Any feedback?
Please rate this page
(sequences.php)
(0/150)

BRENDA support

Sequence of ADX_HUMAN

EC Number:1.14.15.5

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
corticosterone 18-monooxygenase
P10109
Homo sapiens
184
19393
Reaction
corticosterone + 2 reduced adrenodoxin + O2 + 2 H+ = 18-hydroxycorticosterone + 2 oxidized adrenodoxin + H2O
Other sequences found for EC No. 1.14.15.5

General information:

Sequence
show sequence in fasta format
  0 MAAAGGARLL RAASAVLGGP AGRWLHHAGS RAGSSGLLRN RGPGGSAEAS RSLSVSARAR
 60 SSSEDKITVH FINRDGETLT TKGKVGDSLL DVVVENNLDI DGFGACEGTL ACSTCHLIFE
120 DHIYEKLDAI TDEENDMLDL AYGLTDRSRL GCQICLTKSM DNMTVRVPET VADARQSIDV
180 GKTS
Download this sequence
in fasta format
Download all sequences for 1.14.15.5
in fasta format
in csv (Excel, OpenOffice) format
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
640135
Chang C.-Y.,Wu D.-A.,Lai C.-C.,Miller W.L.,Chung B.-C.
Cloning and structure of the human adrenodoxin gene.
DNA
7
609-615
1988
640136
Picado-Leonard J.,Voutilainen R.,Kao L.-C.,Chung B.-C.,Strauss J.F. III,Miller W.L.
Human adrenodoxin: cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells.
J. Biol. Chem.
263
3240-3244
1988
640137
Mittal S.,Zhu Y.-Z.,Vickery L.E.
Molecular cloning and sequence analysis of human placental ferredoxin.
Arch. Biochem. Biophys.
264
383-391
1988
640138
Chang C.-Y.,Wu D.-A.,Mohandas T.K.,Chung B.-C.
Structure, sequence, chromosomal location, and evolution of the human ferredoxin gene family.
DNA Cell Biol.
9
205-212
1990
640141
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
640142
Johnson D.,Norman S.,Tuckey R.C.,Martin L.L.
Electrochemical behaviour of human adrenodoxin on a pyrolytic graphite electrode.
Bioelectrochemistry
59
41-47
2003
640143
Dephoure N.,Zhou C.,Villen J.,Beausoleil S.A.,Bakalarski C.E.,Elledge S.J.,Gygi S.P.
A quantitative atlas of mitotic phosphorylation.
Proc. Natl. Acad. Sci. U.S.A.
105
10762-10767
2008
640144
Sheftel A.D.,Stehling O.,Pierik A.J.,Elsasser H.P.,Muhlenhoff U.,Webert H.,Hobler A.,Hannemann F.,Bernhardt R.,Lill R.
Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis.
Proc. Natl. Acad. Sci. U.S.A.
107
11775-11780
2010
640145
Burkard T.R.,Planyavsky M.,Kaupe I.,Breitwieser F.P.,Buerckstuemmer T.,Bennett K.L.,Superti-Furga G.,Colinge J.
Initial characterization of the human central proteome.
BMC Syst. Biol.
5
17-17
2011
640146
Zhou H.,Di Palma S.,Preisinger C.,Peng M.,Polat A.N.,Heck A.J.,Mohammed S.
Toward a comprehensive characterization of a human cancer cell phosphoproteome.
J. Proteome Res.
12
260-271
2013
640147
Bian Y.,Song C.,Cheng K.,Dong M.,Wang F.,Huang J.,Sun D.,Wang L.,Ye M.,Zou H.
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
J. Proteomics
96
253-262
2014
640148
Vaca Jacome A.S.,Rabilloud T.,Schaeffer-Reiss C.,Rompais M.,Ayoub D.,Lane L.,Bairoch A.,Van Dorsselaer A.,Carapito C.
N-terminome analysis of the human mitochondrial proteome.
Proteomics
15
2519-2524
2015
640149
Skjeldal L.,Markley J.L.,Coghlan V.M.,Vickery L.E.
1H NMR spectra of vertebrate [2Fe-2S] ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins.
Biochemistry
30
9078-9083
1991
640151
Strushkevich N.,MacKenzie F.,Cherkesova T.,Grabovec I.,Usanov S.,Park H.W.
Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system.
Proc. Natl. Acad. Sci. U.S.A.
108
10139-10143
2011