Pyruvate phosphate dikinase: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Pyruvate phosphate dikinase, A Molecular Machine== | ==Pyruvate phosphate dikinase, A Molecular Machine== | ||
(this is a very preliminar page for [https://carb.umbi.umd.edu/herzberg/research Dr Osnat Herzberg]) | |||
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. | |||
<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> | ||
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. | You may also [https://carb.umbi.umd.edu/files/ppdk_release.mpg download] the full High Resolution video. | ||