McKee, Jillian Stewart (1989) Structure and Function of Isocitrate Dehydrogenase From Escherichia coli ML308. PhD thesis, University of Glasgow.
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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.
Item Type: | Thesis (PhD) |
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Qualification Level: | Doctoral |
Keywords: | Biochemistry |
Date of Award: | 1989 |
Depositing User: | Enlighten Team |
Unique ID: | glathesis:1989-76860 |
Copyright: | Copyright of this thesis is held by the author. |
Date Deposited: | 14 Jan 2020 09:31 |
Last Modified: | 14 Jan 2020 09:31 |
URI: | https://theses.gla.ac.uk/id/eprint/76860 |
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