title: The conformational change of rabbit muscle pyruvate kinase induced by activating cations and its substrates.
abstract: 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.
authors.affiliation: Department of Chemistry, Fudan University, Shanghai 200433, China.
authors.forename: Yan
authors.initials: Y
authors.lastname: Ou
authors.forename: Wenbing
authors.initials: W
authors.lastname: Tao
authors.forename: Yun
authors.initials: Y
authors.lastname: Zhang
authors.forename: Guangrong
authors.initials: G
authors.lastname: Wu
authors.forename: Shaoning
authors.initials: S
authors.lastname: Yu
mesh_terms: 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
chemical_list: D002412:Cations; D004791:Enzyme Inhibitors; D012997:Solvents; D014364:Tryptophan; D011770:Pyruvate Kinase