The Experts below are selected from a list of 207 Experts worldwide ranked by ideXlab platform
Yuru Zhang - One of the best experts on this subject based on the ideXlab platform.
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the Cytochrome B5 Reductase hpo 19 is required for biosynthesis of polyunsaturated fatty acids in caenorhabditis elegans
Biochimica et Biophysica Acta, 2016Co-Authors: Yuru Zhang, Haizhen Wang, Jingjing Zhang, Ying Hu, Linqiang Zhang, Xiaoyun WuAbstract:Abstract Polyunsaturated fatty acids (PUFAs) are fatty acids with backbones containing more than one double bond, which are introduced by a series of desaturases that insert double bonds at specific carbon atoms in the fatty acid chain. It has been established that desaturases need flavoprotein-NADH-dependent Cytochrome B5 Reductase (simplified as Cytochrome B5 Reductase) and Cytochrome B5 to pass through electrons for activation. However, it has remained unclear how this multi-enzyme system works for distinct desaturases. The model organism Caenorhabditis elegans contains seven desaturases (FAT-1, -2, -3, -4, -5, -6, -7) for the biosynthesis of PUFAS, providing an excellent model in which to characterize different desaturation reactions. Here, we show that RNAi inactivation of predicted Cytochrome B5 Reductases hpo-19 and T05H4.4 led to increased levels of C18:1n − 9 but decreased levels of PUFAs, small lipid droplets, decreased fat accumulation, reduced brood size and impaired development. Dietary supplementation with different fatty acids showed that HPO-19 and T05H4.4 likely affect the activity of FAT-1, FAT-2, FAT-3, and FAT-4 desaturases, suggesting that these four desaturases use the same Cytochrome B5 Reductase to function. Collectively, these findings indicate that Cytochrome B5 Reductase HPO-19/T05H4.4 is required for desaturation to biosynthesize PUFAs in C. elegans.
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the Cytochrome B5 Reductase hpo 19 is required for biosynthesis of polyunsaturated fatty acids in caenorhabditis elegans molecular and cell biology of lipids
Biochimica et Biophysica Acta, 2016Co-Authors: Yuru Zhang, Haizhen Wang, Jingjing Zhang, Ying Hu, Linqiang Zhang, Xiaoyun Wu, Xiong Su, Tingting Li, Bin LiangAbstract:Polyunsaturated fatty acids (PUFAs) are fatty acids with backbones containing more than one double bond, which are introduced by a series of desaturases that insert double bonds at specific carbon atoms in the fatty acid chain. It has been established that desaturases need flavoprotein-NADH-dependent Cytochrome B5 Reductase (simplified as Cytochrome B5 Reductase) and Cytochrome B5 to pass through electrons for activation. However, it has remained unclear how this multi-enzyme system works for distinct desaturases. The model organism Caenorhabditis elegans contains seven desaturases (FAT-1, -2, -3, -4, -5, -6, -7) for the biosynthesis of PUFAS, providing an excellent model in which to characterize different desaturation reactions. Here, we show that RNAi inactivation of predicted Cytochrome B5 Reductases hpo-19 and T05H4.4 led to increased levels of C18:1n−9 but decreased levels of PUFAs, small lipid droplets, decreased fat accumulation, reduced brood size and impaired development. Dietary supplementation with different fatty acids showed that HPO-19 and T05H4.4 likely affect the activity of FAT-1, FAT-2, FAT-3, and FAT-4 desaturases, suggesting that these four desaturases use the same Cytochrome B5 Reductase to function. Collectively, these findings indicate that Cytochrome B5 Reductase HPO-19/T05H4.4 is required for desaturation to biosynthesize PUFAs in C. elegans.
Steven L Kelly - One of the best experts on this subject based on the ideXlab platform.
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biodiversity of the p450 catalytic cycle yeast Cytochrome B5 nadh Cytochrome B5 Reductase complex efficiently drives the entire sterol 14 demethylation cyp51 reaction
FEBS Letters, 1999Co-Authors: David C Lamb, Diane E Kelly, N J Manning, Mustak A Kaderbhai, Steven L KellyAbstract:The widely accepted catalytic cycle of Cytochromes P450 (CYP) involves the electron transfer from NADPH Cytochrome P450 Reductase (CPR), with a potential for second electron donation from the microsomal Cytochrome B5/NADH Cytochrome B5 Reductase system. The latter system only supported CYP reactions inefficiently. Using purified proteins including Candida albicans CYP51 and yeast NADPH cyto- chrome P450 Reductase, Cytochrome B5 and NADH Cytochrome B5 Reductase, we show here that fungal CYP51 mediated sterol 14K-demethylation can be wholly and efficiently supported by the Cytochrome B5/NADH Cytochrome B5 Reductase electron trans- port system. This alternative catalytic cycle, where both the first and second electrons were donated via the NADH Cytochrome B5 electron transport system, can account for the continued ergosterol production seen in yeast strains containing a disrup- tion of the gene encoding CPR. z 1999 Federation of European Biochemical Societies.
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Biodiversity of the P450 catalytic cycle: yeast Cytochrome B5/NADH Cytochrome B5 Reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction.
FEBS Letters, 1999Co-Authors: David C Lamb, Diane E Kelly, N J Manning, Mustak A Kaderbhai, Steven L KellyAbstract:The widely accepted catalytic cycle of Cytochromes P450 (CYP) involves the electron transfer from NADPH Cytochrome P450 Reductase (CPR), with a potential for second electron donation from the microsomal Cytochrome B5/NADH Cytochrome B5 Reductase system. The latter system only supported CYP reactions inefficiently. Using purified proteins including Candida albicans CYP51 and yeast NADPH cyto- chrome P450 Reductase, Cytochrome B5 and NADH Cytochrome B5 Reductase, we show here that fungal CYP51 mediated sterol 14K-demethylation can be wholly and efficiently supported by the Cytochrome B5/NADH Cytochrome B5 Reductase electron trans- port system. This alternative catalytic cycle, where both the first and second electrons were donated via the NADH Cytochrome B5 electron transport system, can account for the continued ergosterol production seen in yeast strains containing a disrup- tion of the gene encoding CPR. z 1999 Federation of European Biochemical Societies.
Mark T Gladwin - One of the best experts on this subject based on the ideXlab platform.
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The Zebrafish Cytochrome B5/Cytochrome B5 Reductase/NADH System Efficiently Reduces Cytoglobins 1 and 2: Conserved Activity of Cytochrome B5/Cytochrome B5 Reductases during Vertebrate Evolution.
Biochemistry, 2019Co-Authors: Matthew B Amdahl, Elin E Petersen, K A Bocian, Stefan Kaliszuk, Anthony W Demartino, Sagarika Tiwari, Paola Corti, Jason J Rose, Courtney Sparacino-watkins, Mark T GladwinAbstract:: Cytoglobin is a heme protein evolutionarily related to hemoglobin and myoglobin. Cytoglobin is expressed ubiquitously in mammalian tissues; however, its physiological functions are yet unclear. Phylogenetic analyses indicate that the cytoglobin gene is highly conserved in vertebrate clades, from fish to reptiles, amphibians, birds, and mammals. Most proposed roles for cytoglobin require the maintenance of a pool of reduced cytoglobin (FeII). We have shown previously that the human Cytochrome B5/Cytochrome B5 Reductase system, considered a quintessential hemoglobin/myoglobin reductant, can reduce human and zebrafish cytoglobins ≤250-fold faster than human hemoglobin or myoglobin. It was unclear whether this reduction of zebrafish cytoglobins by mammalian proteins indicates a conserved pathway through vertebrate evolution. Here, we report the reduction of zebrafish cytoglobins 1 and 2 by the zebrafish Cytochrome B5 Reductase and the two zebrafish Cytochrome B5 isoforms. In addition, the reducing system also supports reduction of Globin X, a conserved globin in fish and amphibians. Indeed, the zebrafish reducing system can maintain a fully reduced pool for both cytoglobins, and both Cytochrome B5 isoforms can support this process. We determined the P50 for oxygen to be 0.5 Torr for cytoglobin 1 and 4.4 Torr for cytoglobin 2 at 25 °C. Thus, even at low oxygen tensions, the reduced cytoglobins may exist in a predominant oxygen-bound form. Under these conditions, the Cytochrome B5/Cytochrome B5 Reductase system can support a conserved role for cytoglobins through evolution, providing electrons for redox signaling reactions such as nitric oxide dioxygenation, nitrite reduction, and phospholipid oxidation.
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the zebrafish Cytochrome B5 Cytochrome B5 Reductase nadh system efficiently reduces cytoglobins 1 and 2 conserved activity of Cytochrome B5 Cytochrome B5 Reductases during vertebrate evolution
Biochemistry, 2019Co-Authors: Matthew B Amdahl, Courtney Sparacinowatkins, Elin E Petersen, K A Bocian, Stefan Kaliszuk, Anthony W Demartino, Sagarika Tiwari, Paola Corti, Jason J Rose, Mark T GladwinAbstract:: Cytoglobin is a heme protein evolutionarily related to hemoglobin and myoglobin. Cytoglobin is expressed ubiquitously in mammalian tissues; however, its physiological functions are yet unclear. Phylogenetic analyses indicate that the cytoglobin gene is highly conserved in vertebrate clades, from fish to reptiles, amphibians, birds, and mammals. Most proposed roles for cytoglobin require the maintenance of a pool of reduced cytoglobin (FeII). We have shown previously that the human Cytochrome B5/Cytochrome B5 Reductase system, considered a quintessential hemoglobin/myoglobin reductant, can reduce human and zebrafish cytoglobins ≤250-fold faster than human hemoglobin or myoglobin. It was unclear whether this reduction of zebrafish cytoglobins by mammalian proteins indicates a conserved pathway through vertebrate evolution. Here, we report the reduction of zebrafish cytoglobins 1 and 2 by the zebrafish Cytochrome B5 Reductase and the two zebrafish Cytochrome B5 isoforms. In addition, the reducing system also supports reduction of Globin X, a conserved globin in fish and amphibians. Indeed, the zebrafish reducing system can maintain a fully reduced pool for both cytoglobins, and both Cytochrome B5 isoforms can support this process. We determined the P50 for oxygen to be 0.5 Torr for cytoglobin 1 and 4.4 Torr for cytoglobin 2 at 25 °C. Thus, even at low oxygen tensions, the reduced cytoglobins may exist in a predominant oxygen-bound form. Under these conditions, the Cytochrome B5/Cytochrome B5 Reductase system can support a conserved role for cytoglobins through evolution, providing electrons for redox signaling reactions such as nitric oxide dioxygenation, nitrite reduction, and phospholipid oxidation.
Xiaoyun Wu - One of the best experts on this subject based on the ideXlab platform.
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the Cytochrome B5 Reductase hpo 19 is required for biosynthesis of polyunsaturated fatty acids in caenorhabditis elegans
Biochimica et Biophysica Acta, 2016Co-Authors: Yuru Zhang, Haizhen Wang, Jingjing Zhang, Ying Hu, Linqiang Zhang, Xiaoyun WuAbstract:Abstract Polyunsaturated fatty acids (PUFAs) are fatty acids with backbones containing more than one double bond, which are introduced by a series of desaturases that insert double bonds at specific carbon atoms in the fatty acid chain. It has been established that desaturases need flavoprotein-NADH-dependent Cytochrome B5 Reductase (simplified as Cytochrome B5 Reductase) and Cytochrome B5 to pass through electrons for activation. However, it has remained unclear how this multi-enzyme system works for distinct desaturases. The model organism Caenorhabditis elegans contains seven desaturases (FAT-1, -2, -3, -4, -5, -6, -7) for the biosynthesis of PUFAS, providing an excellent model in which to characterize different desaturation reactions. Here, we show that RNAi inactivation of predicted Cytochrome B5 Reductases hpo-19 and T05H4.4 led to increased levels of C18:1n − 9 but decreased levels of PUFAs, small lipid droplets, decreased fat accumulation, reduced brood size and impaired development. Dietary supplementation with different fatty acids showed that HPO-19 and T05H4.4 likely affect the activity of FAT-1, FAT-2, FAT-3, and FAT-4 desaturases, suggesting that these four desaturases use the same Cytochrome B5 Reductase to function. Collectively, these findings indicate that Cytochrome B5 Reductase HPO-19/T05H4.4 is required for desaturation to biosynthesize PUFAs in C. elegans.
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the Cytochrome B5 Reductase hpo 19 is required for biosynthesis of polyunsaturated fatty acids in caenorhabditis elegans molecular and cell biology of lipids
Biochimica et Biophysica Acta, 2016Co-Authors: Yuru Zhang, Haizhen Wang, Jingjing Zhang, Ying Hu, Linqiang Zhang, Xiaoyun Wu, Xiong Su, Tingting Li, Bin LiangAbstract:Polyunsaturated fatty acids (PUFAs) are fatty acids with backbones containing more than one double bond, which are introduced by a series of desaturases that insert double bonds at specific carbon atoms in the fatty acid chain. It has been established that desaturases need flavoprotein-NADH-dependent Cytochrome B5 Reductase (simplified as Cytochrome B5 Reductase) and Cytochrome B5 to pass through electrons for activation. However, it has remained unclear how this multi-enzyme system works for distinct desaturases. The model organism Caenorhabditis elegans contains seven desaturases (FAT-1, -2, -3, -4, -5, -6, -7) for the biosynthesis of PUFAS, providing an excellent model in which to characterize different desaturation reactions. Here, we show that RNAi inactivation of predicted Cytochrome B5 Reductases hpo-19 and T05H4.4 led to increased levels of C18:1n−9 but decreased levels of PUFAs, small lipid droplets, decreased fat accumulation, reduced brood size and impaired development. Dietary supplementation with different fatty acids showed that HPO-19 and T05H4.4 likely affect the activity of FAT-1, FAT-2, FAT-3, and FAT-4 desaturases, suggesting that these four desaturases use the same Cytochrome B5 Reductase to function. Collectively, these findings indicate that Cytochrome B5 Reductase HPO-19/T05H4.4 is required for desaturation to biosynthesize PUFAs in C. elegans.
Jingjing Zhang - One of the best experts on this subject based on the ideXlab platform.
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the Cytochrome B5 Reductase hpo 19 is required for biosynthesis of polyunsaturated fatty acids in caenorhabditis elegans
Biochimica et Biophysica Acta, 2016Co-Authors: Yuru Zhang, Haizhen Wang, Jingjing Zhang, Ying Hu, Linqiang Zhang, Xiaoyun WuAbstract:Abstract Polyunsaturated fatty acids (PUFAs) are fatty acids with backbones containing more than one double bond, which are introduced by a series of desaturases that insert double bonds at specific carbon atoms in the fatty acid chain. It has been established that desaturases need flavoprotein-NADH-dependent Cytochrome B5 Reductase (simplified as Cytochrome B5 Reductase) and Cytochrome B5 to pass through electrons for activation. However, it has remained unclear how this multi-enzyme system works for distinct desaturases. The model organism Caenorhabditis elegans contains seven desaturases (FAT-1, -2, -3, -4, -5, -6, -7) for the biosynthesis of PUFAS, providing an excellent model in which to characterize different desaturation reactions. Here, we show that RNAi inactivation of predicted Cytochrome B5 Reductases hpo-19 and T05H4.4 led to increased levels of C18:1n − 9 but decreased levels of PUFAs, small lipid droplets, decreased fat accumulation, reduced brood size and impaired development. Dietary supplementation with different fatty acids showed that HPO-19 and T05H4.4 likely affect the activity of FAT-1, FAT-2, FAT-3, and FAT-4 desaturases, suggesting that these four desaturases use the same Cytochrome B5 Reductase to function. Collectively, these findings indicate that Cytochrome B5 Reductase HPO-19/T05H4.4 is required for desaturation to biosynthesize PUFAs in C. elegans.
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the Cytochrome B5 Reductase hpo 19 is required for biosynthesis of polyunsaturated fatty acids in caenorhabditis elegans molecular and cell biology of lipids
Biochimica et Biophysica Acta, 2016Co-Authors: Yuru Zhang, Haizhen Wang, Jingjing Zhang, Ying Hu, Linqiang Zhang, Xiaoyun Wu, Xiong Su, Tingting Li, Bin LiangAbstract:Polyunsaturated fatty acids (PUFAs) are fatty acids with backbones containing more than one double bond, which are introduced by a series of desaturases that insert double bonds at specific carbon atoms in the fatty acid chain. It has been established that desaturases need flavoprotein-NADH-dependent Cytochrome B5 Reductase (simplified as Cytochrome B5 Reductase) and Cytochrome B5 to pass through electrons for activation. However, it has remained unclear how this multi-enzyme system works for distinct desaturases. The model organism Caenorhabditis elegans contains seven desaturases (FAT-1, -2, -3, -4, -5, -6, -7) for the biosynthesis of PUFAS, providing an excellent model in which to characterize different desaturation reactions. Here, we show that RNAi inactivation of predicted Cytochrome B5 Reductases hpo-19 and T05H4.4 led to increased levels of C18:1n−9 but decreased levels of PUFAs, small lipid droplets, decreased fat accumulation, reduced brood size and impaired development. Dietary supplementation with different fatty acids showed that HPO-19 and T05H4.4 likely affect the activity of FAT-1, FAT-2, FAT-3, and FAT-4 desaturases, suggesting that these four desaturases use the same Cytochrome B5 Reductase to function. Collectively, these findings indicate that Cytochrome B5 Reductase HPO-19/T05H4.4 is required for desaturation to biosynthesize PUFAs in C. elegans.
