Km for NH4+

Range 100 glutamine synthetase (GS): 2,000 glutamate dehydrogenase (GDH) µM
Organism Bacteria Escherichia coli
Reference Boogerd FC, Ma H, Bruggeman FJ, van Heeswijk WC, García-Contreras R, Molenaar D, Krab K, Westerhoff HV. AmtB-mediated NH3 transport in prokaryotes must be active and as a consequence regulation of transport by GlnK is mandatory to limit futile cycling of NH4(+)/NH3. FEBS Lett. 2011 Jan 3 585(1):23-8 p.24 left column 3rd paragraphPubMed ID21134373
Primary Source [12] Meek, T.D. and Villafranca, J.J. (1980) Kinetic mechanism of Escherichia coli glutamine synthetase. Biochemistry 19, 5513–5519. [13] Colanduoni, J., Nissan, R. and Villafranca, J.J. (1987) Studies of the mechanism of glutamine synthetase utilizing pH-dependent behavior in catalysis and binding. J. Biol. Chem. 262, 3037–3043. [14] Alibhai, M. and Villafranca, J.J. (1994) Kinetic and mutagenic studies of the role of the active site residues Asp-50 and Glu-327 of Escherichia coli glutamine synthetase. Biochemistry 33, 682–686. [15] Sakamoto, N., Kotre, A.M. and Savageau, M.S. (1975) Glutamate dehydrogenase from Escherichia coli: purification and properties. J. Bacteriol. 124, 775–783. [16] Sharkey, M.A. and Engel, P.C. (2008) Apparent negative co-operativity and substrate inhibition in overexpressed glutamate dehydrogenase from Escherichia coli. FEMS Microbiol. Lett. 281, 132–139.PubMed ID6109545, 2880845, 7904829, 241744, 18294195
Comments Primary sources [12-14] for GS, primary sources [15-16] for GDH
Entered by Uri M
ID 106346