NADH peroxidase

From Wikipedia, the free encyclopedia

In enzymology, a NADH peroxidase (EC 1.11.1.1) is an enzyme that catalyzes the chemical reaction

NADH + H⁺ + H₂O₂ $\rightleftharpoons$ NAD⁺ + 2 H₂O

The 3 substrates of this enzyme are NADH, H⁺, and H₂O₂, whereas its two products are NAD⁺ and H₂O.

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. It employs one cofactor, FAD.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1F8W, 1JOA, 1NHP, 1NHQ, 1NHR, 1NHS, 1NPX, and 2NPX.

[edit] References

IUBMB entry for 1.11.1.1
BRENDA references for 1.11.1.1 (Recommended.)
PubMed references for 1.11.1.1
PubMed Central references for 1.11.1.1
Google Scholar references for 1.11.1.1
Domagk GF and Horecker BL (1965). "Fructose and erythrose metabolism in Alcaligenes faecalis". Arch. Biochem. Biophys. 109: 342–349. doi:10.1016/0003-9861(65)90371-1.
Mizushima S and Kitahara K (1962). "Purification and properties of DPNH peroxidase in Lactobacillus casei". J. Gen. Appl. Microbiol. 8: 56–62. doi:10.2323/jgam.8.56.
Walker GA, Kilgour GL (1965). "Pyridine nucleotide oxidizing enzymes of Lactobacillus casei. II Oxidase and peroxidase". Arch. Biochem. Biophys. 111: 534–9. doi:10.1016/0003-9861(65)90232-8. PMID 4285876.