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The largest collection of articles on the three major gene families, this work ranges from enzymology to molecular biology to physiological implications. The three gene families are related in that the enzymes catalyse the NAD(P) dependent oxidation or reduction of carbonyl containing substrates. The substrates are important in diverse areas such as alcoholism, diabetes and cancer related problems as well as simple detoxification. The scope of the chapters, contributed by leading international scientists, is wide and covers gene regulation to enzyme mechanisms and protein structure. This is the only publication dealing in such depth with just three gene families. An important reference for researchers in toxicology and molecular biology.
- Order and disorder in mitochondrial aldehyde dehydrogenase (T. Hurley, S. Parmley, H. Breen).
- Chemical mechanisms and substrate binding sites of NADP-dependent aldehyde dehydrogenase from streptococcus mutans (S. Marchal, D. Cobessi, S. Rahuel-Clermont, F. Tete-Favier, A. Aubry, G. Branlant).
- Differences in nucleotide specificity and catalytic mechanism between vibrio harveyi aldehyde dehydrogenase and other members of the aldehyde dehydrogenase superfamily (Lei Zhang, B. Ahvazi, R. Szittner, A. Vrielink, E. Meighen).
- Beyond the catalytic core of ALDH: A web of important residues begins to emerge (J. Hempel, R. Lindahl, J. Perozich, Bi-Cheng Wang, I. Kuo, H. Nicholas).
- Subunit communication in tetrameric class 2 human liver aldehyde dehydrogenase as the basis for half-of-the-site reactivity and the dominance of the oriental subunit in a heterotetramers (H. Weiner, Baoxian Wei, Jianzhong Zhou).
- Interaction of sheep liver cytosolic aldehyde dehydrongenase with quercetin, resveratrol and diethylstilbestrol (T. M. Kitson, K.E. Kitson, S.A. Moore).
- Complexes of NADH with betaine aldehyde dehydrogenase from leaves of the plant Amaranthus Hypochondriacus (R. A. Munoz, C. Mujica-Jimenez).
- Overview - In Vitro inhibition of aldehyde dehydrogenase by disulfiram and metabolites (J. J. Lipsky, M. L. Shen, S. Naylor).
- In Vivo inhibition of aldehyde dehydrogenase by disulfiram (J. J. Lipsky, M. L. Shen, S. Naylor).
- Catalysis of dehydrogenation of 4-trans-(N,N-dimethylamino)cinnamaldehyde by aldehyde dehydrogenase (R. Pietruszko, T. Lehmann, M. Dryjanski, D. P. Abriola, W. Ambroziak).
- Coenzyme specificity in aldehyde dehydrogenase (J. Perozich, I. Kuo, R. Lindahl, J. Hempel).
- Interaction of human aldehyde dehydrogenase with aromatic substrates and ligands (A. Allali-Hassani, H. Weiner).
- Inhibition of ALDH3A1-catalyzed oxidation by chlorpropamide analogues (N. E. Sladek, G.K. Rekha, M. J. C. Lee, H. T. Nagasawa).
- Role of the C-terminal tail on the quaternary structure of aldehyde dehydrogenase (J. Rodriguez-Zavala, H. Weiner).
- Purification and characterization of grass carp mitochondrial aldehyde dehydrogenase (Wing-Ping Fong, Ka-Fai Choy).
- Making an oriental equivalent of the yeast cystosolic aldehyde dehydrogenase as well as making one with positive cooperativity in coenzyme binding by mutations of glutamate 492 and arginine 480 (Baoxian Wei, H. Weiner).
- Corneal and stomach expression of aldehyde dehydrogenases: From fish to mammals (A. Pappa, N.A. Sophos, V. Vasiliou).
- Betaine aldehyde dehydrogenase from rate liver mitochondrial matrix (R. Pietruszko, Ming-Kai Chern).
- Molecular dynamics simulation of class 3 aldehyde dehydrogenase (T. Wymore, H.B. Nicholas, J. Hempel).
- Inhibition of mouse aldehyde dehydrogenase 2 activity by the oriental variant of the human aldehyde dehydrogenase 2 gene (Jingjua-Jeng, D. Goldman, T. T.-Y. Wang, H. Weiner, B. J. Song).
- The effect of a novel irreversible inhibitor of aldehyde dehydrogenases 1 and 3 on tumor cell growth and death (R.A. Canuto, G. Muzio, R.A. Salvo, M. Maggiora, A. Trombetta, J. Chantepie, G. Fornet, R. Uwe, G. Quash).
- Inhibition of cytosolic class 3 aldehyde dehydrogenase by antisense oligonucleotides in rat hepatoma cells (G. Muzio, R.A. Canuto, A. Trombetta, M. Maggiora).
- Aldehyde dehydrongenase 3 gene regulation: Studies on constitutive and hypoxia-modulated expression (R. Reisdorph, R. Lindahl).
- Effects of 3-methylcholanthrene and aspirin co-administration on ALDH3A1 in HepG2 cells (M. Sotiropoulou, P. Pappas, M. Marselos).
- Three different stable human breast adenocarcinoma sublines that overexpress ALDH3A1 and certain other enzymes, apparently as a consequence of constitutively upregulated gene transcription mediated by transactivated EpREs (Electrophile Responsively Elements) present (S. Laksmaiah, N.E. Sladek ).
- Selective protection by stably transfected human ALDH3A1 ( but not human ALDH1A1) against toxicity of aliphatic aldehydes in V79 cells (A.J. Townsend, S. Leone-Kapler, R.L. Haynes, Yinghui Wu, L. Szweda, K.D. Bunting).
- Phenobarbital inducibility and differences in protein expression of an animal model (P. Pappas, P. Stephanou, P. Karamanakos, V. Vasiliou, M. Marselos).
- The formaldehyde metabolic detoxification enzyme systems and molecular cytotoxic mechanism in isolated rat hepatocytes (S. Teng, K. Beard, J. Pourahmad, M. Moridani, E. Easson, R. Poon, P. J. O'Brien).
- Fatty aldehyde dehydrogenase: Genomic structure, expression and mutation analysis in Sjögren-Larsson Syndrom (W.B. Rizzo, Zhili Lin, G. Carney).
- Characterization of Xenopus cytosolic thyroid-hormone-binding protein (xCTBP) with aldehyde dehydrogenase activity (K. Yamauchi, J.R. Tata).
- Aldehyde dehydrogenase gene superfamily: The 2000 update (N.A. Sophos, A. Pappa, T.L. Ziegler, V. Vasiliou).
ALCOHOL, RETINOL and other DEHYDROGENASES.
- Class II alcohol dehydrogenase (ADH2) - Adding the structure (S. Svensson, P. Strömberg, J.-O. Höög).
- Crystal structure of sorbitol dehydrogenase (K. Johansson, M. El-Ahmad, C. Kaiser, H. Jörnvall, H. Eklund, J.-O. Höög, S. Ramaswamy ).
- Characterization of a microsomal retinol dehydrogenase gene from amiphioxus: Retinoid metabolism before vertabrates (D. Dalfó, C. Cañestro, R. Albalat, R. Gonzàlez-Duarte).
- Ternary complexes of liver alcohol dehydrogenase (Y. Pocker, J.D. Page, Hong Li, C.C. Bhat).
- Bioinorganic and bioorganic studies of liver alcohol dehydrogenase (Y. Pocker).
- Mammalian alcohol dehydrogenase of higher classes. Analyses of human ADH5 and rat ADH6 (J.-O. Höög, M. Brandt, J.J. Hedberg, P. Strömberg).
- Genesis of drosophia ADH: The shaping of the enzymatic activity from an SDR ancestor ( J. Benach, S. Atrian, R. Ladenstein, R. Gonzàlez-Duarte).
- The activity of yeast ADH I and ADH II with long-chain alcohols and diols. (F.M. Dickinson, S. Dack).
- Characterization and functional role of Saccharomyces cerevisiae 2,3-butanediol dehydrogenase (E. González, M.R. Fernádez, C. Larroy, X. Parés, J.A. Biosca).
- Kinetic effects of a single-amino acid mutation in a highly variable loop (residues 114 to 120) of class IV ADH (A. Allali-Hassani, B. Crosas, X. Pares, J. Farres).
- Mouse alcohol dehydrogenase 4: kinetic mechanism, substrate specificy and simulation of effects of ethonol on retinoid metabolism (B.V. Plapp, J.L. Mitchell, K.B. Berst).
- Cloning of the human RoDH-related short chain dehydrogenase gene and analysis of its structure (N.Y. Kedishvili, O.V. Belyeva, W.H. Grough).
- Genetic dissection of retinoid dehydrogenases (G. Duester).
- Identification and expression of cosmids with an allelic variant of class I alcohol dehydrogenase in transgenic mice (G. Szalai, J. Ccci, M. Dewey, M. Felder).
- Variations and constant patterns in eukaryotic MDR enzymes. Conclusions from novel structures and characterized genomes (H. Jörnvall, J. Shafqat, B. Persson).
- The aldo-keto reductase (AKR) superfamily: An update (J.M. Jez, T.M. Penning).
- The crystal structure of the GCY1 protein from S. cerevisiae suggests a divergent aldo-keto reductase catalytic mechanism (E. Hur, D.K. Wilson).
- Characterization of the glutathione binding site of aldose reductase (K.V. Ramana, B.L. Dixit, S. Srivastava, A. Bhatnager, G.K. Balendriran, S.J. Watowich, J.M. Petrash, S.K. Srivastava).
- Metabolism of the 2-oxoaldehyde methylglyoxal by aldose reductase and by glyoxalase -I: Roles for glutathione in both enzymes and implications for diabetic complications (D.L. Vander Jagt, R.K. Hassebrook, L.A. Hunsaker, W.M. Brown, R.E. Royer).
- Involvement of aldose reductase in the metabolism of atherogenic aldehydes (S. Srivastava, Si-Qi Liu, D.J. Conklin, A. Zacarias, S.K. Srivastava , A. Bhatnager).
- Metabolic regulation of aldose reductase activity by nitric oxide donors (B.L. Dixit, K.V. Ramana, D. Chandra, E.B. Jackson, S. Srivastava, A. Bhatnager, S.K. Srivastava).
- Structural and functional properties of aldose reductase from the D-Xylose-metabolizing yeast Candida Tenuis (B. Nidetzky, P. Mayr, W. Neuhauser, M. Puchberger).
- Modulation of aldose reductase activity through S-thiolation by physiological thiois (M. Cappiello, P. Amodeo, B. Lopez Mendez, A. Scaloni, P.G. Vilardo, I. Cecconi, M. Dal Monte, S. Banditelli, V. Micheli, F.J. Giblin, A. Del Corso, U. Mura).
- Effect of bovine small intestine thioredoxin on aldose reductase activity (T. Mizoguchi).
- The role of aldose reductase in sugar cataract formation: aldose reductase plays a key role in lens epithelial cell death (apoptosis) (M. Murata, N. Ohta, S. Sakurai, S. Alam, Jen-Yui Tsai, P.F. Kador, S. Sato).
- Regulation of vascular smooth muscle cell growth by aldose reductase (A. Bhatnagar, J. Ruef, Si-Qi Liu, S. Srivastava, S.K. Srivastava).
- Molecular mechanisms of estrogen recognition and 17-keto reduction by human 17&bgr;-hydroxysteroid dehydrogenase 1 (D. Ghosh, P. Vihko).
- The crystal structure of an aldehyde reductase Y50F mutant-NADP complex and its implications for substrate binding (Q. Ye, D. Hyndman, N.C. Green, L. Li, Z. Jia, T.G. Flynn).
- Engineering steroid hormone specificity into aldo-keto reductases (T.M. Penning, Haiching Ma, J.M. Jez).
- Functional genomic studies of aldo-keto reductases (J.M. Petrash, B.S.N. Murthy, M. Young, K. Morris, L. Rikimaru, T.A. Griest, T. Harter).
- Three aldo-keto reductases of the yeast saccharomyces cerevisiae (G. Ford, E.M. Ellis).
- Forms and functions of human SDR enzymes (U.C.T. Oppermann, C. Filling, H. Jörnvall).
- 3&agr;-hydroxysteroid dehydrogenase / carbonyl reductase from comamonas testosteroni: Structure-function relationships (E. Maser, G. Xiong, C. Grimm, K. Reuter, R. Ficner).
- A model on the regulation of 3&agr;-hydroxysteroid dehydrogenase/carbonyl reductase xxpression in comamonas testosteroni (Guangming Xioong, H.-J. Martin, A. Blum, C. Schafers, E. Maser).
- Characterization of enzymes participating in carbonyl reduction of 4-methylinitrosamin-1-(3-pyridyl)-1-butanone (NNK) in human placenta (A. Atalla, E. Maser).
- Human 11&bgr;-hydroxysteriod dehydrogenase 1 / carbonyl reductase: additional domains for membrane attachment (A. Blum, A. Raum, H.-J. Martin, E. Maser).
- Expression and NNK reducing activities of carbonyl reductase and 118-hydroxysteroid dehydrogenase type 1 human lung (C. Finkh, G. Nagel, A. Atalla, B. Stinner, E. Maser).
- Identity of dimeric dihydrodiol dehydrogenase as NADP+-dependent D-xylose dehydrogenase in pig liver (S. Aoki, S. Ishikura, Y. Asada, N. Usami, A. Hara).
- New development in our understanding of the &bgr;-hydroxyacid dehydrogenases (R.K. Njau, C.A. Herndon, J.W. Hawes).
- 17&bgr;-hydroxysteroid dehydrogenase from the fungus cochliobolus lunatus: Structural and functional aspects (T.L. Rižner, J. Stojan, J. Adamski).
- Novel enzymological profiles of human 11&bgr;-hydroxysteroid dehydrogenase type 1. (M. Hult, C.S.I. Nobel, L. Abrahmsen, D.A. Nicoli-Griffith, H. Jörnvall, U.C.T. Oppermann).
- Metabolic activation of polycyclic aromatic hydrocarbon (PAH) trans-dihydrodiols by ubiquitously expressed aldehyde reductase (AKR1A1) (N.T. Palackal, M.E. Burczynski, R.G. Harvey, T.M. Penning).
- Role of the conserved Ser-Tyr-Lys triad of the SDR family in sepiapterin reductase (K. Fujimoto, M. Hara, H. Yamada, M. Sakurai, A. Inaba, A. Tomomura, S. Katoh).
- Site-directed mutagenesis studies of bovine liver cytosolic dihydrodiol dehydrogenase: The role of Asp-50, Tyr-55, Lys-84, His-117, Cys-145 and Cys-193 in enzymatic activity (T. Terada, N. Fujita, Y. Sugihara, R. Sato, T. Takagi, M. Maeda).
- Characterization of multiple Chinese hamster carbonyl reductases (T. Terada, Y. Sugihara, K. Nakamura, R. Sato, S. Sakuma, Y. Fujimoto, T. Fujita, N. Inazu, M. Maeda).
- Cloning and expression of cDNA encoding hamster liver 3-hydroxyhexobarbital /17&bgr; (3a)-hydroxysteroid dehydrogenase 1 (R. Takenoshita, Y. Nomura, S. Toki).
- Coenzyme specificity of human monomeric carbonyl reductase: contribution of Lys-15, Ala-37 and Arg-38 (M.-A. Sciotti, B. Wermuth). Miscellaneous.
- Enzyme regulation by reversible zinc inhibition: Glycerol phosphate dehydrogenase as an example (W. Maret, C.A. Yetman, Li-Juan Jiang).
- Physiological functions and hormonal regulation of mouse vas deferens protein (AKR1B7) in steroidogenic tissues (A. Martinez, C. Aigueperse, P. Val, M.-H. Dussault, C. Tournaire, M. Berger, G. Veyssière, C. Jean, A.-M. Lefrançois Martinez).
- Biogenic aldehyde(s) derived from the action of MAO may mediate the antidipsotropic effect of daidzin (Wing Ming Keung).
- Cytochrome P450 2E1 metabolically activates propargyl alcohol: propioladehyde-induced hepatocyte cytotoxicity (M.Y. Moridani, S. Khan, T. Chan, S. Teng, K. Beard, P.J. O'Brien).
- Apoptosis of PC 12 cells by 4-hydroxynonenal is mediated through selective activation of the c-Jun N-Terminal protein kinase pathway (B.J. Song, Yunjo Soh, Myung-Ae Bae, Jae-Eun Pie, Ji Wan, Kyu-Shik Jeong).
- Binding of pyridine coenzymes to the b-Subunit of the voltage sensitive potassium channels (Si-Qi Liu, Hongjun Jin, A. Zacarias, S. Srivastava, A. Bhatnager).
- No. of pages:
- © Elsevier Science 2001
- 14th May 2001
- Elsevier Science
- Hardcover ISBN:
Purdue University, Biochemistry Department, West Lafayette, IN 47907-1153, USA
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