EzCatDB: S00228

DB codeS00228
CATH domainDomain 13.20.20.100Catalytic domain
E.C.1.1.1.21
CSA2acu

CATH domainRelated DB codes (homologues)
3.20.20.100S00227,S00229

Enzyme Name
Swiss-protKEGG

O08782P45377P80276P15121
Protein nameAldose reductase-related protein 2Aldose reductase-related protein 2Aldose reductaseAldose reductasealdehyde reductase
aldose reductase
polyol dehydrogenase (NADP+)
ALR2
alditol:NADP+ oxidoreductase
alditol:NADP+ 1-oxidoreductase
NADPH-aldopentose reductase
NADPH-aldose reductase
SynonymsAR
EC 1.1.1.21
Aldehyde reductase
Aldo-keto reductase
AR
EC 1.1.1.21
Aldehyde reductase
Fibroblast growth factor-regulated protein
Protein FR-1
AR
EC 1.1.1.21
Aldehyde reductase
AR
EC 1.1.1.21
Aldehyde reductase

KEGG pathways
MAP codePathways
MAP00040Pentose and glucuronate interconversions
MAP00051Fructose and mannose metabolism
MAP00052Galactose metabolism
MAP00561Glycerolipid metabolism
MAP00620Pyruvate metabolism

Swiss-prot:Accession NumberO08782P45377P80276P15121
Entry nameALD2_CRIGRALD2_MOUSEALDR_PIGALDR_HUMAN
ActivityAlditol + NAD(P)(+) = aldose + NAD(P)H.Alditol + NAD(P)(+) = aldose + NAD(P)H.Alditol + NAD(P)(+) = aldose + NAD(P)H.Alditol + NAD(P)(+) = aldose + NAD(P)H.
SubunitMonomer (By similarity).Monomer (By similarity).Monomer.Monomer.
Subcellular locationCytoplasm (By similarity).Cytoplasm (By similarity).Cytoplasm.Cytoplasm.
Cofactor





SubstratesProducts
KEGG-idC00004C00005C01370C00080C00003C00006C00717
CompoundNADHNADPHAldoseH+NAD+NADP+Alditol
Typeamide group,amine group,nucleotideamide group,amine group,nucleotidecarbohydrateothersamide group,amine group,nucleotideamide group,amine group,nucleotidecarbohydrate
1c9wAUnboundUnboundUnbound
UnboundBound:NAPUnbound
1frbAUnboundUnboundAnalogue:ZST
UnboundBound:NAPUnbound
1ah0AUnboundUnboundAnalogue:SBI
UnboundBound:NAPUnbound
1ah3AUnboundUnboundAnalogue:TOL
UnboundBound:NAPUnbound
1ah4AUnboundUnboundUnbound
UnboundBound:NAPUnbound
1ekoAUnboundUnboundAnalogue:I84
UnboundBound:NAPUnbound
1adsAUnboundUnboundUnbound
UnboundBound:NAPUnbound
1az1AUnboundUnboundAnalogue:ALR 317
UnboundBound:NAPUnbound
1az2AUnboundUnboundAnalogue:CIT
UnboundBound:NAPUnbound
1ef3AUnboundUnboundAnalogue:FID
UnboundBound:NAPUnbound
1ef3BUnboundUnboundAnalogue:FID
UnboundBound:NAPUnbound
1el3AUnboundUnboundAnalogue:I84
UnboundBound:NAPUnbound
1ieiAUnboundUnboundAnalogue:ZES
UnboundBound:NAPUnbound
1pwlAUnboundUnboundAnalogue:1GL
UnboundBound:NAPUnbound
1pwmAUnboundUnboundAnalogue:FID
UnboundBound:NAPUnbound
1t40AUnboundUnboundAnalogue:ID5
UnboundBound:NAPUnbound
1t41AUnboundUnboundAnalogue:ID5
UnboundBound:NAPUnbound
1us0AUnboundBound:NDPAnalogue:LDT
UnboundUnboundUnbound
1x96AUnboundUnboundAnalogue:CIT 319
UnboundBound:NAPUnbound
1x97AUnboundUnboundAnalogue:FIR
UnboundBound:NAPUnbound
1x98AUnboundUnboundAnalogue:CIT
UnboundBound:NAPUnbound
1xgdAUnboundUnboundUnbound
UnboundUnboundUnbound
2acqAUnboundUnboundUnbound
UnboundBound:NAPAnalogue:G6P
2acrAUnboundUnboundUnbound
UnboundBound:NAPAnalogue:CAC
2acsAUnboundUnboundAnalogue:CIT
UnboundBound:NAPUnbound
2acuAUnboundUnboundAnalogue:CIT
UnboundBound:NAPUnbound

Active-site residues
resource
PDB;1az1, 1az2, 2acq, 2acr, 2acs, 2acu & Swiss-prot;P15121, P45377, P80276
pdbCatalytic residuescomment
1c9wAASP 43;TYR 48;LYS 77;HIS 110

1frbAASP 43;TYR 48;LYS 77;HIS 110

1ah0AASP 43;TYR 48;LYS 77;HIS 110

1ah3AASP 43;TYR 48;LYS 77;HIS 110

1ah4AASP 43;TYR 48;LYS 77;HIS 110

1ekoAASP 43;TYR 48;LYS 77;HIS 110

1adsAASP 43;TYR 48;LYS 77;HIS 110

1az1AASP 43;TYR 48;LYS 77;HIS 110
mutant W219Y, C298A
1az2AASP 43;TYR 48;LYS 77;HIS 110
mutant W219Y, C298A
1ef3AASP 43;TYR 48;LYS 77;HIS 110

1ef3BASP 43;TYR 48;LYS 77;HIS 110

1el3AASP 43;TYR 48;LYS 77;HIS 110

1ieiAASP 43;TYR 48;LYS 77;HIS 110

1pwlAASP 43;TYR 48;LYS 77;HIS 110

1pwmAASP 43;TYR 48;LYS 77;HIS 110

1t40AASP 43;TYR 48;LYS 77;HIS 110

1t41AASP 43;TYR 48;LYS 77;HIS 110

1us0AASP 43;TYR 48;LYS 77;HIS 110

1x96AASP 43;TYR 48;LYS 77;HIS 110

1x97AASP 43;TYR 48;LYS 77;HIS 110

1x98AASP 43;TYR 48;LYS 77;HIS 110

1xgdAASP 43;TYR 48;LYS 77;HIS 110

2acqAASP 43;TYR 48;LYS 77;HIS 110

2acrAASP 43;TYR 48;LYS 77;HIS 110

2acsAASP 43;TYR 48;LYS 77;HIS 110

2acuAASP 43;      ;LYS 77;HIS 110
mutant Y48H

References for Catalytic Mechanism
ReferencesSectionsNo. 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
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Year1991
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PubMed ID1902521
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CommentsX-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS)
Medline ID93077587
PubMed ID1447221
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Year1992
Volume267
Pages24841-7
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Related PDB1abn
Related Swiss-protP15121
[7]
PubMed ID1613744
JournalJ Med Chem
Year1992
Volume35
Pages2169-77
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[8]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID92131138
PubMed ID1734286
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Year1992
Volume355
Pages469-72
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TitleNovel NADPH-binding domain revealed by the crystal structure of aldose reductase.
Related PDB1dla
Related Swiss-protP80276
[9]
CommentsX-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS)
Medline ID92320300
PubMed ID1621098
JournalScience
Year1992
Volume257
Pages81-4
AuthorsWilson DK, Bohren KM, Gabbay KH, Quiocho FA
TitleAn unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications.
Related PDB1ads
Related Swiss-protP15121
[10]
CommentsMUTAGENESIS OF ASP-43; TYR-48; LYS-77 AND HIS-110.
PubMed ID8245005
JournalJ Biol Chem
Year1993
Volume268
Pages25687-93
AuthorsTarle I, Borhani DW, Wilson DK, Quiocho FA, Petrash JM
TitleProbing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110.
Related Swiss-protP15121
[11]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID94052189
PubMed ID8234324
JournalProc Natl Acad Sci U S A
Year1993
Volume90
Pages9847-51
AuthorsWilson DK, Tarle I, Petrash JM, Quiocho FA
TitleRefined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat.
Related PDB1mar
Related Swiss-protP15121
[12]
CommentsX-ray crystallography
PubMed ID8117659
JournalBiochemistry
Year1994
Volume33
Pages2021-32
AuthorsBohren KM, Grimshaw CE, Lai CJ, Harrison DH, Ringe D, Petsko GA, Gabbay KH
TitleTyrosine-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 PDB2acq,2acr,2acs,2acu
[13]
PubMed ID8039602
JournalDiabetes
Year1994
Volume43
Pages955-9
AuthorsPetrash JM, Tarle I, Wilson DK, Quiocho FA
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Year1995
Volume372
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Year1995
Volume34
Pages8299-308
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TitleAldose reductase as a target for drug design: molecular modeling calculations on the binding of acyclic sugar substrates to the enzyme.
[16]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS)
Medline ID96062495
PubMed ID7578036
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Year1995
Volume34
Pages14323-30
AuthorsWilson DK, Nakano T, Petrash JM, Quiocho FA
Title1.7 A structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor.
Related PDB1frb
Related Swiss-protP45377
[17]
PubMed ID7622427
JournalJ Antibiot (Tokyo)
Year1995
Volume48
Pages439-46
AuthorsMatsumoto K, Nagashima K, Kamigauchi T, Kawamura Y, Yasuda Y, Ishii K, Uotani N, Sato T, Nakai H, Terui Y, et al
TitleSalfredins, new aldose reductase inhibitors produced by Crucibulum sp. RF-3817. I. Fermentation, isolation and structures of salfredins.
[18]
PubMed ID7552731
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Volume2
Pages687-92
Authorsel-Kabbani O, Judge K, Ginell SL, Myles DA, DeLucas LJ, Flynn TG
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Year1997
Volume414
Pages579-600
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[20]
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Year1997
Volume414
Pages435-42
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TitleStructural studies of aldo-keto reductase inhibition.
[21]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID98070237
PubMed ID9405046
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Year1997
Volume36
Pages16134-40
AuthorsHarrison DH, Bohren KM, Petsko GA, Ringe D, Gabbay KH
TitleThe alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant.
Related PDB1az1,1az2
Related Swiss-protP15121
[22]
PubMed ID9329083
JournalProteins
Year1997
Volume29
Pages186-92
Authorsel-Kabbani O, Carper DA, McGowan MH, Devedjiev Y, Rees-Milton KJ, Flynn TG
TitleStudies on the inhibitor-binding site of porcine aldehyde reductase: crystal structure of the holoenzyme-inhibitor ternary complex.
[23]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
Medline ID97341224
PubMed ID9195881
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TitleA 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil.
Related PDB1ah0,1ah3,1ah4
Related Swiss-protP80276
[24]
PubMed ID9871575
JournalBioorg Med Chem Lett
Year1998
Volume8
Pages641-6
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Year1998
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JournalJ Med Chem
Year1998
Volume41
Pages4118-29
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TitleNovel, 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.
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Year1998
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Year1999
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Pages721-3
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Year1999
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Pages155-63
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[30]
PubMed ID10384727
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Year1999
Volume10
Pages635-47
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PubMed ID10493777
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Year1999
Volume5
Pages20
AuthorsEl-Kabbani O, Old SE, Ginell SL, Carper DA
TitleAldose and aldehyde reductases: structure-function studies on the coenzyme and inhibitor-binding sites.
[32]
PubMed ID10584067
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Year1999
Volume37
Pages218-27
AuthorsVarnai P, Richards WG, Lyne PD
TitleModelling the catalytic reaction in human aldose reductase.
[33]
CommentsX-ray crystallography
PubMed ID10771421
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Year2000
Volume56
Pages536-40
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Related PDB1eko,1el3
[34]
PubMed ID10882025
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Year2000
Volume8
Pages1151-8
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PubMed ID10764810
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Year2000
Volume275
Pages21587-95
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TitleKinetic and structural characterization of the glutathione-binding site of aldose reductase.
[36]
CommentsX-ray crystallography
PubMed ID10882376
JournalJ Med Chem
Year2000
Volume43
Pages2479-83
AuthorsOka M, Matsumoto Y, Sugiyama S, Tsuruta N, Matsushima M
TitleA 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 PDB1ef3
[37]
PubMed ID10737739
JournalJ Med Chem
Year2000
Volume43
Pages1062-70
AuthorsSingh SB, Malamas MS, Hohman TC, Nilakantan R, Carper DA, Kitchen D
TitleMolecular modeling of the aldose reductase-inhibitor complex based on the X-ray crystal structure and studies with single-site-directed mutants.
[38]
PubMed ID11025551
JournalProteins
Year2000
Volume41
Pages407-14
AuthorsEl-Kabbani O, Rogniaux H, Barth P, Chung RP, Fletcher EV, Van Dorsselaer A, Podjarny A
TitleAldose and aldehyde reductases: correlation of molecular modeling and mass spectrometric studies on the binding of inhibitors to the active site.
[39]
PubMed ID10651037
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Year2000
Volume38
Pages41-8
AuthorsYe Q, Hyndman D, Li X, Flynn TG, Jia Z
TitleCrystal structure of CHO reductase, a member of the aldo-keto reductase superfamily.
Related PDB1c9w
[40]
PubMed ID11444967
JournalBiochemistry
Year2001
Volume40
Pages8216-26
AuthorsKurono M, Fujiwara I, Yoshida K
TitleStereospecific interaction of a novel spirosuccinimide type aldose reductase inhibitor, AS-3201, with aldose reductase.
[41]
PubMed ID11306077
JournalChem Biol Interact
Year2001
Volume130-132
Pages583-95
AuthorsNidetzky B, Mayr P, Neuhauser W, Puchberger M
TitleStructural and functional properties of aldose xylose reductase from the D-xylose-metabolizing yeast Candida tenuis.
[42]
PubMed ID11306083
JournalChem Biol Interact
Year2001
Volume130-132
Pages651-8
AuthorsYe Q, Hyndman D, Green NC, Li L, Jia Z, Flynn TG
TitleThe crystal structure of an aldehyde reductase Y50F mutant-NADP complex and its implications for substrate binding.
[43]
PubMed ID11278684
JournalJ Biol Chem
Year2001
Volume276
Pages19132-40
AuthorsCrosas B, Cederlund E, Torres D, Jornvall H, Farres J, Pares X
TitleA vertebrate aldo-keto reductase active with retinoids and ethanol.
[44]
PubMed ID11356107
JournalJ Med Chem
Year2001
Volume44
Pages1718-28
AuthorsIwata Y, Arisawa M, Hamada R, Kita Y, Mizutani MY, Tomioka N, Itai A, Miyamoto S
TitleDiscovery of novel aldose reductase inhibitors using a protein structure-based approach: 3D-database search followed by design and synthesis.
[45]
CommentsX-ray crystallography
PubMed ID11914486
JournalActa Crystallogr D Biol Crystallogr
Year2002
Volume58
Pages622-6
AuthorsKinoshita T, Miyake H, Fujii T, Takakura S, Goto T
TitleThe structure of human recombinant aldose reductase complexed with the potent inhibitor zenarestat.
Related PDB1iei
[46]
PubMed ID12003638
JournalBiochem J
Year2002
Volume366
Pages889-99
AuthorsMayr P, Nidetzky B
TitleCatalytic reaction profile for NADH-dependent reduction of aromatic aldehydes by xylose reductase from Candida tenuis.
[47]
PubMed ID12102621
JournalBiochemistry
Year2002
Volume41
Pages8785-95
AuthorsKavanagh KL, Klimacek M, Nidetzky B, Wilson DK
TitleThe structure of apo and holo forms of xylose reductase, a dimeric aldo-keto reductase from Candida tenuis.
Related PDB1jez,1k8c
[48]
PubMed ID12413844
JournalBioorg Med Chem
Year2002
Volume10
Pages3923-31
AuthorsCostantino L, Ferrari AM, Gamberini MC, Rastelli G
TitleNitrophenyl derivatives as aldose reductase inhibitors.
[49]
PubMed ID12007809
JournalFEMS Microbiol Lett
Year2002
Volume209
Pages223-8
AuthorsJeong EY, Kim IS, Lee H
TitleIdentification of lysine-78 as an essential residue in the Saccharomyces cerevisiae xylose reductase.
[50]
PubMed ID11839745
JournalJ Biol Chem
Year2002
Volume277
Pages16285-93
AuthorsKozma E, Brown E, Ellis EM, Lapthorn AJ
TitleThe crystal structure of rat liver AKR7A1. A dimeric member of the aldo-keto reductase superfamily.
[51]
PubMed ID12193020
JournalJ Nat Prod
Year2002
Volume65
Pages1151-5
AuthorsYoshikawa M, Murakami T, Ishiwada T, Morikawa T, Kagawa M, Higashi Y, Matsuda H
TitleNew flavonol oligoglycosides and polyacylated sucroses with inhibitory effects on aldose reductase and platelet aggregation from the flowers of Prunus mume.
[52]
PubMed ID12604217
JournalChem Biol Interact
Year2003
Volume143-144
Pages307-16
AuthorsLee YS, Hodoscek M, Kador PF, Sugiyama K
TitleHydrogen bonding interactions between aldose reductase complexed with NADP(H) and inhibitor tolrestat studied by molecular dynamics simulations and binding assay.
[53]
PubMed ID12855766
JournalProc Natl Acad Sci U S A
Year2003
Volume100
Pages8742-7
AuthorsMuzet N, Guillot B, Jelsch C, Howard E, Lecomte C
TitleElectrostatic complementarity in an aldose reductase complex from ultra-high-resolution crystallography and first-principles calculations.
[54]
PubMed ID15095003
JournalCell Mol Life Sci
Year2004
Volume61
Pages783-93
AuthorsKlebe G, Kramer O, Sotriffer C
TitleStrategies for the design of inhibitors of aldose reductase, an enzyme showing pronounced induced-fit adaptations.
[55]
PubMed ID15146478
JournalProteins
Year2004
Volume55
Pages792-804
AuthorsHoward 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
TitleUltrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A.
Related PDB1us0
[56]
CommentsX-ray crystallography
PubMed ID15146479
JournalProteins
Year2004
Volume55
Pages805-13
AuthorsEl-Kabbani O, Darmanin C, Schneider TR, Hazemann I, Ruiz F, Oka M, Joachimiak A, Schulze-Briese C, Tomizaki T, Mitschler A, Podjarny A
TitleUltrahigh 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 PDB1pwl,1pwm
[57]
PubMed ID15272156
JournalActa Crystallogr D Biol Crystallogr
Year2004
Volume60
Pages1347-54
AuthorsRuiz F, Hazemann I, Mitschler A, Joachimiak A, Schneider T, Karplus M, Podjarny A
TitleThe crystallographic structure of the aldose reductase-IDD552 complex shows direct proton donation from tyrosine 48.
Related PDB1t40,1t41
[58]
PubMed ID15317464
JournalJ Med Chem
Year2004
Volume47
Pages4530-7
AuthorsEl-Kabbani O, Darmanin C, Oka M, Schulze-Briese C, Tomizaki T, Hazemann I, Mitschler A, Podjarny A
TitleHigh-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 PDB1x96,1x97,1x98
[59]
PubMed ID15769597
JournalBiochim Biophys Acta
Year2005
Volume1748
Pages201-12
AuthorsBohren KM, Brownlee JM, Milne AC, Gabbay KH, Harrison DH
TitleThe structure of Apo R268A human aldose reductase: hinges and latches that control the kinetic mechanism.
Related PDB1xgd

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

createdupdated
2004-08-122009-09-28


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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