Enzyme dynamics during catalysis.
Internal protein dynamics are intimately connected to enzymatic catalysis. However, enzyme motions linked to substrate turnover remain largely unknown. We have studied dynamics of an enzyme during catalysis at atomic resolution using nuclear magnetic resonance relaxation methods. During catalytic action of the enzyme cyclophilin A, we detect conformational fluctuations of the active site that occur on a time scale of hundreds of microseconds. The rates of conformational dynamics of the enzyme strongly correlate with the microscopic rates of substrate turnover. The present results, together with available structural data, allow a prediction of the reaction trajectory.
Eisenmesser
Elan Zohar
EZ
Department of Biochemistry, Brandeis University, Waltham, MA 02454, USA.
Bosco
Daryl A
DA
Akke
Mikael
M
Kern
Dorothee
D
D001665:Binding Sites; D002384:Catalysis; D021984:Cyclophilin A / Q000737:chemistry* / Q000378:metabolism*; D006860:Hydrogen Bonding; D007536:Isomerism; D007700:Kinetics; D008433:Mathematics; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D011487:Protein Conformation
D021984:Cyclophilin A