Abstract
The Jordan group's interest center on: E. coli (ec) and human (h) pyruvate dehydrogenase (PDHc), 2-oxoglutarate dehydrogenase (OGDHc) and 2-oxoadipate dehydrogenase (OADHc) complexes; and on 1-deoxy-D-xylulose-5-phosphate synthase (DXPS). The most important findings were: (1) the first components of OGDHc and OADHc and ecDXPS aerobically generated the ThDP-enamine radical species in “off-pathway” mechanism. (2) The pre-steady-state rate constants for conversion of pyruvate to all intermediates were determined on the entire E. coli PDHc. (3) The hydrogen–deuterium exchange MS (HDX-MS) method provided a snapshot of (i) the conformational dynamics of the full-length E. coli DXPS; (ii) interaction loci of the ecE1p-ecE2p subcomplex; (iii) the unique inter-component interaction sites in the hE1o-hE2o subcomplex, also complemented by chemical cross-linking MS. (4) Protein engineering using site saturation mutagenesis was applied to the first and second components of the ecOGDHc and led to formation of acyl-Coenzyme A with a variety acyl groups.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Reference Module in Chemistry, Molecular Sciences and Chemical Engineering
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
