Pyruvate phosphate dikinase
From Proteopedia
| Line 4: | Line 4: | ||
{| | {| | ||
| - | | <swf width="300" height="300">https://carb.umbi.umd.edu/system/files/ppdk_release.swf</swf> | + | | <swf width="300" height="300">https://carb.umbi.umd.edu/system/files/ppdk_release.swf</swf><br> |
| + | You may also [https://carb.umbi.umd.edu/files/ppdk_release.mpg download] the full High Resolution video. | ||
| | | | ||
Two PEP-utilizing enzymes function in vastly different biological contexts, yet both catalyze phosphoryl group transfer by shuttling a phosphohistidine residue between remote active centers. These enzymes utilize a swivel domain mechanism to deliver the phosphoryl group to the appropriate substrate. | Two PEP-utilizing enzymes function in vastly different biological contexts, yet both catalyze phosphoryl group transfer by shuttling a phosphohistidine residue between remote active centers. These enzymes utilize a swivel domain mechanism to deliver the phosphoryl group to the appropriate substrate. | ||
| Line 10: | Line 11: | ||
Pyruvate phosphate dikinase (PPDK), catalyzes the interconversion of PEP, AMP and PPi to pyruvate, ATP and Pi. The PEP/pyruvate bind in a site remotely located from the nucleotide and phosphate binding site. Enzyme I of the bacterial PEP:sugar phosphotransferase system (PTS), transfers the phosphoryl group of PEP to the next PTS protein, HPr. HPr~P then proceeds to phosphorylate a sugar specific permease responsible for the uptake of the incoming sugar. Again, PEP and HPR bind remotely from one another. | Pyruvate phosphate dikinase (PPDK), catalyzes the interconversion of PEP, AMP and PPi to pyruvate, ATP and Pi. The PEP/pyruvate bind in a site remotely located from the nucleotide and phosphate binding site. Enzyme I of the bacterial PEP:sugar phosphotransferase system (PTS), transfers the phosphoryl group of PEP to the next PTS protein, HPr. HPr~P then proceeds to phosphorylate a sugar specific permease responsible for the uptake of the incoming sugar. Again, PEP and HPR bind remotely from one another. | ||
|} | |} | ||
| - | |||
| - | |||
| - | |||
| - | You may also [https://carb.umbi.umd.edu/files/ppdk_release.mpg download] the full High Resolution video. | ||
Revision as of 09:45, 15 July 2008
Pyruvate phosphate dikinase, A Molecular Machine
(this is a very preliminar page for Dr Osnat Herzberg)
| <swf width="300" height="300">https://carb.umbi.umd.edu/system/files/ppdk_release.swf</swf> You may also download the full High Resolution video. |
Two PEP-utilizing enzymes function in vastly different biological contexts, yet both catalyze phosphoryl group transfer by shuttling a phosphohistidine residue between remote active centers. These enzymes utilize a swivel domain mechanism to deliver the phosphoryl group to the appropriate substrate. Pyruvate phosphate dikinase (PPDK), catalyzes the interconversion of PEP, AMP and PPi to pyruvate, ATP and Pi. The PEP/pyruvate bind in a site remotely located from the nucleotide and phosphate binding site. Enzyme I of the bacterial PEP:sugar phosphotransferase system (PTS), transfers the phosphoryl group of PEP to the next PTS protein, HPr. HPr~P then proceeds to phosphorylate a sugar specific permease responsible for the uptake of the incoming sugar. Again, PEP and HPR bind remotely from one another. |
Proteopedia Page Contributors and Editors (what is this?)
Joel L. Sussman, Osnat Herzberg, Michal Harel, Jaime Prilusky, Alexander Berchansky, Dan Bolser, Karl Oberholser, David Canner, Eran Hodis
