DB code: S00228

CATH domain 3.20.20.100 : TIM Barrel Catalytic domain
E.C. 1.1.1.21
CSA 2acu
M-CSA 2acu
MACiE

CATH domain Related DB codes (homologues)
3.20.20.100 : TIM Barrel S00227 S00229

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
O08782 Aldose reductase-related protein 2
AR
EC 1.1.1.21
Aldehyde reductase
Aldo-keto reductase
NP_001233680.1 (Protein)
NM_001246751.1 (DNA/RNA sequence)
PF00248 (Aldo_ket_red)
[Graphical View]
P45377 Aldose reductase-related protein 2
AR
EC 1.1.1.21
Aldehyde reductase
Fibroblast growth factor-regulated protein
Protein FR-1
NP_032038.1 (Protein)
NM_008012.1 (DNA/RNA sequence)
PF00248 (Aldo_ket_red)
[Graphical View]
P80276 Aldose reductase
AR
EC 1.1.1.21
Aldehyde reductase
NP_001001539.1 (Protein)
NM_001001539.2 (DNA/RNA sequence)
PF00248 (Aldo_ket_red)
[Graphical View]
P15121 Aldose reductase
AR
EC 1.1.1.21
Aldehyde reductase
Aldo-keto reductase family 1 member B1
NP_001619.1 (Protein)
NM_001628.2 (DNA/RNA sequence)
PF00248 (Aldo_ket_red)
[Graphical View]

KEGG enzyme name
aldehyde reductase
aldose reductase
polyol dehydrogenase (NADP+)
ALR2
alditol:NADP+ oxidoreductase
alditol:NADP+ 1-oxidoreductase
NADPH-aldopentose reductase
NADPH-aldose reductase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
O08782 ALD2_CRIGR Alditol + NAD(P)(+) = aldose + NAD(P)H. Monomer (By similarity). Cytoplasm (By similarity).
P45377 ALD2_MOUSE Alditol + NAD(P)(+) = aldose + NAD(P)H. Monomer (By similarity). Cytoplasm (By similarity).
P80276 ALDR_PIG Alditol + NAD(P)(+) = aldose + NAD(P)H. Monomer. Cytoplasm.
P15121 ALDR_HUMAN Alditol + NAD(P)(+) = aldose + NAD(P)H. Monomer. Cytoplasm.

KEGG Pathways
Map code Pathways E.C.
MAP00040 Pentose and glucuronate interconversions
MAP00051 Fructose and mannose metabolism
MAP00052 Galactose metabolism
MAP00561 Glycerolipid metabolism
MAP00620 Pyruvate metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00004 C00005 C01370 C00080 C00003 C00006 C00717
E.C.
Compound NADH NADPH Aldose H+ NAD+ NADP+ Alditol
Type amide group,amine group,nucleotide amide group,amine group,nucleotide carbohydrate others amide group,amine group,nucleotide amide group,amine group,nucleotide carbohydrate
ChEBI 16908
16474
15378
15846
18009
PubChem 439153
5884
1038
5893
5886
1c9wA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Bound:NAP Unbound
1frbA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:ZST Unbound Bound:NAP Unbound
1ah0A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:SBI Unbound Bound:NAP Unbound
1ah3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:TOL Unbound Bound:NAP Unbound
1ah4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Bound:NAP Unbound
1ekoA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:I84 Unbound Bound:NAP Unbound
1adsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Bound:NAP Unbound
1az1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:ALR_317 Unbound Bound:NAP Unbound
1az2A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:CIT Unbound Bound:NAP Unbound
1ef3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:FID Unbound Bound:NAP Unbound
1ef3B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:FID Unbound Bound:NAP Unbound
1el3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:I84 Unbound Bound:NAP Unbound
1ieiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:ZES Unbound Bound:NAP Unbound
1pwlA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:1GL Unbound Bound:NAP Unbound
1pwmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:FID Unbound Bound:NAP Unbound
1t40A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:ID5 Unbound Bound:NAP Unbound
1t41A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:ID5 Unbound Bound:NAP Unbound
1us0A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NDP Analogue:LDT Unbound Unbound Unbound
1x96A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:CIT_319 Unbound Bound:NAP Unbound
1x97A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:FIR Unbound Bound:NAP Unbound
1x98A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:CIT Unbound Bound:NAP Unbound
1xgdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2acqA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Bound:NAP Analogue:G6P
2acrA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Bound:NAP Analogue:CAC
2acsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:CIT Unbound Bound:NAP Unbound
2acuA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:CIT Unbound Bound:NAP Unbound

Reference for Active-site residues
resource references E.C.
PDB;1az1, 1az2, 2acq, 2acr, 2acs, 2acu & Swiss-prot;P15121, P45377, P80276

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1c9wA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1frbA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1ah0A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1ah3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1ah4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1ekoA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1adsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1az1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110 mutant W219Y, C298A
1az2A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110 mutant W219Y, C298A
1ef3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1ef3B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1el3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1ieiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1pwlA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1pwmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1t40A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1t41A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1us0A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1x96A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1x97A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1x98A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
1xgdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
2acqA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
2acrA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
2acsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43;TYR 48;LYS 77;HIS 110
2acuA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 43; ;LYS 77;HIS 110 mutant Y48H

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[9]
p.84
[10]
p.25690-25692
[12]
p.2028-2031
[13]
Fig.2, p.956
[15]
Fig.6
[16]
p.14327
[18]
p.689-690
[32]
Fig.1, p.223-226
[45]
Scheme 1
[48]
Fig.1

References
[1]
Resource
Comments
Medline ID
PubMed ID 3138530
Journal Mol Pharmacol
Year 1988
Volume 34
Pages 377-87
Authors Ishida T, In Y, Ohishi H, Yamamoto D, Inoue M, Tanaka C, Ueno Y, Ohmomo Y, Kanda N, Tanaka A, et al
Title Structure-activity relationship of aldose reductase inhibitors based on X-ray crystal structures of oxazolecarbamate derivatives.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2125247
Journal Chem Pharm Bull (Tokyo)
Year 1990
Volume 38
Pages 1911-9
Authors Ohishi Y, Mukai T, Nagahara M, Yajima M, Kajikawa N, Miyahara K, Takano T
Title Preparations of 5-alkylmethylidene-3-carboxymethylrhodanine derivatives and their aldose reductase inhibitory activity.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 2120443
Journal J Med Chem
Year 1990
Volume 33
Pages 2892-9
Authors Ellingboe J, Alessi T, Millen J, Sredy J, King A, Prusiewicz C, Guzzo F, VanEngen D, Bagli J
Title (Pyrimidinyloxy)acetic acids and pyrimidineacetic acids as a novel class of aldose reductase inhibitors.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 1899452
Journal J Med Chem
Year 1991
Volume 34
Pages 108-22
Authors Mylari BL, Larson ER, Beyer TA, Zembrowski WJ, Aldinger CE, Dee MF, Siegel TW, Singleton DH
Title Novel, potent aldose reductase inhibitors: 3,4-dihydro-4-oxo-3-[[5-(trifluoromethyl)-2-benzothiazolyl] methyl]-1-phthalazineacetic acid (zopolrestat) and congeners.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 1902521
Journal J Mol Biol
Year 1991
Volume 218
Pages 695-8
Authors el-Kabbani O, Narayana SV, Babu YS, Moore KM, Flynn TG, Petrash JM, Westbrook EM, DeLucas LJ, Bugg CE
Title Purification, crystallization and preliminary crystallographic analysis of porcine aldose reductase.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS)
Medline ID 93077587
PubMed ID 1447221
Journal J Biol Chem
Year 1992
Volume 267
Pages 24841-7
Authors Borhani DW, Harter TM, Petrash JM
Title The crystal structure of the aldose reductase.NADPH binary complex.
Related PDB 1abn
Related UniProtKB P15121
[7]
Resource
Comments
Medline ID
PubMed ID 1613744
Journal J Med Chem
Year 1992
Volume 35
Pages 2169-77
Authors Lipinski CA, Aldinger CE, Beyer TA, Bordner J, Burdi DF, Bussolotti DL, Inskeep PB, Siegel TW
Title Hydantoin bioisosteres. In vivo active spiro hydroxy acetic acid aldose reductase inhibitors.
Related PDB
Related UniProtKB
[8]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID 92131138
PubMed ID 1734286
Journal Nature
Year 1992
Volume 355
Pages 469-72
Authors Rondeau JM, Tete-Favier F, Podjarny A, Reymann JM, Barth P, Biellmann JF, Moras D
Title Novel NADPH-binding domain revealed by the crystal structure of aldose reductase.
Related PDB 1dla
Related UniProtKB P80276
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS)
Medline ID 92320300
PubMed ID 1621098
Journal Science
Year 1992
Volume 257
Pages 81-4
Authors Wilson DK, Bohren KM, Gabbay KH, Quiocho FA
Title An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications.
Related PDB 1ads
Related UniProtKB P15121
[10]
Resource
Comments MUTAGENESIS OF ASP-43; TYR-48; LYS-77 AND HIS-110.
Medline ID
PubMed ID 8245005
Journal J Biol Chem
Year 1993
Volume 268
Pages 25687-93
Authors Tarle I, Borhani DW, Wilson DK, Quiocho FA, Petrash JM
Title Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110.
Related PDB
Related UniProtKB P15121
[11]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID 94052189
PubMed ID 8234324
Journal Proc Natl Acad Sci U S A
Year 1993
Volume 90
Pages 9847-51
Authors Wilson DK, Tarle I, Petrash JM, Quiocho FA
Title Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat.
Related PDB 1mar
Related UniProtKB P15121
[12]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8117659
Journal Biochemistry
Year 1994
Volume 33
Pages 2021-32
Authors Bohren KM, Grimshaw CE, Lai CJ, Harrison DH, Ringe D, Petsko GA, Gabbay KH
Title Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme.
Related PDB 2acq 2acr 2acs 2acu
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 8039602
Journal Diabetes
Year 1994
Volume 43
Pages 955-9
Authors Petrash JM, Tarle I, Wilson DK, Quiocho FA
Title Aldose reductase catalysis and crystallography. Insights from recent advances in enzyme structure and function.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 7484379
Journal Adv Exp Med Biol
Year 1995
Volume 372
Pages 193-201
Authors Flynn TG, Green NC, Bhatia MB, el-Kabbani O
Title Structure and mechanism of aldehyde reductase.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 7599122
Journal Biochemistry
Year 1995
Volume 34
Pages 8299-308
Authors De Winter HL, von Itzstein M
Title Aldose reductase as a target for drug design: molecular modeling calculations on the binding of acyclic sugar substrates to the enzyme.
Related PDB
Related UniProtKB
[16]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS)
Medline ID 96062495
PubMed ID 7578036
Journal Biochemistry
Year 1995
Volume 34
Pages 14323-30
Authors Wilson DK, Nakano T, Petrash JM, Quiocho FA
Title 1.7 A structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor.
Related PDB 1frb
Related UniProtKB P45377
[17]
Resource
Comments
Medline ID
PubMed ID 7622427
Journal J Antibiot (Tokyo)
Year 1995
Volume 48
Pages 439-46
Authors Matsumoto K, Nagashima K, Kamigauchi T, Kawamura Y, Yasuda Y, Ishii K, Uotani N, Sato T, Nakai H, Terui Y, et al
Title Salfredins, new aldose reductase inhibitors produced by Crucibulum sp. RF-3817. I. Fermentation, isolation and structures of salfredins.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 7552731
Journal Nat Struct Biol
Year 1995
Volume 2
Pages 687-92
Authors el-Kabbani O, Judge K, Ginell SL, Myles DA, DeLucas LJ, Flynn TG
Title Structure of porcine aldehyde reductase holoenzyme.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 9059665
Journal Adv Exp Med Biol
Year 1997
Volume 414
Pages 579-600
Authors Jez JM, Flynn TG, Penning TM
Title A nomenclature system for the aldo-keto reductase superfamily.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 9059648
Journal Adv Exp Med Biol
Year 1997
Volume 414
Pages 435-42
Authors Wilson DK, Nakano T, Petrash JM, Quiocho FA
Title Structural studies of aldo-keto reductase inhibition.
Related PDB
Related UniProtKB
[21]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID 98070237
PubMed ID 9405046
Journal Biochemistry
Year 1997
Volume 36
Pages 16134-40
Authors Harrison DH, Bohren KM, Petsko GA, Ringe D, Gabbay KH
Title The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant.
Related PDB 1az1 1az2
Related UniProtKB P15121
[22]
Resource
Comments
Medline ID
PubMed ID 9329083
Journal Proteins
Year 1997
Volume 29
Pages 186-92
Authors el-Kabbani O, Carper DA, McGowan MH, Devedjiev Y, Rees-Milton KJ, Flynn TG
Title Studies on the inhibitor-binding site of porcine aldehyde reductase: crystal structure of the holoenzyme-inhibitor ternary complex.
Related PDB
Related UniProtKB
[23]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
Medline ID 97341224
PubMed ID 9195881
Journal Structure
Year 1997
Volume 5
Pages 601-12
Authors Urzhumtsev A, Tete-Favier F, Mitschler A, Barbanton J, Barth P, Urzhumtseva L, Biellmann JF, Podjarny A, Moras D
Title A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil.
Related PDB 1ah0 1ah3 1ah4
Related UniProtKB P80276
[24]
Resource
Comments
Medline ID
PubMed ID 9871575
Journal Bioorg Med Chem Lett
Year 1998
Volume 8
Pages 641-6
Authors Rastelli G, Costantino L
Title Molecular dynamics simulations of the structure of aldose reductase complexed with the inhibitor tolrestat.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 9822541
Journal J Med Chem
Year 1998
Volume 41
Pages 4706-15
Authors Fresneau P, Cussac M, Morand JM, Szymonski B, Tranqui D, Leclerc G
Title Synthesis, activity, and molecular modeling of new 2, 4-dioxo-5-(naphthylmethylene)-3-thiazolidineacetic acids and 2-thioxo analogues as potent aldose reductase inhibitors.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 9767647
Journal J Med Chem
Year 1998
Volume 41
Pages 4118-29
Authors Negoro T, Murata M, Ueda S, Fujitani B, Ono Y, Kuromiya A, Komiya M, Suzuki K, Matsumoto J
Title Novel, highly potent aldose reductase inhibitors: (R)-(-)-2-(4-bromo-2-fluorobenzyl)-1,2,3,4- tetrahydropyrrolo[1,2-a]pyrazine -4-spiro-3'-pyrrolidine-1,2',3,5'-tetrone (AS-3201) and its congeners.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 9549756
Journal Pharmacol Rev
Year 1998
Volume 50
Pages 21-33
Authors Yabe-Nishimura C
Title Aldose reductase in glucose toxicity: a potential target for the prevention of diabetic complications.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 10089480
Journal Acta Crystallogr D Biol Crystallogr
Year 1999
Volume 55
Pages 721-3
Authors Lamour V, Barth P, Rogniaux H, Poterszman A, Howard E, Mitschler A, Van Dorsselaer A, Podjarny A, Moras D
Title Production of crystals of human aldose reductase with very high resolution diffraction.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 10533811
Journal Drug Des Discov
Year 1999
Volume 16
Pages 155-63
Authors Nakao K, Asao M, Shirai H, Shimizu R
Title 3D-pharmacophore analyses of aldose reductase inhibitory spiroquinazolinones.
Related PDB
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 10384727
Journal J Am Soc Mass Spectrom
Year 1999
Volume 10
Pages 635-47
Authors Rogniaux H, Van Dorsselaer A, Barth P, Biellmann JF, Barbanton J, van Zandt M, Chevrier B, Howard E, Mitschler A, Potier N, Urzhumtseva L, Moras D, Podjarny A
Title Binding of aldose reductase inhibitors: correlation of crystallographic and mass spectrometric studies.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 10493777
Journal Mol Vis
Year 1999
Volume 5
Pages 20
Authors El-Kabbani O, Old SE, Ginell SL, Carper DA
Title Aldose and aldehyde reductases: structure-function studies on the coenzyme and inhibitor-binding sites.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 10584067
Journal Proteins
Year 1999
Volume 37
Pages 218-27
Authors Varnai P, Richards WG, Lyne PD
Title Modelling the catalytic reaction in human aldose reductase.
Related PDB
Related UniProtKB
[33]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10771421
Journal Acta Crystallogr D Biol Crystallogr
Year 2000
Volume 56
Pages 536-40
Authors Calderone V, Chevrier B, Van Zandt M, Lamour V, Howard E, Poterszman A, Barth P, Mitschler A, Lu J, Dvornik DM, Klebe G, Kraemer O, Moorman AR, Moras D, Podjarny A
Title The structure of human aldose reductase bound to the inhibitor IDD384.
Related PDB 1eko 1el3
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 10882025
Journal Bioorg Med Chem
Year 2000
Volume 8
Pages 1151-8
Authors Rastelli G, Antolini L, Benvenuti S, Costantino L
Title Structural bases for the inhibition of aldose reductase by phenolic compounds.
Related PDB
Related UniProtKB
[35]
Resource
Comments
Medline ID
PubMed ID 10764810
Journal J Biol Chem
Year 2000
Volume 275
Pages 21587-95
Authors Dixit BL, Balendiran GK, Watowich SJ, Srivastava S, Ramana KV, Petrash JM, Bhatnagar A, Srivastava SK
Title Kinetic and structural characterization of the glutathione-binding site of aldose reductase.
Related PDB
Related UniProtKB
[36]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10882376
Journal J Med Chem
Year 2000
Volume 43
Pages 2479-83
Authors Oka M, Matsumoto Y, Sugiyama S, Tsuruta N, Matsushima M
Title A potent aldose reductase inhibitor, (2S,4S)-6-fluoro-2', 5'-dioxospiro[chroman-4,4'-imidazolidine]-2-carboxamide (Fidarestat): its absolute configuration and interactions with the aldose reductase by X-ray crystallography.
Related PDB 1ef3
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 10737739
Journal J Med Chem
Year 2000
Volume 43
Pages 1062-70
Authors Singh SB, Malamas MS, Hohman TC, Nilakantan R, Carper DA, Kitchen D
Title Molecular modeling of the aldose reductase-inhibitor complex based on the X-ray crystal structure and studies with single-site-directed mutants.
Related PDB
Related UniProtKB
[38]
Resource
Comments
Medline ID
PubMed ID 11025551
Journal Proteins
Year 2000
Volume 41
Pages 407-14
Authors El-Kabbani O, Rogniaux H, Barth P, Chung RP, Fletcher EV, Van Dorsselaer A, Podjarny A
Title Aldose and aldehyde reductases: correlation of molecular modeling and mass spectrometric studies on the binding of inhibitors to the active site.
Related PDB
Related UniProtKB
[39]
Resource
Comments
Medline ID
PubMed ID 10651037
Journal Proteins
Year 2000
Volume 38
Pages 41-8
Authors Ye Q, Hyndman D, Li X, Flynn TG, Jia Z
Title Crystal structure of CHO reductase, a member of the aldo-keto reductase superfamily.
Related PDB 1c9w
Related UniProtKB
[40]
Resource
Comments
Medline ID
PubMed ID 11444967
Journal Biochemistry
Year 2001
Volume 40
Pages 8216-26
Authors Kurono M, Fujiwara I, Yoshida K
Title Stereospecific interaction of a novel spirosuccinimide type aldose reductase inhibitor, AS-3201, with aldose reductase.
Related PDB
Related UniProtKB
[41]
Resource
Comments
Medline ID
PubMed ID 11306077
Journal Chem Biol Interact
Year 2001
Volume 130-132
Pages 583-95
Authors Nidetzky B, Mayr P, Neuhauser W, Puchberger M
Title Structural and functional properties of aldose xylose reductase from the D-xylose-metabolizing yeast Candida tenuis.
Related PDB
Related UniProtKB
[42]
Resource
Comments
Medline ID
PubMed ID 11306083
Journal Chem Biol Interact
Year 2001
Volume 130-132
Pages 651-8
Authors Ye Q, Hyndman D, Green NC, Li L, Jia Z, Flynn TG
Title The crystal structure of an aldehyde reductase Y50F mutant-NADP complex and its implications for substrate binding.
Related PDB
Related UniProtKB
[43]
Resource
Comments
Medline ID
PubMed ID 11278684
Journal J Biol Chem
Year 2001
Volume 276
Pages 19132-40
Authors Crosas B, Cederlund E, Torres D, Jornvall H, Farres J, Pares X
Title A vertebrate aldo-keto reductase active with retinoids and ethanol.
Related PDB
Related UniProtKB
[44]
Resource
Comments
Medline ID
PubMed ID 11356107
Journal J Med Chem
Year 2001
Volume 44
Pages 1718-28
Authors Iwata Y, Arisawa M, Hamada R, Kita Y, Mizutani MY, Tomioka N, Itai A, Miyamoto S
Title Discovery of novel aldose reductase inhibitors using a protein structure-based approach: 3D-database search followed by design and synthesis.
Related PDB
Related UniProtKB
[45]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11914486
Journal Acta Crystallogr D Biol Crystallogr
Year 2002
Volume 58
Pages 622-6
Authors Kinoshita T, Miyake H, Fujii T, Takakura S, Goto T
Title The structure of human recombinant aldose reductase complexed with the potent inhibitor zenarestat.
Related PDB 1iei
Related UniProtKB
[46]
Resource
Comments
Medline ID
PubMed ID 12003638
Journal Biochem J
Year 2002
Volume 366
Pages 889-99
Authors Mayr P, Nidetzky B
Title Catalytic reaction profile for NADH-dependent reduction of aromatic aldehydes by xylose reductase from Candida tenuis.
Related PDB
Related UniProtKB
[47]
Resource
Comments
Medline ID
PubMed ID 12102621
Journal Biochemistry
Year 2002
Volume 41
Pages 8785-95
Authors Kavanagh KL, Klimacek M, Nidetzky B, Wilson DK
Title The structure of apo and holo forms of xylose reductase, a dimeric aldo-keto reductase from Candida tenuis.
Related PDB 1jez 1k8c
Related UniProtKB
[48]
Resource
Comments
Medline ID
PubMed ID 12413844
Journal Bioorg Med Chem
Year 2002
Volume 10
Pages 3923-31
Authors Costantino L, Ferrari AM, Gamberini MC, Rastelli G
Title Nitrophenyl derivatives as aldose reductase inhibitors.
Related PDB
Related UniProtKB
[49]
Resource
Comments
Medline ID
PubMed ID 12007809
Journal FEMS Microbiol Lett
Year 2002
Volume 209
Pages 223-8
Authors Jeong EY, Kim IS, Lee H
Title Identification of lysine-78 as an essential residue in the Saccharomyces cerevisiae xylose reductase.
Related PDB
Related UniProtKB
[50]
Resource
Comments
Medline ID
PubMed ID 11839745
Journal J Biol Chem
Year 2002
Volume 277
Pages 16285-93
Authors Kozma E, Brown E, Ellis EM, Lapthorn AJ
Title The crystal structure of rat liver AKR7A1. A dimeric member of the aldo-keto reductase superfamily.
Related PDB
Related UniProtKB
[51]
Resource
Comments
Medline ID
PubMed ID 12193020
Journal J Nat Prod
Year 2002
Volume 65
Pages 1151-5
Authors Yoshikawa M, Murakami T, Ishiwada T, Morikawa T, Kagawa M, Higashi Y, Matsuda H
Title New flavonol oligoglycosides and polyacylated sucroses with inhibitory effects on aldose reductase and platelet aggregation from the flowers of Prunus mume.
Related PDB
Related UniProtKB
[52]
Resource
Comments
Medline ID
PubMed ID 12604217
Journal Chem Biol Interact
Year 2003
Volume 143-144
Pages 307-16
Authors Lee YS, Hodoscek M, Kador PF, Sugiyama K
Title Hydrogen bonding interactions between aldose reductase complexed with NADP(H) and inhibitor tolrestat studied by molecular dynamics simulations and binding assay.
Related PDB
Related UniProtKB
[53]
Resource
Comments
Medline ID
PubMed ID 12855766
Journal Proc Natl Acad Sci U S A
Year 2003
Volume 100
Pages 8742-7
Authors Muzet N, Guillot B, Jelsch C, Howard E, Lecomte C
Title Electrostatic complementarity in an aldose reductase complex from ultra-high-resolution crystallography and first-principles calculations.
Related PDB
Related UniProtKB
[54]
Resource
Comments
Medline ID
PubMed ID 15095003
Journal Cell Mol Life Sci
Year 2004
Volume 61
Pages 783-93
Authors Klebe G, Kramer O, Sotriffer C
Title Strategies for the design of inhibitors of aldose reductase, an enzyme showing pronounced induced-fit adaptations.
Related PDB
Related UniProtKB
[55]
Resource
Comments
Medline ID
PubMed ID 15146478
Journal Proteins
Year 2004
Volume 55
Pages 792-804
Authors Howard EI, Sanishvili R, Cachau RE, Mitschler A, Chevrier B, Barth P, Lamour V, Van Zandt M, Sibley E, Bon C, Moras D, Schneider TR, Joachimiak A, Podjarny A
Title Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A.
Related PDB 1us0
Related UniProtKB
[56]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 15146479
Journal Proteins
Year 2004
Volume 55
Pages 805-13
Authors El-Kabbani O, Darmanin C, Schneider TR, Hazemann I, Ruiz F, Oka M, Joachimiak A, Schulze-Briese C, Tomizaki T, Mitschler A, Podjarny A
Title Ultrahigh resolution drug design. II. Atomic resolution structures of human aldose reductase holoenzyme complexed with Fidarestat and Minalrestat: implications for the binding of cyclic imide inhibitors.
Related PDB 1pwl 1pwm
Related UniProtKB
[57]
Resource
Comments
Medline ID
PubMed ID 15272156
Journal Acta Crystallogr D Biol Crystallogr
Year 2004
Volume 60
Pages 1347-54
Authors Ruiz F, Hazemann I, Mitschler A, Joachimiak A, Schneider T, Karplus M, Podjarny A
Title The crystallographic structure of the aldose reductase-IDD552 complex shows direct proton donation from tyrosine 48.
Related PDB 1t40 1t41
Related UniProtKB
[58]
Resource
Comments
Medline ID
PubMed ID 15317464
Journal J Med Chem
Year 2004
Volume 47
Pages 4530-7
Authors El-Kabbani O, Darmanin C, Oka M, Schulze-Briese C, Tomizaki T, Hazemann I, Mitschler A, Podjarny A
Title High-resolution structures of human aldose reductase holoenzyme in complex with stereoisomers of the potent inhibitor Fidarestat: stereospecific interaction between the enzyme and a cyclic imide type inhibitor.
Related PDB 1x96 1x97 1x98
Related UniProtKB
[59]
Resource
Comments
Medline ID
PubMed ID 15769597
Journal Biochim Biophys Acta
Year 2005
Volume 1748
Pages 201-12
Authors Bohren KM, Brownlee JM, Milne AC, Gabbay KH, Harrison DH
Title The structure of Apo R268A human aldose reductase: hinges and latches that control the kinetic mechanism.
Related PDB 1xgd
Related UniProtKB

Comments
This enzyme catalyzes the following reaction:
(A) Hydride transfer from nicotinamide ring of NAD(P)H to the carbonyl group of substrate (aldose):

Created Updated
2004-08-12 2009-09-28