Protonation states and catalysis: Molecular dynamics studies of intermediates in tryptophan synthase.

ABSTRACT: The importance of protonation states and proton transfer in pyridoxal 5'-phosphate (PLP)-chemistry can hardly be overstated. Although experimental approaches to investigate pKa values can provide general guidance for assigning proton locations, only static pictures of the chemical species are available. To obtain the overall protein dynamics for the interpretation of detailed enzyme catalysis in this study, guided by information from solid-state NMR, we performed molecular dynamics (MD) simulations for the PLP-dependent enzyme tryptophan synthase (TRPS), whose catalytic mechanism features multiple quasi-stable intermediates. The primary objective of this work is to elucidate how the position of a single proton on the reacting substrate affects local and global protein dynamics during the c

SUBMITTER: Huang YM 

PROVIDER: S-EPMC4815307 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature