The importance of the link between Glu super(204) of the catalytic chain and Arg super(130) of the regulatory chain for the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase

Recent x-ray crystallographic studies of aspartate transcarbamoylase bound with CTP have detected molecular asymmetry in the interface between the catalytic and regulatory subunits. In three of the six interfaces, a salt link occurs between Arg super(130) of the regulatory chain and Glu super(204) o...

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Bibliographic Details
Published in:The Journal of biological chemistry 1989-01, Vol.264 (25), p.14860-14864
Main Authors: Stebbins, J W, Kantrowitz, E R
Format: Article
Language:English
Subjects:
asparaginine
aspartate carbamoyltransferase
glutamine
Online Access:Get full text
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Summary:Recent x-ray crystallographic studies of aspartate transcarbamoylase bound with CTP have detected molecular asymmetry in the interface between the catalytic and regulatory subunits. In three of the six interfaces, a salt link occurs between Arg super(130) of the regulatory chain and Glu super(204) of the catalytic chain; however, these same residues are 15 angstroms apart in the other three interfaces. In order to determine if this is important for the function of the enzyme, two mutant versions of aspartate transcarbamoylase were created by site-specific mutagenesis.
ISSN:0021-9258