Adrenodoxin-NADP+ reductase

Adrenodoxin-NADP reductase (EC 1.18.1.6, adrenodoxin reductase, nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase, ADR, NADPH:adrenal ferredoxin oxidoreductase) is an enzyme with systematic name adrendoxin:NADP oxidoreductase. This enzyme catalyses the following chemical reaction

2 reduced adrenodoxin + NADP

\rightleftharpoons

2 oxidized adrenodoxin + NADPH + H

Adrenodoxin-NADP+ reductase is a flavoprotein (FAD).

References

Omura T, Sanders E, Estabrook RW, Cooper DY, Rosenthal O (1966). "Isolation from adrenal cortex of a nonheme iron protein and a flavoprotein functional as a reduced triphosphopyridine nucleotide-cytochrome P-450 reductase". Arch. Biochem. Biophys. 117 (3): 660–673. doi:10.1016/0003-9861(66)90108-1.
Chu JW, Kimura T (March 1973). "Studies on adrenal steroid hydroxylases. Molecular and catalytic properties of adrenodoxin reductase (a flavoprotein)". The Journal of Biological Chemistry. 248 (6): 2089–94. PMID 4144106.
Sugiyama T, Yamano T (March 1975). "Purification and crystallization of NADPH-adrenodoxin reductase from bovine adrenocortical mitochondria". FEBS Letters. 52 (1): 145–8. doi:10.1016/0014-5793(75)80658-2. PMID 235468.
Hanukoglu I, Jefcoate CR (April 1980). "Mitochondrial cytochrome P-450scc. Mechanism of electron transport by adrenodoxin". The Journal of Biological Chemistry. 255 (7): 3057–61. PMID 6766943.
Hanukoglu I, Hanukoglu Z (May 1986). "Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase in adrenal cortex and corpus luteum. Implications for membrane organization and gene regulation". European Journal of Biochemistry. 157 (1): 27–31. doi:10.1111/j.1432-1033.1986.tb09633.x. PMID 3011431.
Hanukoglu I, Gutfinger T (March 1989). "cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases". European Journal of Biochemistry. 180 (2): 479–84. doi:10.1111/j.1432-1033.1989.tb14671.x. PMID 2924777.
Ziegler GA, Vonrhein C, Hanukoglu I, Schulz GE (June 1999). "The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis". Journal of Molecular Biology. 289 (4): 981–90. doi:10.1006/jmbi.1999.2807. PMID 10369776.

External links

Adrenodoxin-NADP++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