Methylmalonyl -Coa Decarboxylase (Ygfg) for Escherichia Coli: A New Activity for the Crotonase Superfamily
Haller, Toomas
This item is only available for download by members of the University of Illinois community. Students, faculty, and staff at the U of I may log in with your NetID and password to view the item. If you are trying to access an Illinois-restricted dissertation or thesis, you can request a copy through your library's Inter-Library Loan office or purchase a copy directly from ProQuest.
Permalink
https://hdl.handle.net/2142/84776
Description
Title
Methylmalonyl -Coa Decarboxylase (Ygfg) for Escherichia Coli: A New Activity for the Crotonase Superfamily
Author(s)
Haller, Toomas
Issue Date
2001
Doctoral Committee Chair(s)
Gerlt, John A.
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Microbiology
Language
eng
Abstract
The E113Q mutant exhibited significantly larger isotope effect for both kcat and kcat/Km than wild-type, suggesting differences in reaction mechanism between wild type and E113Q. Although experimental difficulties encountered did not allow quantitative studies of stereochemistry of the MMDC reaction, the reaction catalyzed by wild-type MMDC proceeds with retention of configuration using (S)-methylmalonyl-CoA as a substrate, and with inversion of configuration using (R)-methylmalonyl-CoA as a substrate. H66F catalyzed the MMDC reaction with at least partial racemization. I postulated that His66 is important in retaining structure of the active site.
Use this login method if you
don't
have an
@illinois.edu
email address.
(Oops, I do have one)
IDEALS migrated to a new platform on June 23, 2022. If you created
your account prior to this date, you will have to reset your password
using the forgot-password link below.
