ADH1/YOL086C Literature Guide Help

Other names published for ADH1: ADC1, alcohol dehydrogenase ADH1, YOL086C

ADH1 - Non-Fungal Related Genes/Proteins (37)

ReferenceOther Genes Addressed
Devi PG, et al.  (2009) Inhibition of a Zn(II)-containing enzyme, alcohol dehydrogenase, by anticancer antibiotics, mithramycin and chromomycin A(3). J Biol Inorg Chem 14(3):347-59
Smith ED, et al.  (2008) Quantitative evidence for conserved longevity pathways between divergent eukaryotic species. Genome Res 18(4):564-70
Gonzalez-Duarte R and Albalat R  (2005) Merging protein, gene and genomic data: the evolution of the MDR-ADH family. Heredity 95(3):184-97
Trivedi A, et al.  (2005) Optimization of adsorptive immobilization of alcohol dehydrogenases. J Biosci Bioeng 99(4):340-7
Jin L, et al.  (2004) Inhibition of alcohol dehydrogenase by bismuth. J Inorg Biochem 98(8):1331-7
Jornvall H, et al.  (2003) Multiplicity of eukaryotic ADH and other MDR forms. Chem Biol Interact 143-144:255-61
Riveros-Rosas H, et al.  (2003) Diversity, taxonomy and evolution of medium-chain dehydrogenase/reductase superfamily. Eur J Biochem 270(16):3309-34
Nordling E, et al.  (2002) Differential multiplicity of MDR alcohol dehydrogenases: enzyme genes in the human genome versus those in organisms initially studied. Cell Mol Life Sci 59(6):1070-5
Nordling E, et al.  (2002) Medium-chain dehydrogenases/reductases (MDR). Family characterizations including genome comparisons and active site modeling. Eur J Biochem 269(17):4267-76
Foreman TM, et al.  (2001) Effects of charged water-soluble polymers on the stability and activity of yeast alcohol dehydrogenase and subtilisin Carlsberg. Biotechnol Bioeng 76(3):241-6
Jornvall H, et al.  (2001) Variations and constant patterns in eukaryotic MDR enzymes. Conclusions from novel structures and characterized genomes. Chem Biol Interact 130-132(1-3):491-8
Bakker BM, et al.  (2000) Compartmentation protects trypanosomes from the dangerous design of glycolysis. Proc Natl Acad Sci U S A 97(5):2087-92
Benos P, et al.  (2000) Acquisition of a potential marker for insect transformation: isolation of a novel alcohol dehydrogenase gene from Bactrocera oleae by functional complementation in yeast. Mol Gen Genet 263(1):90-5
Tynan J, et al.  (2000) Synthesis of a highly substituted N(6)-linked immobilized NAD(+) derivative using a rapid solid-phase modular approach: suitability for use with the kinetic locking-on tactic for bioaffinity purification of NAD(+)-dependent dehydrogenases. Protein Expr Purif 20(3):421-34
Conway TT, et al.  (1999) Diethylcarbamoylating/nitroxylating agents as dual action inhibitors of aldehyde dehydrogenase: a disulfiram-cyanamide merger. J Med Chem 42(20):4016-20
Fan F and Plapp BV  (1999) Probing the affinity and specificity of yeast alcohol dehydrogenase I for coenzymes. Arch Biochem Biophys 367(2):240-9
Dallet S and Legoy MD  (1996) Hydrostatic pressure induces conformational and catalytic changes on two alcohol dehydrogenases but no oligomeric dissociation. Biochim Biophys Acta 1294(1):15-24
Derrick S and Large PJ  (1993) Activities of the enzymes of the Ehrlich pathway and formation of branched-chain alcohols in Saccharomyces cerevisiae and Candida utilis grown in continuous culture on valine or ammonium as sole nitrogen source. J Gen Microbiol 139(11):2783-92
Green DW, et al.  (1993) Inversion of the substrate specificity of yeast alcohol dehydrogenase. J Biol Chem 268(11):7792-8
Rucker J, et al.  (1992) Role of internal thermodynamics in determining hydrogen tunneling in enzyme-catalyzed hydrogen transfer reactions. Biochemistry 31(46):11489-99
Fan F, et al.  (1991) An aspartate residue in yeast alcohol dehydrogenase I determines the specificity for coenzyme. Biochemistry 30(26):6397-401
Gould RM and Plapp BV  (1990) Substitution of arginine for histidine-47 in the coenzyme binding site of yeast alcohol dehydrogenase I. Biochemistry 29(23):5463-8
De Weck Z, et al.  (1987) Interdependence of coenzyme-induced conformational work and binding potential in yeast alcohol and porcine heart lactate dehydrogenases: a hydrogen-deuterium exchange study. Biochemistry 26(15):4769-76
Hasinoff BB, et al.  (1987) The association reaction of yeast alcohol dehydrogenase with coenzyme is partly diffusion-controlled in solvents of increased viscosity. Biochim Biophys Acta 911(1):53-8
Suarez MD and Ferguson-Miller S  (1987) Yeast and horse liver alcohol dehydrogenases: potential problems in target size analysis and evidence for a monomer active unit. Biochemistry 26(12):3340-7
Eklund H, et al.  (1985) Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases. Biochemistry 24(27):8005-12
Jornvall H, et al.  (1984) Extended superfamily of short alcohol-polyol-sugar dehydrogenases: structural similarities between glucose and ribitol dehydrogenases. FEBS Lett 165(2):190-6
Jornvall H, et al.  (1984) Extensive variations and basic features in the alcohol dehydrogenase-sorbitol dehydrogenase family. Eur J Biochem 140(1):17-23
Yamazaki Y, et al.  (1984) A kinetic study on the binding of monomeric and polymeric derivatives of NAD+ to yeast alcohol dehydrogenase. J Biochem 95(1):109-15
Woenckhaus C, et al.  (1979) Affinity labelling of yeast and liver alcohol dehydrogenases with the NAD analogue 4-(3-bromoacetylpyridinio)butyldiphosphoadenosine. Eur J Biochem 93(1):65-90