Sequence of AK1CL_MOUSE
EC Number:1.1.1.209
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
androsterone + NAD(P)+ = 5alpha-androstane-3,17-dione + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.209
General information:
Sequence
0 MNSKCHCVIL NDGNFIPVLG FGTALPLECP KSKAKELTKI AIDAGFHHFD SASVYNTEDH
60 VGEAIRSKIA DGTVRREDIF YTSKVWCTSL HPELVRASLE RSLQKLQFDY VDLYLIHYPM
120 ALKPGEENFP VDEHGKLIFD RVDLCATWEA MEKCKDAGLT KSIGVSNFNY RQLEMILNKP
180 GLKYKPVCNQ VECHPYLNQM KLLDFCKSKD IVLVAYGVLG TQRYGGWVDQ NSPVLLDEPV
240 LGSMAKKYNR TPALIALRYQ LQRGIVVLNT SLKEERIKEN MQVFEFQLSS EDMKVLDGLN
300 RNMRYIPAAI FKGHPNWPFL DEY
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
641073
Ishikura S.,Usami N.,Nakajima S.,Shiraishi H.,El-Kabbani O.,Hara A.
Characterization of two isoforms of mouse 3(17)alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase family.
Biol. Pharm. Bull.
27
1939-1945
2004
641074
Bellemare V.,Faucher F.,Breton R.,Luu-The V.
Characterization of 17alpha-hydroxysteroid dehydrogenase activity (17-alpha-HSD) and its involvement in the biosynthesis of epitestosterone.
BMC Biochem.
6
12-12
2005
641075
Carninci P.,Kasukawa T.,Katayama S.,Gough J.,Frith M.C.,Maeda N.,Oyama R.,Ravasi T.,Lenhard B.,Wells C.,Kodzius R.,Shimokawa K.,Bajic V.B.,Brenner S.E.,Batalov S.,Forrest A.R.,Zavolan M.,Davis M.J.,Wilming L.G.,Aidinis V.,Allen J.E.,Ambesi-Impiombato A.,Apweiler R.,Aturaliya R.N.,Bailey T.L.,Bansal M.,Baxter L.,Beisel K.W.,Bersano T.,Bono H.,Chalk A.M.,Chiu K.P.,Choudhary V.,Christoffels A.,Clutterbuck D.R.,Crowe M.L.,Dalla E.,Dalrymple B.P.,de Bono B.,Della Gatta G.,di Bernardo D.,Down T.,Engstrom P.,Fagiolini M.,Faulkner G.,Fletcher C.F.,Fukushima T.,Furuno M.,Futaki S.,Gariboldi M.,Georgii-Hemming P.,Gingeras T.R.,Gojobori T.,Green R.E.,Gustincich S.,Harbers M.,Hayashi Y.,Hensch T.K.,Hirokawa N.,Hill D.,Huminiecki L.,Iacono M.,Ikeo K.,Iwama A.,Ishikawa T.,Jakt M.,Kanapin A.,Katoh M.,Kawasawa Y.,Kelso J.,Kitamura H.,Kitano H.,Kollias G.,Krishnan S.P.,Kruger A.,Kummerfeld S.K.,Kurochkin I.V.,Lareau L.F.,Lazarevic D.,Lipovich L.,Liu J.,Liuni S.,McWilliam S.,Madan Babu M.,Madera M.,Marchionni L.,Matsuda H.,Matsuzawa S.,Miki H.,Mignone F.,Miyake S.,Morris K.,Mottagui-Tabar S.,Mulder N.,Nakano N.,Nakauchi H.,Ng P.,Nilsson R.,Nishiguchi S.,Nishikawa S.,Nori F.,Ohara O.,Okazaki Y.,Orlando V.,Pang K.C.,Pavan W.J.,Pavesi G.,Pesole G.,Petrovsky N.,Piazza S.,Reed J.,Reid J.F.,Ring B.Z.,Ringwald M.,Rost B.,Ruan Y.,Salzberg S.L.,Sandelin A.,Schneider C.,Schoenbach C.,Sekiguchi K.,Semple C.A.,Seno S.,Sessa L.,Sheng Y.,Shibata Y.,Shimada H.,Shimada K.,Silva D.,Sinclair B.,Sperling S.,Stupka E.,Sugiura K.,Sultana R.,Takenaka Y.,Taki K.,Tammoja K.,Tan S.L.,Tang S.,Taylor M.S.,Tegner J.,Teichmann S.A.,Ueda H.R.,van Nimwegen E.,Verardo R.,Wei C.L.,Yagi K.,Yamanishi H.,Zabarovsky E.,Zhu S.,Zimmer A.,Hide W.,Bult C.,Grimmond S.M.,Teasdale R.D.,Liu E.T.,Brusic V.,Quackenbush J.,Wahlestedt C.,Mattick J.S.,Hume D.A.,Kai C.,Sasaki D.,Tomaru Y.,Fukuda S.,Kanamori-Katayama M.,Suzuki M.,Aoki J.,Arakawa T.,Iida J.,Imamura K.,Itoh M.,Kato T.,Kawaji H.,Kawagashira N.,Kawashima T.,Kojima M.,Kondo S.,Konno H.,Nakano K.,Ninomiya N.,Nishio T.,Okada M.,Plessy C.,Shibata K.,Shiraki T.,Suzuki S.,Tagami M.,Waki K.,Watahiki A.,Okamura-Oho Y.,Suzuki H.,Kawai J.,Hayashizaki Y.
The transcriptional landscape of the mammalian genome.
Science
309
1559-1563
2005
641076
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
641077
Huttlin E.L.,Jedrychowski M.P.,Elias J.E.,Goswami T.,Rad R.,Beausoleil S.A.,Villen J.,Haas W.,Sowa M.E.,Gygi S.P.
A tissue-specific atlas of mouse protein phosphorylation and expression.
Cell
143
1174-1189
2010
641078
Faucher F.,Pereira de Jesus-Tran K.,Cantin L.,Luu-The V.,Labrie F.,Breton R.
Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase (apoenzyme and enzyme-NADP(H) binary complex): identification of molecular determinants responsible for the unique 17alpha-reductive activity of this enzyme.
J. Mol. Biol.
364
747-763
2006
641079
Dhagat U.,Carbone V.,Chung R.P.-T.,Schulze-Briese C.,Endo S.,Hara A.,El-Kabbani O.
Structure of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) holoenzyme from an orthorhombic crystal form: an insight into the bifunctionality of the enzyme.
Acta Crystallogr. F
63
825-830
2007
641080
Faucher F.,Cantin L.,Pereira de Jesus-Tran K.,Lemieux M.,Luu-The V.,Labrie F.,Breton R.
Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto reductases: identification and characterization of amino acid residues critical for substrate binding.
J. Mol. Biol.
369
525-540
2007
641081
Dhagat U.,Endo S.,Mamiya H.,Hara A.,El-Kabbani O.
Structure of the G225P/G226P mutant of mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) ternary complex: implications for the binding of inhibitor and substrate.
Acta Crystallogr. D
65
257-265
2009
641082
Dhagat U.,Endo S.,Mamiya H.,Hara A.,El-Kabbani O.
Studies on a Tyr residue critical for the binding of coenzyme and substrate in mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21): structure of the Y224D mutant enzyme.
Acta Crystallogr. D
66
198-204
2010
