EzCatDB S00228

EzCatDB: S00228

DB code	S00228
CATH domain	Domain 1	3.20.20.100		Catalytic domain
E.C.	1.1.1.21
CSA	2acu

CATH domain	Related DB codes (homologues)
3.20.20.100	S00227,S00229

Enzyme Name
Swiss-prot					KEGG
	O08782	P45377	P80276	P15121	KEGG
Protein name	Aldose reductase-related protein 2	Aldose reductase-related protein 2	Aldose reductase	Aldose reductase	aldehyde reductase aldose reductase polyol dehydrogenase (NADP+) ALR2 alditol:NADP+ oxidoreductase alditol:NADP+ 1-oxidoreductase NADPH-aldopentose reductase NADPH-aldose reductase
Synonyms	AR 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 code	Pathways
MAP00040	Pentose and glucuronate interconversions
MAP00051	Fructose and mannose metabolism
MAP00052	Galactose metabolism
MAP00561	Glycerolipid metabolism
MAP00620	Pyruvate metabolism

Swiss-prot:Accession Number	O08782	P45377	P80276	P15121
Entry name	ALD2_CRIGR	ALD2_MOUSE	ALDR_PIG	ALDR_HUMAN
Activity	Alditol + 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.
Subunit	Monomer (By similarity).	Monomer (By similarity).	Monomer.	Monomer.
Subcellular location	Cytoplasm (By similarity).	Cytoplasm (By similarity).	Cytoplasm.	Cytoplasm.
Cofactor

		Substrates				Products
KEGG-id		C00004	C00005	C01370	C00080	C00003	C00006	C00717
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
1c9wA		Unbound	Unbound	Unbound		Unbound	Bound:NAP	Unbound
1frbA		Unbound	Unbound	Analogue:ZST		Unbound	Bound:NAP	Unbound
1ah0A		Unbound	Unbound	Analogue:SBI		Unbound	Bound:NAP	Unbound
1ah3A		Unbound	Unbound	Analogue:TOL		Unbound	Bound:NAP	Unbound
1ah4A		Unbound	Unbound	Unbound		Unbound	Bound:NAP	Unbound
1ekoA		Unbound	Unbound	Analogue:I84		Unbound	Bound:NAP	Unbound
1adsA		Unbound	Unbound	Unbound		Unbound	Bound:NAP	Unbound
1az1A		Unbound	Unbound	Analogue:ALR 317		Unbound	Bound:NAP	Unbound
1az2A		Unbound	Unbound	Analogue:CIT		Unbound	Bound:NAP	Unbound
1ef3A		Unbound	Unbound	Analogue:FID		Unbound	Bound:NAP	Unbound
1ef3B		Unbound	Unbound	Analogue:FID		Unbound	Bound:NAP	Unbound
1el3A		Unbound	Unbound	Analogue:I84		Unbound	Bound:NAP	Unbound
1ieiA		Unbound	Unbound	Analogue:ZES		Unbound	Bound:NAP	Unbound
1pwlA		Unbound	Unbound	Analogue:1GL		Unbound	Bound:NAP	Unbound
1pwmA		Unbound	Unbound	Analogue:FID		Unbound	Bound:NAP	Unbound
1t40A		Unbound	Unbound	Analogue:ID5		Unbound	Bound:NAP	Unbound
1t41A		Unbound	Unbound	Analogue:ID5		Unbound	Bound:NAP	Unbound
1us0A		Unbound	Bound:NDP	Analogue:LDT		Unbound	Unbound	Unbound
1x96A		Unbound	Unbound	Analogue:CIT 319		Unbound	Bound:NAP	Unbound
1x97A		Unbound	Unbound	Analogue:FIR		Unbound	Bound:NAP	Unbound
1x98A		Unbound	Unbound	Analogue:CIT		Unbound	Bound:NAP	Unbound
1xgdA		Unbound	Unbound	Unbound		Unbound	Unbound	Unbound
2acqA		Unbound	Unbound	Unbound		Unbound	Bound:NAP	Analogue:G6P
2acrA		Unbound	Unbound	Unbound		Unbound	Bound:NAP	Analogue:CAC
2acsA		Unbound	Unbound	Analogue:CIT		Unbound	Bound:NAP	Unbound
2acuA		Unbound	Unbound	Analogue:CIT		Unbound	Bound:NAP	Unbound

Active-site residues
resource
PDB;1az1, 1az2, 2acq, 2acr, 2acs, 2acu & Swiss-prot;P15121, P45377, P80276
pdb		Catalytic residues	comment
1c9wA		`ASP 43;TYR 48;LYS 77;HIS 110`
1frbA		`ASP 43;TYR 48;LYS 77;HIS 110`
1ah0A		`ASP 43;TYR 48;LYS 77;HIS 110`
1ah3A		`ASP 43;TYR 48;LYS 77;HIS 110`
1ah4A		`ASP 43;TYR 48;LYS 77;HIS 110`
1ekoA		`ASP 43;TYR 48;LYS 77;HIS 110`
1adsA		`ASP 43;TYR 48;LYS 77;HIS 110`
1az1A		`ASP 43;TYR 48;LYS 77;HIS 110`	`mutant W219Y, C298A`
1az2A		`ASP 43;TYR 48;LYS 77;HIS 110`	`mutant W219Y, C298A`
1ef3A		`ASP 43;TYR 48;LYS 77;HIS 110`
1ef3B		`ASP 43;TYR 48;LYS 77;HIS 110`
1el3A		`ASP 43;TYR 48;LYS 77;HIS 110`
1ieiA		`ASP 43;TYR 48;LYS 77;HIS 110`
1pwlA		`ASP 43;TYR 48;LYS 77;HIS 110`
1pwmA		`ASP 43;TYR 48;LYS 77;HIS 110`
1t40A		`ASP 43;TYR 48;LYS 77;HIS 110`
1t41A		`ASP 43;TYR 48;LYS 77;HIS 110`
1us0A		`ASP 43;TYR 48;LYS 77;HIS 110`
1x96A		`ASP 43;TYR 48;LYS 77;HIS 110`
1x97A		`ASP 43;TYR 48;LYS 77;HIS 110`
1x98A		`ASP 43;TYR 48;LYS 77;HIS 110`
1xgdA		`ASP 43;TYR 48;LYS 77;HIS 110`
2acqA		`ASP 43;TYR 48;LYS 77;HIS 110`
2acrA		`ASP 43;TYR 48;LYS 77;HIS 110`
2acsA		`ASP 43;TYR 48;LYS 77;HIS 110`
2acuA		`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]
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.
[2]
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.
[3]
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.
[4]
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.
[5]
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.
[6]
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 Swiss-prot	P15121
[7]
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.
[8]
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 Swiss-prot	P80276
[9]
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 Swiss-prot	P15121
[10]
Comments	MUTAGENESIS OF ASP-43; TYR-48; LYS-77 AND HIS-110.
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 Swiss-prot	P15121
[11]
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 Swiss-prot	P15121
[12]
Comments	X-ray crystallography
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
[13]
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.
[14]
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.
[15]
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.
[16]
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 Swiss-prot	P45377
[17]
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.
[18]
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.
[19]
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.
[20]
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.
[21]
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 Swiss-prot	P15121
[22]
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.
[23]
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 Swiss-prot	P80276
[24]
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.
[25]
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.
[26]
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.
[27]
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.
[28]
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.
[29]
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.
[30]
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.
[31]
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.
[32]
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.
[33]
Comments	X-ray crystallography
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
[34]
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.
[35]
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.
[36]
Comments	X-ray crystallography
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
[37]
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.
[38]
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.
[39]
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
[40]
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.
[41]
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.
[42]
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.
[43]
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.
[44]
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.
[45]
Comments	X-ray crystallography
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
[46]
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.
[47]
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
[48]
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.
[49]
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.
[50]
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.
[51]
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.
[52]
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.
[53]
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.
[54]
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.
[55]
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
[56]
Comments	X-ray crystallography
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
[57]
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
[58]
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
[59]
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

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

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)

© Computational Biology Research Center, AIST, 2004 All Rights Reserved.