Difference between revisions of "YMR145C"
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| − | '''Description of YMR145C:''' Mitochondrial external NADH dehydrogenase, catalyzes the oxidation of cytosolic NADH; Nde1p and Nde2p | + | '''Description of YMR145C:''' Mitochondrial external NADH dehydrogenase, a type II NAD(P)H:quinone oxidoreductase that catalyzes the oxidation of cytosolic NADH; Nde1p and Nde2p provide cytosolic NADH to the mitochondrial respiratory chain<ref name='S000079980'>Melo AM, et al. (2004) New insights into type II NAD(P)H:quinone oxidoreductases. Microbiol Mol Biol Rev 68(4):603-16 {{SGDpaper|S000079980}} PMID 15590775</ref><ref name='S000070271'>Pahlman IL, et al. (2002) Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. J Biol Chem 277(31):27991-5 {{SGDpaper|S000070271}} PMID 12032156</ref><ref name='S000042730'>Small WC and McAlister-Henn L (1998) Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae. J Bacteriol 180(16):4051-5 {{SGDpaper|S000042730}} PMID 9696750</ref><ref name='S000040550'>Luttik MA, et al. (1998) The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH. J Biol Chem 273(38):24529-34 {{SGDpaper|S000040550}} PMID 9733747</ref><ref name='S000039774'>Overkamp KM, et al. (2000) In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria. J Bacteriol 182(10):2823-30 |
{{SGDpaper|S000039774}} PMID 10781551</ref> | {{SGDpaper|S000039774}} PMID 10781551</ref> | ||
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Revision as of 06:21, 26 February 2009
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| Systematic name | YMR145C |
| Gene name | NDE1 |
| Aliases | NDH1 |
| Feature type | ORF, Verified |
| Coordinates | Chr XIII:556474..554792 |
| Primary SGDID | S000004753 |
Description of YMR145C: Mitochondrial external NADH dehydrogenase, a type II NAD(P)H:quinone oxidoreductase that catalyzes the oxidation of cytosolic NADH; Nde1p and Nde2p provide cytosolic NADH to the mitochondrial respiratory chain[1][2][3][4][5]
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Protein Details
Other Protein Details
Other Topic: Regulated by the diauxic shift (glycerol)
Apart form the overall increase in mitochondrial protein mass after the diauxic shift this protein remains unchanged after the diauxic shift. [6] [7]
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References
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- ↑ Melo AM, et al. (2004) New insights into type II NAD(P)H:quinone oxidoreductases. Microbiol Mol Biol Rev 68(4):603-16 SGD PMID 15590775
- ↑ Pahlman IL, et al. (2002) Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. J Biol Chem 277(31):27991-5 SGD PMID 12032156
- ↑ Small WC and McAlister-Henn L (1998) Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae. J Bacteriol 180(16):4051-5 SGD PMID 9696750
- ↑ Luttik MA, et al. (1998) The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH. J Biol Chem 273(38):24529-34 SGD PMID 9733747
- ↑ Overkamp KM, et al. (2000) In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria. J Bacteriol 182(10):2823-30 SGD PMID 10781551
- ↑ 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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