The conformational change of rabbit muscle pyruvate kinase induced by activating cations and its substrates.
Catalysis by rabbit muscle pyruvate kinase involves domain movements and conformational changes induced by activating cations and its substrates. Fluorescence acrylamide quenching analyses reveal that interactions with Mg(2+) and K(+) lead to a more exposed active site of PK while interactions with PEP and ADP decrease solvent accessibility of the active site.
Ou
Yan
Y
Department of Chemistry, Fudan University, Shanghai 200433, China.
Tao
Wenbing
W
Zhang
Yun
Y
Wu
Guangrong
G
Yu
Shaoning
S
D000818:Animals; D002412:Cations / Q000494:pharmacology; D002942:Circular Dichroism; D004789:Enzyme Activation / Q000187:drug effects; D004791:Enzyme Inhibitors / Q000494:pharmacology; D008958:Models, Molecular; D009132:Muscles / Q000201:enzymology*; D011487:Protein Conformation / Q000187:drug effects; D011489:Protein Denaturation / Q000187:drug effects; D011770:Pyruvate Kinase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D011817:Rabbits; D012997:Solvents / Q000737:chemistry; D013050:Spectrometry, Fluorescence; D013696:Temperature; D014364:Tryptophan
D002412:Cations; D004791:Enzyme Inhibitors; D012997:Solvents; D014364:Tryptophan; D011770:Pyruvate Kinase