Other names published for SFA1: ADH5, bifunctional alcohol dehydrogenase/S-(hydroxymethyl)glutathione dehydrogenase, YDL168W
SFA1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
SFA1 - Protein Physical Properties (13)
| Reference | Other Genes Addressed |
|---|---|
| Kondo T, et al. (2012) Genetic engineering to enhance the Ehrlich pathway and alter carbon flux for increased isobutanol production from glucose by Saccharomyces cerevisiae. J Biotechnol 159(1-2):32-7 | |
| Canelas AB, et al. (2011) An in vivo data-driven framework for classification and quantification of enzyme kinetics and determination of apparent thermodynamic data. Metab Eng 13(3):294-306 | |
| van Eunen K, et al. (2010) Measuring enzyme activities under standardized in vivo-like conditions for systems biology. FEBS J 277(3):749-60 | |
| Tong L, et al. (2009) Hydrolase regulates NAD+ metabolites and modulates cellular redox. J Biol Chem 284(17):11256-66 | |
| van Eunen K, et al. (2009) Time-dependent regulation analysis dissects shifts between metabolic and gene-expression regulation during nitrogen starvation in baker's yeast. FEBS J 276(19):5521-36 | |
| van den Brink J, et al. (2008) Dynamics of glycolytic regulation during adaptation of Saccharomyces cerevisiae to fermentative metabolism. Appl Environ Microbiol 74(18):5710-23 | |
| Hassler BL and Worden RM (2006) Versatile bioelectronic interfaces based on heterotrifunctional linking molecules. Biosens Bioelectron 21(11):2146-54 | |
| Petersson A, et al. (2006) A 5-hydroxymethyl furfural reducing enzyme encoded by the Saccharomyces cerevisiae ADH6 gene conveys HMF tolerance. Yeast 23(6):455-64 | |
| Park H, et al. (2005) Effects of pressure on deuterium isotope effects of yeast alcohol dehydrogenase using alternative substrates. Arch Biochem Biophys 433(1):335-40 | |
| Fernandez MR, et al. (1999) A double residue substitution in the coenzyme-binding site accounts for the different kinetic properties between yeast and human formaldehyde dehydrogenases. J Biol Chem 274(53):37869-75 | |
| 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 | |
| Fernandez MR, et al. (1995) Class III alcohol dehydrogenase from Saccharomyces cerevisiae: structural and enzymatic features differ toward the human/mammalian forms in a manner consistent with functional needs in formaldehyde detoxication. FEBS Lett 370(1-2):23-6 | |
| Jones RC and Hough JS (1970) The effect of temperature on the metabolism of baker's yeast growing on continuous culture. J Gen Microbiol 60(1):107-16 |



