Use this URL to cite or link to this record in EThOS: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.796146
Title: Structure and function of isocitrate dehydrogenase from Escherichia coli ML308
Author: McKee, Jillian Stewart
Awarding Body: University of Glasgow
Current Institution: University of Glasgow
Date of Award: 1989
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Abstract:
The level of activity of the NADP-dependent isocitrate dehydrogenase (ICDH) of E. coli ML308 is controlled by a reversible phosphorylation mechanism during growth on acetate as sole carbon source. Under such conditions the enzymes of the glyoxylate bypass, isocitrate lyase (ICL) and malate synthase are induced. This results in competition between ICDH and ICL for the available isocitrate. To allow efficient use of isocitrate via the glyoxylate bypass ICDH is phosphorylated on a single serine residue per subunit which completely inactivates it. Phosphorylation of ICDH is believed to occur at the NADP+ binding site, and so the enzyme is inactive because it cannot bind its cofactor.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.796146  DOI: Not available
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