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Phanelie Percheletuvee - One of the best experts on this subject based on the ideXlab platform.
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4 demethylwyosine synthase from pyrococcus abyssi is a radical s adenosyl l methionine enzyme with an additional 4fe 4s 2 cluster that interacts with the pyruvate co substrate
Journal of Biological Chemistry, 2012Co-Authors: Phanelie Percheletuvee, Velavan Kathirvelu, Gustav Berggren, Martin Clemancey, Jeanmarc Latour, Vincent Maurel, Thierry Douki, Jean Armengaud, Etienne MulliezAbstract:Wybutosine and its derivatives are found in position 37 of tRNA encoding Phe in eukaryotes and archaea. They are believed to play a key role in the Decoding Function of the ribosome. The second ste ...
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4 demethylwyosine synthase from pyrococcus abyssi is a radical sam enzyme with an additional 4fe 4s 2 cluster which interacts with the pyruvate co substrate
Journal of Biological Chemistry, 2012Co-Authors: Phanelie Percheletuvee, Velavan Kathirvelu, Gustav Berggren, Martin Clemancey, Jeanmarc Latour, Vincent Maurel, Thierry Douki, Jean Armengaud, Etienne Mulliez, Marc FontecaveAbstract:Abstract Wybutosine (yW) and its derivatives are found in position 37 of tRNA encoding Phe in eukaryotes and archaea. They are believed to play a key role in the Decoding Function of the ribosome. The second step in the biosynthesis of yW is catalyzed by TYW1 protein which is a member of the well-established class of metalloenzymes called Radical-SAM. These enzymes use a [4Fe-4S] cluster, chelated by three cysteines in a CysX3CysX2Cys motif, and S-Adenosyl-L-Methionine (SAM) to generate a 5-deoxyadenosyl radical that initiates various chemically challenging reactions. Sequence analysis of TYW1 proteins revealed, in the N-terminal half of the enzyme, beside the Radical-SAM cysteine triad an additional highly conserved cysteine motif. In this study we show by combining analytical and spectroscopic methods including UV-visible absorption, Mossbauer, EPR and HYSCORE spectroscopies that these additional cysteines are involved in the coordination of a second [4Fe-4S] cluster displaying a free coordination site able to bind pyruvate, the second substrate of the reaction. The presence of two distinct iron-sulfur clusters on TYW1 is reminiscent of MiaB, another tRNA-modifying metalloenzyme whose active form was shown to bind two iron-sulfur clusters. A possible role for the second [4Fe-4S] cluster in the enzyme activity is discussed
Etienne Mulliez - One of the best experts on this subject based on the ideXlab platform.
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4 demethylwyosine synthase from pyrococcus abyssi is a radical s adenosyl l methionine enzyme with an additional 4fe 4s 2 cluster that interacts with the pyruvate co substrate
Journal of Biological Chemistry, 2012Co-Authors: Phanelie Percheletuvee, Velavan Kathirvelu, Gustav Berggren, Martin Clemancey, Jeanmarc Latour, Vincent Maurel, Thierry Douki, Jean Armengaud, Etienne MulliezAbstract:Wybutosine and its derivatives are found in position 37 of tRNA encoding Phe in eukaryotes and archaea. They are believed to play a key role in the Decoding Function of the ribosome. The second ste ...
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4 demethylwyosine synthase from pyrococcus abyssi is a radical sam enzyme with an additional 4fe 4s 2 cluster which interacts with the pyruvate co substrate
Journal of Biological Chemistry, 2012Co-Authors: Phanelie Percheletuvee, Velavan Kathirvelu, Gustav Berggren, Martin Clemancey, Jeanmarc Latour, Vincent Maurel, Thierry Douki, Jean Armengaud, Etienne Mulliez, Marc FontecaveAbstract:Abstract Wybutosine (yW) and its derivatives are found in position 37 of tRNA encoding Phe in eukaryotes and archaea. They are believed to play a key role in the Decoding Function of the ribosome. The second step in the biosynthesis of yW is catalyzed by TYW1 protein which is a member of the well-established class of metalloenzymes called Radical-SAM. These enzymes use a [4Fe-4S] cluster, chelated by three cysteines in a CysX3CysX2Cys motif, and S-Adenosyl-L-Methionine (SAM) to generate a 5-deoxyadenosyl radical that initiates various chemically challenging reactions. Sequence analysis of TYW1 proteins revealed, in the N-terminal half of the enzyme, beside the Radical-SAM cysteine triad an additional highly conserved cysteine motif. In this study we show by combining analytical and spectroscopic methods including UV-visible absorption, Mossbauer, EPR and HYSCORE spectroscopies that these additional cysteines are involved in the coordination of a second [4Fe-4S] cluster displaying a free coordination site able to bind pyruvate, the second substrate of the reaction. The presence of two distinct iron-sulfur clusters on TYW1 is reminiscent of MiaB, another tRNA-modifying metalloenzyme whose active form was shown to bind two iron-sulfur clusters. A possible role for the second [4Fe-4S] cluster in the enzyme activity is discussed
Velavan Kathirvelu - One of the best experts on this subject based on the ideXlab platform.
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4 demethylwyosine synthase from pyrococcus abyssi is a radical s adenosyl l methionine enzyme with an additional 4fe 4s 2 cluster that interacts with the pyruvate co substrate
Journal of Biological Chemistry, 2012Co-Authors: Phanelie Percheletuvee, Velavan Kathirvelu, Gustav Berggren, Martin Clemancey, Jeanmarc Latour, Vincent Maurel, Thierry Douki, Jean Armengaud, Etienne MulliezAbstract:Wybutosine and its derivatives are found in position 37 of tRNA encoding Phe in eukaryotes and archaea. They are believed to play a key role in the Decoding Function of the ribosome. The second ste ...
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4 demethylwyosine synthase from pyrococcus abyssi is a radical sam enzyme with an additional 4fe 4s 2 cluster which interacts with the pyruvate co substrate
Journal of Biological Chemistry, 2012Co-Authors: Phanelie Percheletuvee, Velavan Kathirvelu, Gustav Berggren, Martin Clemancey, Jeanmarc Latour, Vincent Maurel, Thierry Douki, Jean Armengaud, Etienne Mulliez, Marc FontecaveAbstract:Abstract Wybutosine (yW) and its derivatives are found in position 37 of tRNA encoding Phe in eukaryotes and archaea. They are believed to play a key role in the Decoding Function of the ribosome. The second step in the biosynthesis of yW is catalyzed by TYW1 protein which is a member of the well-established class of metalloenzymes called Radical-SAM. These enzymes use a [4Fe-4S] cluster, chelated by three cysteines in a CysX3CysX2Cys motif, and S-Adenosyl-L-Methionine (SAM) to generate a 5-deoxyadenosyl radical that initiates various chemically challenging reactions. Sequence analysis of TYW1 proteins revealed, in the N-terminal half of the enzyme, beside the Radical-SAM cysteine triad an additional highly conserved cysteine motif. In this study we show by combining analytical and spectroscopic methods including UV-visible absorption, Mossbauer, EPR and HYSCORE spectroscopies that these additional cysteines are involved in the coordination of a second [4Fe-4S] cluster displaying a free coordination site able to bind pyruvate, the second substrate of the reaction. The presence of two distinct iron-sulfur clusters on TYW1 is reminiscent of MiaB, another tRNA-modifying metalloenzyme whose active form was shown to bind two iron-sulfur clusters. A possible role for the second [4Fe-4S] cluster in the enzyme activity is discussed
Marc Fontecave - One of the best experts on this subject based on the ideXlab platform.
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4 demethylwyosine synthase from pyrococcus abyssi is a radical sam enzyme with an additional 4fe 4s 2 cluster which interacts with the pyruvate co substrate
Journal of Biological Chemistry, 2012Co-Authors: Phanelie Percheletuvee, Velavan Kathirvelu, Gustav Berggren, Martin Clemancey, Jeanmarc Latour, Vincent Maurel, Thierry Douki, Jean Armengaud, Etienne Mulliez, Marc FontecaveAbstract:Abstract Wybutosine (yW) and its derivatives are found in position 37 of tRNA encoding Phe in eukaryotes and archaea. They are believed to play a key role in the Decoding Function of the ribosome. The second step in the biosynthesis of yW is catalyzed by TYW1 protein which is a member of the well-established class of metalloenzymes called Radical-SAM. These enzymes use a [4Fe-4S] cluster, chelated by three cysteines in a CysX3CysX2Cys motif, and S-Adenosyl-L-Methionine (SAM) to generate a 5-deoxyadenosyl radical that initiates various chemically challenging reactions. Sequence analysis of TYW1 proteins revealed, in the N-terminal half of the enzyme, beside the Radical-SAM cysteine triad an additional highly conserved cysteine motif. In this study we show by combining analytical and spectroscopic methods including UV-visible absorption, Mossbauer, EPR and HYSCORE spectroscopies that these additional cysteines are involved in the coordination of a second [4Fe-4S] cluster displaying a free coordination site able to bind pyruvate, the second substrate of the reaction. The presence of two distinct iron-sulfur clusters on TYW1 is reminiscent of MiaB, another tRNA-modifying metalloenzyme whose active form was shown to bind two iron-sulfur clusters. A possible role for the second [4Fe-4S] cluster in the enzyme activity is discussed
Jean Armengaud - One of the best experts on this subject based on the ideXlab platform.
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4 demethylwyosine synthase from pyrococcus abyssi is a radical s adenosyl l methionine enzyme with an additional 4fe 4s 2 cluster that interacts with the pyruvate co substrate
Journal of Biological Chemistry, 2012Co-Authors: Phanelie Percheletuvee, Velavan Kathirvelu, Gustav Berggren, Martin Clemancey, Jeanmarc Latour, Vincent Maurel, Thierry Douki, Jean Armengaud, Etienne MulliezAbstract:Wybutosine and its derivatives are found in position 37 of tRNA encoding Phe in eukaryotes and archaea. They are believed to play a key role in the Decoding Function of the ribosome. The second ste ...
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4 demethylwyosine synthase from pyrococcus abyssi is a radical sam enzyme with an additional 4fe 4s 2 cluster which interacts with the pyruvate co substrate
Journal of Biological Chemistry, 2012Co-Authors: Phanelie Percheletuvee, Velavan Kathirvelu, Gustav Berggren, Martin Clemancey, Jeanmarc Latour, Vincent Maurel, Thierry Douki, Jean Armengaud, Etienne Mulliez, Marc FontecaveAbstract:Abstract Wybutosine (yW) and its derivatives are found in position 37 of tRNA encoding Phe in eukaryotes and archaea. They are believed to play a key role in the Decoding Function of the ribosome. The second step in the biosynthesis of yW is catalyzed by TYW1 protein which is a member of the well-established class of metalloenzymes called Radical-SAM. These enzymes use a [4Fe-4S] cluster, chelated by three cysteines in a CysX3CysX2Cys motif, and S-Adenosyl-L-Methionine (SAM) to generate a 5-deoxyadenosyl radical that initiates various chemically challenging reactions. Sequence analysis of TYW1 proteins revealed, in the N-terminal half of the enzyme, beside the Radical-SAM cysteine triad an additional highly conserved cysteine motif. In this study we show by combining analytical and spectroscopic methods including UV-visible absorption, Mossbauer, EPR and HYSCORE spectroscopies that these additional cysteines are involved in the coordination of a second [4Fe-4S] cluster displaying a free coordination site able to bind pyruvate, the second substrate of the reaction. The presence of two distinct iron-sulfur clusters on TYW1 is reminiscent of MiaB, another tRNA-modifying metalloenzyme whose active form was shown to bind two iron-sulfur clusters. A possible role for the second [4Fe-4S] cluster in the enzyme activity is discussed
