Adrenodoxin reductase

FDXR
Identifiers
AliasesFDXR, ADXR, Adrenodoxin reductase, ferredoxin reductase, ANOA, ADR
External IDsOMIM: 103270; MGI: 104724; HomoloGene: 3033; GeneCards: FDXR; OMA:FDXR - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_007997

RefSeq (protein)

NP_032023

Location (UCSC)Chr 17: 74.86 – 74.87 MbChr 11: 115.16 – 115.17 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Adrenodoxin reductase (Enzyme Nomenclature name: adrenodoxin-NADP+ reductase, EC 1.18.1.6), was first isolated from bovine adrenal cortex where it functions as the first enzyme in the mitochondrial P450 systems that catalyze essential steps in steroid hormone biosynthesis.[5][6] Examination of complete genome sequences revealed that adrenodoxin reductase gene is present in most metazoans and prokaryotes.[7]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000161513Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000018861Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Omura T, Sanders E, Estabrook RW, Cooper DY, Rosenthal O (December 1966). "Isolation from adrenal cortex of a nonheme iron protein and a flavoprotein functional as a reduced triphosphopyridine nucleotide-cytochrome P-450 reductase". Archives of Biochemistry and Biophysics. 117 (3): 660–673. doi:10.1016/0003-9861(66)90108-1.
  6. ^ Hanukoglu I (Dec 1992). "Steroidogenic enzymes: structure, function, and role in regulation of steroid hormone biosynthesis". The Journal of Steroid Biochemistry and Molecular Biology. 43 (8): 779–804. doi:10.1016/0960-0760(92)90307-5. PMID 22217824. S2CID 112729.
  7. ^ Hanukoglu I (2017). "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme". Journal of Molecular Evolution. 85 (5): 205–218. Bibcode:2017JMolE..85..205H. doi:10.1007/s00239-017-9821-9. PMID 29177972. S2CID 7120148.