Natalia Nemeria
Department of Chemistry at Rutgers
the State University
Newark
New Jersey 07102
USA
Name/email consistency: high
- Glutamate 636 of the Escherichia coli pyruvate dehydrogenase-E1 participates in active center communication and behaves as an engineered acetolactate synthase with unusual stereoselectivity. Nemeria, N., Tittmann, K., Joseph, E., Zhou, L., Vazquez-Coll, M.B., Arjunan, P., Hübner, G., Furey, W., Jordan, F. J. Biol. Chem. (2005)
- Tetrahedral intermediates in thiamin diphosphate-dependent decarboxylations exist as a 1',4'-imino tautomeric form of the coenzyme, unlike the michaelis complex or the free coenzyme. Nemeria, N., Baykal, A., Joseph, E., Zhang, S., Yan, Y., Furey, W., Jordan, F. Biochemistry (2004)
- Histidine 407, a phantom residue in the E1 subunit of the Escherichia coli pyruvate dehydrogenase complex, activates reductive acetylation of lipoamide on the E2 subunit. An explanation for conservation of active sites between the E1 subunit and transketolase. Nemeria, N., Arjunan, P., Brunskill, A., Sheibani, F., Wei, W., Yan, Y., Zhang, S., Jordan, F., Furey, W. Biochemistry (2002)
