Comparison of inactivation and unfolding of yeast alcohol dehydrogenase during denaturation in urea solutions.
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Summary
In this study, inactivation and unfolding of yeast alcohol dehydrogenase containing zinc ions in urea solutions of different concentrations are compared and the results show that much lower concentrations of urea are required to bring about inactivation than significant unfolding of the enzyme molecule.
- Type
- article
- Published
- 1996-08-01
- Cited by
- 15
- References
- 17
- OpenAlex
- https://openalex.org/W2011685374
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:22881789
Keywords
Chemistry, Alcohol dehydrogenase, Urea, Denaturation (fissile materials), Enzyme
References
- Importance of the structural zinc atom for the stability of yeast alcohol dehydrogenase.
- Protein denaturation.
- Conformational Changes at the Active Site of Creatine Kinase During Denaturation of Urea
- Yeast alcohol dehydrogenase: molecular weight, coenzyme binding, and reaction equilibria.
- Comparison of the activity and conformation changes of lactate dehydrogenase H4 during denaturation by guanidinium chloride.
- Fluorescence analysis of denaturation and reassembly of dansylated creatine kinase.
- Comparison of the rates of inactivation and conformational changes of creatine kinase during urea denaturation.
- Conformational and activity changes during guanidine denaturation of D-glyceraldehyde-3-phosphate dehydrogenase.
- Inactivation and unfolding of aminoacylase during denaturation in sodium dodecyl sulfate solutions
- Comparison of inactivation and conformational changes of aminoacylase during guanidinium chloride denaturation.
- Growth, isolation, and characterization of a yeast manganese alcohol dehydrogenase.
- Mercury-199 NMR of the metal receptor site in MerR and its protein-DNA complex.
- Location of the active sites of some enzymes in limited and flexible molecular regions
- The zinc content of yeast alcohol dehydrogenase.
- Pathways and mechanisms of protein folding.
- Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding.
- Conformational changes at the active site of creatine kinase at low concentrations of guanidinium chloride.
- 七星瓢虫脑咽侧体活化因子对咽侧体的活化作用
Cited by
- Multiple unfolded states of alcohol dehydrogenase I from Kluyveromyces lactis by guanidinium chloride.
- Cloning and expression of (R)-hydroxynitrile lyase from Linum usitatissimum (flax)
- Effect of Urea on Activity and Conformation of a Glycoprotein
- Effect of ethanol on the activity and conformation of Penaeus penicillatus acid phosphatase.
- Inhibition of alcohol dehydrogenase by bismuth
- Conformational changes and inactivation of calf intestinal alkaline phosphatase in trifluoroethanol solutions.
- Inhibition of a Zn(II)-containing enzyme, alcohol dehydrogenase, by anticancer antibiotics, mithramycin and chromomycin A3
- One stop mycology
- Pyrene Excimer Fluorescence of Yeast Alcohol Dehydrogenase: A Sensitive Probe to Investigate Ligand Binding and Unfolding Pathway of the Enzyme
- Slowed Diffusion and Excluded Volume Both Contribute to the Effects of Macromolecular Crowding on Alcohol Dehydrogenase Steady-State Kinetics.
- The Alcohol Dehydrogenase Kinetics Laboratory: Enhanced Data Analysis and Student-Designed Mini-Projects
- Microbiological Control and Mechanisms of Action of High Voltage Atmospheric Cold Plasma
- Chaperone activity of large-size subunit catalases.
- Protection of Alcohol Dehydrogenase against Freeze–Thaw Stress by Ice-Binding Proteins Is Proportional to Their Ice Recrystallization Inhibition Property
- One stop mycology
- Natural deep eutectic solvents as green and biocompatible reaction medium for carbonic anhydrase catalysis.
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