Apparent negative co-operativity and substrate inhibition in overexpressed glutamate dehydrogenase from Escherichia coli.
In: FEMS microbiology letters, Jg. 281 (2008-04-01), Heft 2, S. 132-9
Online
academicJournal
Zugriff:
The gene for Escherichia coli glutamate dehydrogenase (EcGDH) has been overexpressed, and a simplified purification procedure afforded greatly increased yields of c. 40 mg pure EcGDH L(-1) culture. EcGDH was unstable at a low concentration in plastic tubes, but stabilization measures allowed a robust kinetic characterization. Contrary to past reports, EcGDH deviates from Michaelis-Menten kinetics, exhibiting apparent mild negative co-operativity with both l-glutamate and NADP+, with Hill coefficients of 0.90 and 0.92, respectively. NADPH yielded simple Michaelis-Menten kinetics but both 2-oxoglutarate and NH4+ showed substrate inhibition. pH optima were 9 for oxidative deamination and 8 for reductive amination.
| Titel: |
Apparent negative co-operativity and substrate inhibition in overexpressed glutamate dehydrogenase from Escherichia coli.
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| Autor/in / Beteiligte Person: | Sharkey, MA ; Engel, PC |
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| Zeitschrift: | FEMS microbiology letters, Jg. 281 (2008-04-01), Heft 2, S. 132-9 |
| Veröffentlichung: | 2015- : Oxford Oxford University Press ; <i>Original Publication</i>: Amsterdam, Published by Elsevier/North Holland on behalf of the Federation of European Microbiological Societies., 2008 |
| Medientyp: | academicJournal |
| ISSN: | 0378-1097 (print) |
| DOI: | 10.1111/j.1574-6968.2008.01086.x |
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