Sandbox 177
From Proteopedia
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==General Information== | ==General Information== | ||
| - | NADPH-cytochrome P450 oxidoreductase (CYPOR) is a ~78kDa, multidomain flavoprotein (5). Containing three co-factors, FMN, FAD and NADPH, CYPOR is the archetype for the mammalian diflavin-containing enzyme family (5). | + | NADPH-cytochrome P450 oxidoreductase (CYPOR) is a ~78kDa, multidomain flavoprotein (5). Containing three co-factors, FMN, FAD and NADPH, CYPOR is the archetype for the mammalian diflavin-containing enzyme family (5). |
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Horecker first identified this protein in 1950 as NADPH-specific cytochrome c reductase, based on his assumption that it was the redox partner for cytochrome c, found in the mitochondria (1). However, studies in the 1960s and later showed that its main function is actually as the redox partner for cytochrome P450 in microsomal electron transport chains, thus the name change (4,5). | Horecker first identified this protein in 1950 as NADPH-specific cytochrome c reductase, based on his assumption that it was the redox partner for cytochrome c, found in the mitochondria (1). However, studies in the 1960s and later showed that its main function is actually as the redox partner for cytochrome P450 in microsomal electron transport chains, thus the name change (4,5). | ||
| - | Regulation of this protein is largely at the transcriptional level and appears to involve the thyroid hormone T3 in most cases (3). Adrenocorticotrophic hormone acts as a regulator in a few specific cases (3). | + | |
| + | Regulation of this protein, which is found all tissues to some extent, is largely at the transcriptional level and appears to involve the thyroid hormone T3 in most cases (3). Adrenocorticotrophic hormone acts as a regulator in a few specific cases (3). | ||
Revision as of 21:56, 25 March 2010
NADPH-cytochrome P450 oxidoreductase
Taya O'Neill
|
General Information
NADPH-cytochrome P450 oxidoreductase (CYPOR) is a ~78kDa, multidomain flavoprotein (5). Containing three co-factors, FMN, FAD and NADPH, CYPOR is the archetype for the mammalian diflavin-containing enzyme family (5).
Horecker first identified this protein in 1950 as NADPH-specific cytochrome c reductase, based on his assumption that it was the redox partner for cytochrome c, found in the mitochondria (1). However, studies in the 1960s and later showed that its main function is actually as the redox partner for cytochrome P450 in microsomal electron transport chains, thus the name change (4,5).
Regulation of this protein, which is found all tissues to some extent, is largely at the transcriptional level and appears to involve the thyroid hormone T3 in most cases (3). Adrenocorticotrophic hormone acts as a regulator in a few specific cases (3).
| Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. Andrea Gorrell. |
