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Sequence of RDH16_HUMAN

EC Number:1.1.1.53

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3alpha(or 20beta)-hydroxysteroid dehydrogenase
O75452
Homo sapiens
317
35673
Reaction
androstan-3alpha,17beta-diol + NAD+ = 17beta-hydroxyandrostan-3-one + NADH + H+
Other sequences found for EC No. 1.1.1.53

EC Number:1.1.1.105

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
all-trans-retinol dehydrogenase (NAD+)
O75452
Homo sapiens
317
35673
Reaction
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+ = all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
Other sequences found for EC No. 1.1.1.105

EC Number:1.1.1.209

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3(or 17)alpha-hydroxysteroid dehydrogenase
O75452
Homo sapiens
317
35673
Reaction
androsterone + NAD(P)+ = 5alpha-androstane-3,17-dione + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.209

EC Number:1.1.1.315

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
11-cis-retinol dehydrogenase
O75452
Homo sapiens
317
35673
Reaction
11-cis-retinol-[retinal-binding-protein] + NAD+ = 11-cis-retinal-[retinol-binding-protein] + NADH + H+
Other sequences found for EC No. 1.1.1.315

General information:

Sequence
show sequence in fasta format
  0 MWLYLAVFVG LYYLLHWYRE RQVLSHLRDK YVFITGCDSG FGKLLARQLD ARGLRVLAAC
 60 LTEKGAEQLR GQTSDRLETV TLDVTKTESV AAAAQWVKEC VRDKGLWGLV NNAGISLPTA
120 PNELLTKQDF VTILDVNLLG VIDVTLSLLP LVRRARGRVV NVSSVMGRVS LFGGGYCISK
180 YGVEAFSDSL RRELSYFGVK VAMIEPGYFK TAVTSKERFL KSFLEIWDRS SPEVKEAYGE
240 KFVADYKKSA EQMEQKCTQD LSLVTNCMEH ALIACHPRTR YSAGWDAKLL YLPMSYMPTF
300 LVDAIMYWVS PSPAKAL
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
980529
Gough W.H.,VanOoteghem S.,Sint T.,Kedishvili N.Y.
cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3alpha-hydroxysteroids.
J. Biol. Chem.
273
19778-19785
1998
980530
Jurukovski V.,Markova N.G.,Karaman-Jurukovska N.,Randolph R.K.,Su J.,Napoli J.L.,Simon M.
Cloning and characterization of retinol dehydrogenase transcripts expressed in human epidermal keratinocytes.
Mol. Genet. Metab.
67
62-73
1999
980531
Cain J.M.,Zaino R.,Shearer D.,Bennett R.A.,Olt G.,Weisz J.
Expression of a retinol dehydrogenase (hRoDH-4), a member of the retinol/steroid dehydrogenase family implicated in retinoic acid biosynthesis, in normal and neoplastic endometria.
Am. J. Obstet. Gynecol.
186
675-683
2002
980532
Lapshina E.A.,Belyaeva O.V.,Chumakova O.V.,Kedishvili N.Y.
Differential recognition of the free versus bound retinol by human microsomal retinol/sterol dehydrogenases: characterization of the holo-CRBP dehydrogenase activity of RoDH-4.
Biochemistry
42
776-784
2003
980533
Persson B.,Kallberg Y.,Bray J.E.,Bruford E.,Dellaporta S.L.,Favia A.D.,Duarte R.G.,Joernvall H.,Kavanagh K.L.,Kedishvili N.,Kisiela M.,Maser E.,Mindnich R.,Orchard S.,Penning T.M.,Thornton J.M.,Adamski J.,Oppermann U.
The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative.
Chem. Biol. Interact.
178
94-98
2009
980534
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
980535
Fiandalo M.V.,Stocking J.J.,Pop E.A.,Wilton J.H.,Mantione K.M.,Li Y.,Attwood K.M.,Azabdaftari G.,Wu Y.,Watt D.S.,Wilson E.M.,Mohler J.L.
Inhibition of dihydrotestosterone synthesis in prostate cancer by combined frontdoor and backdoor pathway blockade.
Oncotarget
9
11227-11242
2018