ADH1/YOL086C Literature Guide Help

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

ADH1 - Protein Sequence Features (28)

ReferenceOther Genes Addressed
Brandes N, et al.  (2011) Using quantitative redox proteomics to dissect the yeast redoxome. J Biol Chem 286(48):41893-903
Carroll KM, et al.  (2011) Absolute quantification of the glycolytic pathway in yeast: deployment of a complete QconCAT approach. Mol Cell Proteomics 10(12):M111.007633
Tanaka N, et al.  (2011) Selected reaction monitoring by linear ion-trap mass spectrometry can effectively be applicable to simultaneous quantification of multiple peptides. Biol Pharm Bull 34(1):135-41
Auer R, et al.  (2010) Pharmacophore mapping via cross-relaxation during adiabatic fast passage. J Am Chem Soc 132(5):1480-1
Marino SM, et al.  (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21
Kwiecien RA, et al.  (2009) Probing stereoselectivity and pro-chirality of hydride transfer during short-chain alcohol dehydrogenase activity: a combined quantitative 2H NMR and computational approach. Arch Biochem Biophys 482(1-2):42-51
Pal S, et al.  (2009) Activity of yeast alcohol dehydrogenases on benzyl alcohols and benzaldehydes: characterization of ADH1 from Saccharomyces carlsbergensis and transition state analysis. Chem Biol Interact 178(1-3):16-23
Turunen O, et al.  (2009) In silico evidence for functional specialization after genome duplication in yeast. FEMS Yeast Res 9(1):16-31
Xie H, et al.  (2009) Characterization of protein impurities and site-specific modifications using peptide mapping with liquid chromatography and data independent acquisition mass spectrometry. Anal Chem 81(14):5699-708
Laadan B, et al.  (2008) Identification of an NADH-dependent 5-hydroxymethylfurfural-reducing alcohol dehydrogenase in Saccharomyces cerevisiae. Yeast 25(3):191-8
Men L and Wang Y  (2007) The oxidation of yeast alcohol dehydrogenase-1 by hydrogen peroxide in vitro. J Proteome Res 6(1):216-25
Qiu H and Wang Y  (2007) Probing adenosine nucleotide-binding proteins with an affinity-labeled nucleotide probe and mass spectrometry. Anal Chem 79(15):5547-56
Kenny DJ, et al.  (2006) A parallel approach to post source decay MALDI-TOF analysis. J Am Soc Mass Spectrom 17(1):60-6
Santra MK, et al.  (2006) Pyrene excimer fluorescence of yeast alcohol dehydrogenase: a sensitive probe to investigate ligand binding and unfolding pathway of the enzyme. Photochem Photobiol 82(2):480-6
Bhattacharyya J, et al.  (2003) A peptide sequence-YSGVCHTDLHAWHGDWPLPVK [40-60]-in yeast alcohol dehydrogenase prevents the aggregation of denatured substrate proteins. Biochem Biophys Res Commun 307(1):1-7
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
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
Leskovac V, et al.  (1998) Use of competitive dead-end inhibitors to determine the chemical mechanism of action of yeast alcohol dehydrogenase. Mol Cell Biochem 178(1-2):219-27
Green DW, et al.  (1993) Inversion of the substrate specificity of yeast alcohol dehydrogenase. J Biol Chem 268(11):7792-8
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
Ganzhorn AJ and Plapp BV  (1988) Carboxyl groups near the active site zinc contribute to catalysis in yeast alcohol dehydrogenase. J Biol Chem 263(11):5446-54
Ganzhorn AJ, et al.  (1987) Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity. J Biol Chem 262(8):3754-61
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
van Loon AP and Young ET  (1986) Intracellular sorting of alcohol dehydrogenase isoenzymes in yeast: a cytosolic location reflects absence of an amino-terminal targeting sequence for the mitochondrion. EMBO J 5(1):161-5
Jornvall H, et al.  (1984) Extensive variations and basic features in the alcohol dehydrogenase-sorbitol dehydrogenase family. Eur J Biochem 140(1):17-23
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
Jornvall H  (1977) The primary structure of yeast alcohol dehydrogenase. Eur J Biochem 72(3):425-42