Difference between revisions of "YMR303C"
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| − | '''Description of YMR303C:''' Glucose-repressible alcohol dehydrogenase II, catalyzes the conversion of ethanol to acetaldehyde; involved in the production of certain carboxylate esters; regulated by ADR1 | + | '''Description of YMR303C:''' Glucose-repressible alcohol dehydrogenase II, catalyzes the conversion of ethanol to acetaldehyde; involved in the production of certain carboxylate esters; regulated by ADR1<ref name='S000057237'>Bennetzen JL and Hall BD (1982) The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase. J Biol Chem 257(6):3018-25 {{SGDpaper|S000057237}} PMID 6277922</ref><ref name='S000072614'>Dickinson JR, et al. (2003) The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae. J Biol Chem 278(10):8028-34 {{SGDpaper|S000072614}} PMID 12499363</ref><ref name='S000050567'>Young ET and Pilgrim D (1985) Isolation and DNA sequence of ADH3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae. Mol Cell Biol 5(11):3024-34 |
| − | {{SGDpaper| | + | {{SGDpaper|S000050567}} PMID 2943982</ref> |
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Revision as of 13:05, 25 February 2010
Share your knowledge...Edit this entry! <protect>
| Systematic name | YMR303C |
| Gene name | ADH2 |
| Aliases | ADR2 |
| Feature type | ORF, Verified |
| Coordinates | Chr XIII:874336..873290 |
| Primary SGDID | S000004918 |
Description of YMR303C: Glucose-repressible alcohol dehydrogenase II, catalyzes the conversion of ethanol to acetaldehyde; involved in the production of certain carboxylate esters; regulated by ADR1[1][2][3]
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Contents
Community Commentary
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DNA and RNA Details
Other DNA and RNA Details
Other Topic: expression
Specifically higher expression in carbon limited chemostat cultures versus carbon excess. [4] [5]
Protein Details
Other Protein Details
Other Topic: Regulated by the diauxic shift (glycerol)
Apart from the overall increase in mitochondrial protein mass this protein is induced after the diauxic shift. [6] [7]
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References
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- ↑ Bennetzen JL and Hall BD (1982) The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase. J Biol Chem 257(6):3018-25 SGD PMID 6277922
- ↑ Dickinson JR, et al. (2003) The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae. J Biol Chem 278(10):8028-34 SGD PMID 12499363
- ↑ Young ET and Pilgrim D (1985) Isolation and DNA sequence of ADH3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae. Mol Cell Biol 5(11):3024-34 SGD PMID 2943982
- ↑ Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. J Biol Chem 278(5):3265-74 SGD PMID 12414795
- ↑ submitted by Viktor Boer on 2003-07-25
- ↑ Ohlmeier S, et al. (2004) The yeast mitochondrial proteome, a study of fermentative and respiratory growth. J Biol Chem 279(6):3956-79 SGD PMID 14597615
- ↑ submitted by Steffen Ohlmeier on 2004-04-08
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