Difference between revisions of "YIL107C"
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| − | '''Description of YIL107C:''' 6-phosphofructo-2-kinase, inhibited by phosphoenolpyruvate and sn-glycerol 3-phosphate; has negligible fructose-2,6-bisphosphatase activity; transcriptional regulation involves protein kinase A<ref name='S000054923'>Goncalves PM, et al. (1997) Signalling pathways leading to transcriptional regulation of genes involved in the activation of glycolysis in yeast. Mol Microbiol 25(3):483-93 {{SGDpaper|S000054923}} PMID 9302011</ref><ref name='S000055185'>Kretschmer M, et al. (1993) Mutation of monofunctional 6-phosphofructo-2-kinase in yeast to bifunctional 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase. Biochemistry 32(41):11143-8 {{SGDpaper|S000055185}} PMID 8218176 | + | '''Description of YIL107C:''' 6-phosphofructo-2-kinase, inhibited by phosphoenolpyruvate and sn-glycerol 3-phosphate; has negligible fructose-2,6-bisphosphatase activity; transcriptional regulation involves protein kinase A<ref name='S000076089'>Bedri A, et al. (1989) Kinetics of 6-phosphofructo-2-kinase from Saccharomyces cerevisiae: inhibition of the enzyme by ATP. Biomed Biochim Acta 48(7):403-11 {{SGDpaper|S000076089}} PMID 2529854</ref><ref name='S000054923'>Goncalves PM, et al. (1997) Signalling pathways leading to transcriptional regulation of genes involved in the activation of glycolysis in yeast. Mol Microbiol 25(3):483-93 {{SGDpaper|S000054923}} PMID 9302011</ref><ref name='S000055185'>Kretschmer M, et al. (1993) Mutation of monofunctional 6-phosphofructo-2-kinase in yeast to bifunctional 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase. Biochemistry 32(41):11143-8 |
| − | + | {{SGDpaper|S000055185}} PMID 8218176</ref> | |
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Revision as of 13:05, 25 February 2010
Share your knowledge...Edit this entry! <protect>
| Systematic name | YIL107C |
| Gene name | PFK26 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr IX:165758..163275 |
| Primary SGDID | S000001369 |
Description of YIL107C: 6-phosphofructo-2-kinase, inhibited by phosphoenolpyruvate and sn-glycerol 3-phosphate; has negligible fructose-2,6-bisphosphatase activity; transcriptional regulation involves protein kinase A[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]
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References
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- ↑ Bedri A, et al. (1989) Kinetics of 6-phosphofructo-2-kinase from Saccharomyces cerevisiae: inhibition of the enzyme by ATP. Biomed Biochim Acta 48(7):403-11 SGD PMID 2529854
- ↑ Goncalves PM, et al. (1997) Signalling pathways leading to transcriptional regulation of genes involved in the activation of glycolysis in yeast. Mol Microbiol 25(3):483-93 SGD PMID 9302011
- ↑ Kretschmer M, et al. (1993) Mutation of monofunctional 6-phosphofructo-2-kinase in yeast to bifunctional 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase. Biochemistry 32(41):11143-8 SGD PMID 8218176
- ↑ 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
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