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Aldose reductase and ϱ-crystallin belong to the same protein superfamily as aldehyde reductase [PDF]

FEBS Letters, 1987
Aldose reductase (EC 1.1.1.21) has been implicated in a variety of diabetic complications. Here we present the first primary sequence data for the rat lens enzyme, obtained by amino acid and cDNA analysis.
Toshimichi Shinohara, Cheryl M Craft, C Nishimura   +2 more
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Aldehyde Reductase

Michihiko Kataoka
exaly   +2 more sources

Rat liver aldehyde reductase

Biochemical Pharmacology, 1977
Abstract Rat liver aldehyde reductase is a soluble constitutive enzyme having the ability to catalyze the reduction of several natural aldehydes such as lactaldehyde, glyceraldehyde, glyceraldehyde-3-phosphate, glucuronate, glucuronolactone, and succinic semialdehyde.
R L, Felsted, D R, Richter, N R, Bachur
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In vivo role of aldehyde reductase

Biochimica et Biophysica Acta (BBA) - General Subjects, 2012
Aldehyde reductase (AKR1A; EC 1.1.1.2) catalyzes the reduction of various types of aldehydes. To ascertain the physiological role of AKR1A, we examined AKR1A knockout mice.Ascorbic acid concentrations in AKR1A knockout mice tissues were examined, and the effects of human AKR1A transgene were analyzed.
Motoko, Takahashi, Satoshi, Miyata, Junichi, Fujii, Yoko, Inai, Shigemitsu, Ueyama, Motoko, Araki, Tomoyoshi, Soga, Reiko, Fujinawa, Chiaki, Nishitani, Shigeru, Ariki, Takeyuki, Shimizu, Tomomi, Abe, Yoshito, Ihara, Morimitsu, Nishikimi, Yasunori, Kozutsumi, Naoyuki, Taniguchi, Yoshio, Kuroki   +16 more
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Inhibition of aldehyde reductase by aldose reductase inhibitors

Biochemical Pharmacology, 1990
A broad group of structurally diverse aldose reductase inhibitors including flavonoids, carboxylic acids and hydantoins, have been examined for their ability to inhibit rat kidney aldehyde reductase (EC 1.1.1.19, EC 1.1.1.20) versus rat lens aldose reductase (EC 1.1.1.21).
S, Sato, P F, Kador
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Identification of Pig Brain Aldehyde Reductases with the High‐Km Aldehyde Reductase, the Low‐Km Aldehyde Reductase and Aldose Reductase, Carbonyl Reductase, and Succinic Semialdehyde Reductase

Journal of Neurochemistry, 1985
Abstract: Four NADPH‐dependent aldehyde reductases (ALRs) isolated from pig brain have been characterized with respect to substrate specificity, inhibition by drugs, and immunological criteria. The major enzyme, ALR1, is identical in these respects with the high‐Km aldehyde reductase, glucuronate reductase, and tissue‐specific, e.g., pig kidney ...
J A, Cromlish, T G, Flynn
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Structure and Mechanism of Aldehyde Reductase

1995
Aldehyde reductase (ALR1, EC 1.1.1.2) and aldose reductase (ALR2, EC 1.1.1.21) catalyze the NADPH-dependent reduction of a wide range of aromatic and aliphatic aldehydes to their corresponding alcohols. Despite a recently expressed opinion that aldose reductase is of little consequence (Harding, 1992) the past few years have seen a great advancement in
T G, Flynn, N C, Green, M B, Bhatia, O, el-Kabbani   +3 more
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Human kidney aldose and aldehyde reductases

Journal of Diabetes and its Complications, 1993
Mounting experimental evidence links increased aldose reductase activity with diabetes-related kidney functional changes. To investigate the interrelationship of NADPH-dependent reductases in the human kidney, both aldose reductase and aldehyde reductase were purified from human kidney by a series of chromatographic procedures, including gel filtration
S, Sato, P F, Kador
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Structure of porcine aldehyde reductase holoenzyme

Nature Structural Biology, 1995
Aldehyde reductase, a member of the aldo-keto reductase superfamily, catalyzes the NADPH-dependent reduction of a variety of aldehydes to their corresponding alcohols. The structure of porcine aldehyde reductase-NADPH binary complex has been determined by x-ray diffraction methods and refined to a crystallographic R-factor of 0.20 at 2.4 A resolution ...
O, el-Kabbani, K, Judge, S L, Ginell, D A, Myles, L J, DeLucas, T G, Flynn   +5 more
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Evolution of Aldehyde Reductase: An Immunological Approach to the Relatedness of Aldehyde Reductase from Different Species

1980
Antisera to aldehyde reductase from fruit-fly (Drosophila melanogaster) and chicken were cross-reacted with aldehyde reductase from several species of insects and birds using the technique of microcomplement fixation. Large differences in immunological distances are evident between species of the Class Insecta and of the Class Aves indicating ...
W S, Davidson, T G, Flynn
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