Chem. 265 (17): 9857–63. PMID 2161844.
In enzymology, a NADHperoxidase (EC 1.11.1.1) is an enzyme that catalyzes the chemical reaction NADH + H+ + H2O2 ⇌ {\displaystyle \rightleftharpoons }...
(non-catalase) peroxidase but do not have catalase. More specifically, they may use a NADH oxidase/NADHperoxidase (NOX/NPR) system or a glutathione peroxidase system...
it is activated by a peroxidase enzyme, which oxidizes the compound into a free radical form. This radical then reacts with NADH, to produce adducts that...
medium. In the absence of heme and menaquinone, oxygen is consumed by NADH-peroxidase with hydrogen peroxide as intermediate and water as end product. The...
names in common use include peroxidase-M2, and Mn-dependent (NADH-oxidizing) peroxidase. It employs one cofactor, heme. This enzyme needs Ca2+ for activity...
between nicotinamide adenine dinucleotide (NAD) and its reduced form (NADH). Pyruvate + NADH --(enzyme lactate dehydrogenase)--> L-lactate + NAD Blood sugar...
Ascorbate peroxidase (or L-ascorbate peroxidase, APX or APEX) (EC 1.11.1.11) is an enzyme that catalyzes the chemical reaction L-ascorbate + H2O2 ⇌ {\displaystyle...
citric acid cycle, producing carbon dioxide and the energetic electron donors NADH and FADH. Oxidative phosphorylation uses these molecules and O2 to produce...
this reaction from glycolysis: Pi + glyceraldehyde-3-phosphate + NAD+ → NADH + H+ + 1,3-bisphosphoglycerate In this reaction, NAD+ is the oxidant (electron...
Deiodinase (monodeiodinase) is a peroxidase enzyme that is involved in the activation or deactivation of thyroid hormones. Types of deiodinases include:...
NADH + H+ NAD+ is mostly used in catabolic pathways, such as glycolysis, that break down energy molecules to produce ATP. The ratio of NAD+ to NADH is...
resorufin (used in many assays combining for example horseradish peroxidase (HRP), or NADH, NADPH using enzymes). 7-ethoxyresorufin, a compound used as the...
catalase-peroxidase enzyme in Mycobacterium tuberculosis. KatG catalyzes the formation of the isonicotinic acyl radical, which spontaneously couples with NADH...
their intrinsic peroxidase mimicry. A scaffolded "INAzyme" ("integrated nanozyme") arrangement was described, locating hemin (a peroxidase mimic) with glucose...
are the most common types. Enzymes used in ELISAs include horseradish peroxidase (HRP), alkaline phosphatase (AP) or glucose oxidase. These enzymes allow...
common coenzymes NADH and NADPH absorb UV light in their reduced forms, but do not in their oxidized forms. An oxidoreductase using NADH as a substrate...
be used as a readout for successful pathogen recognition via a luminol-peroxidase based assay. Herb M, Schramm M (February 2021). "Functions of ROS in Macrophages...
adenine dinucleotide (NAD+) to its reduced form NADH in a redox reaction. By causing an imbalance of the NAD+/NADH redox system, alcoholic beverages make normal...
using NADH and FADH most commonly – though C. jejuni uses NADH poorly compared to FADH due to a replacement of genes encoding subunits for NADH dehydrogenases...
adenine dinucleotide exists in two related forms in the cell, NADH and NADPH. The NAD+/NADH form is more important in catabolic reactions, while NADP+/NADPH...
scavenging (by enzymes like superoxide dismutase, catalase, glutathione peroxidase and others). However, some mutations that increase ROS production (e.g...
Youichi; Nishiyama, Yoshitaka; Miki, Kunio (1 August 1999). "Stimulation of Peroxidase Activity by Decamerization Related to Ionic Strength: AhpC Protein from...
does not require selenocysteine or cysteine for catalysis, is part of the NADH oxidase/flavin reductase superfamily, and removes iodide when the substrate...
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