Putidaredoxin—NAD+ reductase

Putidaredoxin—NAD reductase (EC 1.18.1.5, putidaredoxin reductase, camA (gene)) is an enzyme with systematic name putidaredoxin:NAD oxidoreductase. This enzyme catalyses the following chemical reaction

reduced putidaredoxin + NAD

\rightleftharpoons

oxidized putidaredoxin + NADH + H

Putidaredoxin—NAD reductase requires FAD.

References

Roome PW, Philley JC, Peterson JA (February 1983). "Purification and properties of putidaredoxin reductase". The Journal of Biological Chemistry. 258 (4): 2593–8. PMID 6401738.
Koga H, Yamaguchi E, Matsunaga K, Aramaki H, Horiuchi T (November 1989). "Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam hydroxylase of Pseudomonas putida". Journal of Biochemistry. 106 (5): 831–6. PMID 2613690.
Peterson JA, Lorence MC, Amarneh B (April 1990). "Putidaredoxin reductase and putidaredoxin. Cloning, sequence determination, and heterologous expression of the proteins". The Journal of Biological Chemistry. 265 (11): 6066–73. PMID 2180940.
Sevrioukova IF, Poulos TL (July 2002). "Putidaredoxin reductase, a new function for an old protein". The Journal of Biological Chemistry. 277 (28): 25831–9. doi:10.1074/jbc.m201110200. PMID 12011076.
Sevrioukova IF, Garcia C, Li H, Bhaskar B, Poulos TL (October 2003). "Crystal structure of putidaredoxin, the component of the P450cam monooxygenase system from Pseudomonas putida". Journal of Molecular Biology. 333 (2): 377–92. doi:10.1016/j.jmb.2003.08.028. PMID 14529624.
Sevrioukova IF, Li H, Poulos TL (February 2004). "Crystal structure of putidaredoxin reductase from Pseudomonas putida, the final structural component of the cytochrome P450cam monooxygenase". Journal of Molecular Biology. 336 (4): 889–902. doi:10.1016/j.jmb.2003.12.067. PMID 15095867.
Smith N, Mayhew M, Holden MJ, Kelly H, Robinson H, Heroux A, Vilker VL, Gallagher DT (May 2004). "Structure of C73G putidaredoxin from Pseudomonas putida" (PDF). Acta Crystallographica Section D. 60 (Pt 5): 816–22. doi:10.1107/s0907444904003348. PMID 15103126.

External links

Putidaredoxin---NAD++reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Other oxidoreductases (EC 1.15–1.21)
1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3
1.16: Oxidizing metal ions	Ceruloplasmin (Methionine synthase) reductase
1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase 7-Hydroxymethyl chlorophyll a reductase
1.18: Acting on iron–sulfur proteins as donors	Nitrogenase
1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)
1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5
1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase Columbamine oxidase Reticuline oxidase Sulochrin oxidase (+)-bisdechlorogeodin-forming (-)-bisdechlorogeodin-forming Aureusidin synthase Tetrahydrocannabinolic acid synthase Cannabidiolic acid synthase Dichlorochromopyrrolate synthase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 1.18.1