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Sequence of ALDR_HUMAN

EC Number:1.1.1.21

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
aldose reductase
P15121
Homo sapiens
316
35853
Reaction
alditol + NAD(P)+ = aldose + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.21

EC Number:1.1.1.54

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
allyl-alcohol dehydrogenase
P15121
Homo sapiens
316
35853
Reaction
allyl alcohol + NADP+ = acrolein + NADPH + H+
Other sequences found for EC No. 1.1.1.54

EC Number:1.1.1.188

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
prostaglandin-F synthase
P15121
Homo sapiens
316
35853
Reaction
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Other sequences found for EC No. 1.1.1.188

EC Number:1.1.1.300

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
NADP-retinol dehydrogenase
P15121
Homo sapiens
316
35853
Reaction
retinol + NADP+ = retinal + NADPH + H+
Other sequences found for EC No. 1.1.1.300

EC Number:1.1.1.372

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
D/L-glyceraldehyde reductase
P15121
Homo sapiens
316
35853
Reaction
glycerol + NADP+ = D-glyceraldehyde + NADPH + H+
Other sequences found for EC No. 1.1.1.372

General information:

Sequence
show sequence in fasta format
  0 MASRLLLNNG AKMPILGLGT WKSPPGQVTE AVKVAIDVGY RHIDCAHVYQ NENEVGVAIQ
 60 EKLREQVVKR EELFIVSKLW CTYHEKGLVK GACQKTLSDL KLDYLDLYLI HWPTGFKPGK
120 EFFPLDESGN VVPSDTNILD TWAAMEELVD EGLVKAIGIS NFNHLQVEMI LNKPGLKYKP
180 AVNQIECHPY LTQEKLIQYC QSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK
240 HNKTTAQVLI RFPMQRNLVV IPKSVTPERI AENFKVFDFE LSSQDMTTLL SYNRNWRVCA
300 LLSCTSHKDY PFHEEF
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
641429
Bohren K.M.,Bullock B.,Wermuth B.,Gabbay K.H.
The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases.
J. Biol. Chem.
264
9547-9551
1989
641430
Chung S.,Lamendola J.
Cloning and sequence determination of human placental aldose reductase gene.
J. Biol. Chem.
264
14775-14777
1989
641431
Graham A.,Hedge P.J.,Powell S.J.,Riley J.,Brown L.,Gammack A.,Carey F.,Markham A.F.
Nucleotide sequence of cDNA for human aldose reductase.
Nucleic Acids Res.
17
8368-8368
1989
641432
Grundmann U.,Bohn H.,Obermeier R.,Amann E.
Cloning and prokaryotic expression of a biologically active human placental aldose reductase.
DNA Cell Biol.
9
149-157
1990
641433
Nishimura C.,Matsuura Y.,Kokai Y.,Akera T.,Carper D.,Morjana N.,Lyons C.,Flynn T.G.
Cloning and expression of human aldose reductase.
J. Biol. Chem.
265
9788-9792
1990
641434
Graham A.,Brown L.,Hedge P.J.,Gammack A.J.,Markham A.F.
Structure of the human aldose reductase gene.
J. Biol. Chem.
266
6872-6877
1991
641435
Ko B.C.B.,Ruepp B.,Bohren K.M.,Gabbay K.H.,Chung S.S.
Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene.
J. Biol. Chem.
272
16431-16437
1997
641436
Hartmann T.B.,Thiel D.,Dummer R.,Schadendorf D.,Eichmueller S.
SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma.
Br. J. Dermatol.
150
252-258
2004
641437
Ota T.,Suzuki Y.,Nishikawa T.,Otsuki T.,Sugiyama T.,Irie R.,Wakamatsu A.,Hayashi K.,Sato H.,Nagai K.,Kimura K.,Makita H.,Sekine M.,Obayashi M.,Nishi T.,Shibahara T.,Tanaka T.,Ishii S.,Yamamoto J.,Saito K.,Kawai Y.,Isono Y.,Nakamura Y.,Nagahari K.,Murakami K.,Yasuda T.,Iwayanagi T.,Wagatsuma M.,Shiratori A.,Sudo H.,Hosoiri T.,Kaku Y.,Kodaira H.,Kondo H.,Sugawara M.,Takahashi M.,Kanda K.,Yokoi T.,Furuya T.,Kikkawa E.,Omura Y.,Abe K.,Kamihara K.,Katsuta N.,Sato K.,Tanikawa M.,Yamazaki M.,Ninomiya K.,Ishibashi T.,Yamashita H.,Murakawa K.,Fujimori K.,Tanai H.,Kimata M.,Watanabe M.,Hiraoka S.,Chiba Y.,Ishida S.,Ono Y.,Takiguchi S.,Watanabe S.,Yosida M.,Hotuta T.,Kusano J.,Kanehori K.,Takahashi-Fujii A.,Hara H.,Tanase T.-O.,Nomura Y.,Togiya S.,Komai F.,Hara R.,Takeuchi K.,Arita M.,Imose N.,Musashino K.,Yuuki H.,Oshima A.,Sasaki N.,Aotsuka S.,Yoshikawa Y.,Matsunawa H.,Ichihara T.,Shiohata N.,Sano S.,Moriya S.,Momiyama H.,Satoh N.,Takami S.,Terashima Y.,Suzuki O.,Nakagawa S.,Senoh A.,Mizoguchi H.,Goto Y.,Shimizu F.,Wakebe H.,Hishigaki H.,Watanabe T.,Sugiyama A.,Takemoto M.,Kawakami B.,Yamazaki M.,Watanabe K.,Kumagai A.,Itakura S.,Fukuzumi Y.,Fujimori Y.,Komiyama M.,Tashiro H.,Tanigami A.,Fujiwara T.,Ono T.,Yamada K.,Fujii Y.,Ozaki K.,Hirao M.,Ohmori Y.,Kawabata A.,Hikiji T.,Kobatake N.,Inagaki H.,Ikema Y.,Okamoto S.,Okitani R.,Kawakami T.,Noguchi S.,Itoh T.,Shigeta K.,Senba T.,Matsumura K.,Nakajima Y.,Mizuno T.,Morinaga M.,Sasaki M.,Togashi T.,Oyama M.,Hata H.,Watanabe M.,Komatsu T.,Mizushima-Sugano J.,Satoh T.,Shirai Y.,Takahashi Y.,Nakagawa K.,Okumura K.,Nagase T.,Nomura N.,Kikuchi H.,Masuho Y.,Yamashita R.,Nakai K.,Yada T.,Nakamura Y.,Ohara O.,Isogai T.,Sugano S.
Complete sequencing and characterization of 21,243 full-length human cDNAs.
Nat. Genet.
36
40-45
2004
641440
Scherer S.W.,Cheung J.,MacDonald J.R.,Osborne L.R.,Nakabayashi K.,Herbrick J.-A.,Carson A.R.,Parker-Katiraee L.,Skaug J.,Khaja R.,Zhang J.,Hudek A.K.,Li M.,Haddad M.,Duggan G.E.,Fernandez B.A.,Kanematsu E.,Gentles S.,Christopoulos C.C.,Choufani S.,Kwasnicka D.,Zheng X.H.,Lai Z.,Nusskern D.R.,Zhang Q.,Gu Z.,Lu F.,Zeesman S.,Nowaczyk M.J.,Teshima I.,Chitayat D.,Shuman C.,Weksberg R.,Zackai E.H.,Grebe T.A.,Cox S.R.,Kirkpatrick S.J.,Rahman N.,Friedman J.M.,Heng H.H.Q.,Pelicci P.G.,Lo-Coco F.,Belloni E.,Shaffer L.G.,Pober B.,Morton C.C.,Gusella J.F.,Bruns G.A.P.,Korf B.R.,Quade B.J.,Ligon A.H.,Ferguson H.,Higgins A.W.,Leach N.T.,Herrick S.R.,Lemyre E.,Farra C.G.,Kim H.-G.,Summers A.M.,Gripp K.W.,Roberts W.,Szatmari P.,Winsor E.J.T.,Grzeschik K.-H.,Teebi A.,Minassian B.A.,Kere J.,Armengol L.,Pujana M.A.,Estivill X.,Wilson M.D.,Koop B.F.,Tosi S.,Moore G.E.,Boright A.P.,Zlotorynski E.,Kerem B.,Kroisel P.M.,Petek E.,Oscier D.G.,Mould S.J.,Doehner H.,Doehner K.,Rommens J.M.,Vincent J.B.,Venter J.C.,Li P.W.,Mural R.J.,Adams M.D.,Tsui L.-C.
Human chromosome 7: DNA sequence and biology.
Science
300
767-772
2003
641442
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
641443
Ferraretto A.,Negri A.,Giuliani A.,De Grada L.,Fuhrman Conti A.M.,Ronchi S.
Aldose reductase is involved in long-term adaptation of EUE cells to hyperosmotic stress.
Biochim. Biophys. Acta
1175
283-288
1993
641444
Morjana N.A.,Lyons C.,Flynn T.G.
Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine.
J. Biol. Chem.
264
2912-2919
1989
641446
Liu S.Q.,Bhatnagar A.,Ansari N.H.,Srivastava S.K.
Identification of the reactive cysteine residue in human placenta aldose reductase.
Biochim. Biophys. Acta
1164
268-272
1993
641447
Jaquinod M.,Potier N.,Klarskov K.,Reymann J.-M.,Sorokine O.,Kieffer S.,Barth P.,Andriantomanga V.,Biellmann J.-F.,van Dorsselaer A.
Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes.
Eur. J. Biochem.
218
893-903
1993
641448
Hamada Y.,Kitoh R.,Raskin P.
Crucial role of aldose reductase activity and plasma glucose level in sorbitol accumulation in erythrocytes from diabetic patients.
Diabetes
40
1233-1240
1991
641449
Tarle I.,Borhani D.W.,Wilson D.K.,Quiocho F.A.,Petrash J.M.
Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110.
J. Biol. Chem.
268
25687-25693
1993
641450
O'Connor T.,Ireland L.S.,Harrison D.J.,Hayes J.D.
Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members.
Biochem. J.
343
487-504
1999
641451
Crosas B.,Hyndman D.J.,Gallego O.,Martras S.,Pares X.,Flynn T.G.,Farres J.
Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism.
Biochem. J.
373
973-979
2003
641452
Spite M.,Baba S.P.,Ahmed Y.,Barski O.A.,Nijhawan K.,Petrash J.M.,Bhatnagar A.,Srivastava S.
Substrate specificity and catalytic efficiency of aldo-keto reductases with phospholipid aldehydes.
Biochem. J.
405
95-105
2007
641453
Kabututu Z.,Manin M.,Pointud J.C.,Maruyama T.,Nagata N.,Lambert S.,Lefrancois-Martinez A.M.,Martinez A.,Urade Y.
Prostaglandin F2alpha synthase activities of aldo-keto reductase 1B1, 1B3 and 1B7.
J. Biochem.
145
161-168
2009
641454
Shen Y.,Zhong L.,Johnson S.,Cao D.
Human aldo-keto reductases 1B1 and 1B10: a comparative study on their enzyme activity toward electrophilic carbonyl compounds.
Chem. Biol. Interact.
191
192-198
2011
641455
Ruiz F.X.,Moro A.,Gallego O.,Ardevol A.,Rovira C.,Petrash J.M.,Pares X.,Farres J.
Human and rodent aldo-keto reductases from the AKR1B subfamily and their specificity with retinaldehyde.
Chem. Biol. Interact.
191
199-205
2011
641456
Gauci S.,Helbig A.O.,Slijper M.,Krijgsveld J.,Heck A.J.,Mohammed S.
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
Anal. Chem.
81
4493-4501
2009
641457
Choudhary C.,Kumar C.,Gnad F.,Nielsen M.L.,Rehman M.,Walther T.C.,Olsen J.V.,Mann M.
Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Science
325
834-840
2009
641458
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
641459
Wilson D.K.,Bohren K.M.,Gabbay K.H.,Quiocho F.A.
An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications.
Science
257
81-84
1992
641460
Borhani D.W.,Harter T.M.,Pertrash J.M.
The crystal structure of the aldose reductase.NADPH binary complex.
J. Biol. Chem.
267
24841-24847
1992
641461
Wilson D.K.,Tarle I.,Petrash J.M.,Quiocho F.A.
Refined 1.8-A structure of human aldose reductase complexed with the potent inhibitor zopolrestat.
Proc. Natl. Acad. Sci. U.S.A.
90
9847-9851
1993
641462
Harrison D.H.,Bohren K.M.,Petsko G.A.,Ringe D.,Gabbay K.H.
The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant.
Biochemistry
36
16134-16140
1997
641463
Ruiz F.,Hazemann I.,Mitschler A.,Joachimiak A.,Schneider T.,Karplus M.,Podjarny A.
The crystallographic structure of the aldose reductase-IDD552 complex shows direct proton donation from tyrosine 48.
Acta Crystallogr. D
60
1347-1354
2004
641464
Howard E.I.,Sanishvili R.,Cachau R.E.,Mitschler A.,Chevrier B.,Barth P.,Lamour V.,Van Zandt M.,Sibley E.,Bon C.,Moras D.,Schneider T.R.,Joachimiak A.,Podjarny A.
Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A.
Proteins
55
792-804
2004
641465
Steuber H.,Zentgraf M.,Podjarny A.,Heine A.,Klebe G.
High-resolution crystal structure of aldose reductase complexed with the novel sulfonyl-pyridazinone inhibitor exhibiting an alternative active site anchoring group.
J. Mol. Biol.
356
45-56
2006
641466
Biadene M.,Hazemann I.,Cousido A.,Ginell S.,Joachimiak A.,Sheldrick G.M.,Podjarny A.,Schneider T.R.
The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop.
Acta Crystallogr. D
63
665-672
2007
641467
Steuber H.,Zentgraf M.,La Motta C.,Sartini S.,Heine A.,Klebe G.
Evidence for a novel binding site conformer of aldose reductase in ligand-bound state.
J. Mol. Biol.
369
186-197
2007
641468
Steuber H.,Heine A.,Klebe G.
Structural and thermodynamic study on aldose reductase: nitro-substituted inhibitors with strong enthalpic binding contribution.
J. Mol. Biol.
368
618-638
2007