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Adrenal ferredoxin

From Wikipedia, the free encyclopedia

FDX1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesFDX1, ADX, FDX, LOH11CR1D, ferredoxin 1
External IDsOMIM: 103260; MGI: 103224; HomoloGene: 31216; GeneCards: FDX1; OMA:FDX1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004109

NM_001301728
NM_007996

RefSeq (protein)

NP_004100

NP_001288657
NP_032022

Location (UCSC)Chr 11: 110.43 – 110.46 MbChr 9: 51.85 – 51.87 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Adrenal ferredoxin (also adrenodoxin (ADX), adrenodoxin, mitochondrial, hepatoredoxin, ferredoxin-1 (FDX1)) is a protein that in humans is encoded by the FDX1 gene.[5][6] In addition to the expressed gene at this chromosomal locus (11q22), there are pseudogenes located on chromosomes 20 and 21.

Function

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Adrenodoxin is a small iron-sulfur protein that can accept and carry a single electron. Adrenodoxin functions as an electron transfer protein in the mitochondrial cytochrome P450 systems.[7] The first enzyme in this system is adrenodoxin reductase that carries an FAD. FAD can be reduced by two electrons donated from coenzyme NADPH.[8] These two electrons are transferred one a time to adrenodoxin. Adrenodoxin in return reduces mitochondrial cytochrome P450.[7] This particular oxidation/reduction system is involved in the synthesis of steroid hormones in steroidogenic tissues. In addition, similar systems also function in vitamin D and bile acid synthesis in the kidney and liver respectively. Adrenodoxin has been identified in a number of different tissues but all forms have been shown to be identical and are not tissue specific.[6]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000137714Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032051Ensembl, 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. ^ Mittal S, Zhu YZ, Vickery LE (Sep 1988). "Molecular cloning and sequence analysis of human placental ferredoxin". Arch Biochem Biophys. 264 (2): 383–91. doi:10.1016/0003-9861(88)90303-7. PMID 2969697.
  6. ^ a b "Entrez Gene: FDX1 ferredoxin 1".
  7. ^ a b Hanukoglu I, Jefcoate CR (Apr 1980). "Mitochondrial cytochrome P-450scc. Mechanism of electron transport by adrenodoxin" (PDF). The Journal of Biological Chemistry. 255 (7): 3057–61. doi:10.1016/S0021-9258(19)85851-9. PMID 6766943.
  8. ^ 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.

Further reading

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