The Journal of biological chemistry, 272(28), 17293-17302 (1997-07-11)
Two high resolution crystal structures of cytosolic aspartate aminotransferase from pig heart provide additional insights into the stereochemical mechanism for ligand-induced conformational changes in this enzyme. Structures of the homodimeric native structure and its complex with the substrate analog 2-methylaspartate
Intrinsic deuterium kinetic isotope effects in glutamate mutase measured by an intramolecular competition experiment.
Miri Yoon et al.
Angewandte Chemie (International ed. in English), 46(44), 8455-8459 (2007-10-03)
Journal of molecular biology, 239(2), 285-305 (1994-06-03)
Three crystal structures of wild type E. coli aspartate aminotransferase (E.C.2.6.1.1) in space group P2(1) have been determined at resolution limits between 2.6 and 2.35 A. The unliganded enzyme and its complexes with the substrate analogues maleate and 2-methylaspartate resulted
Proceedings of the National Academy of Sciences of the United States of America, 99(1), 123-127 (2001-12-14)
Chemoreceptors in Escherichia coli are coupled to the flagella by a labile phosphorylated intermediate, CheY approximately P. Its activity can be inferred from the rotational bias of flagellar motors, but motor response is stochastic and limited to a narrow physiological
Nitric oxide : biology and chemistry, 17(3-4), 115-121 (2007-09-18)
Nitric oxide (NO) is an important vasorelaxant produced along with L-citrulline from L-arginine in a reaction catalyzed by endothelial nitric oxide synthase (eNOS). Previous studies suggested that the recycling of L-citrulline to L-arginine is essential for NO production in endothelial
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