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- W2510346937 abstract "The enzymic activity of crystalline mitochon- drial aspartate aminotransferase (L-aspartate:2-oxoglutarate ami- notransferase, EC 2.6.'1.1) was determined in suspensions of non- crosslinked microcrystals in 30% (wt/vol) polyethylene glycol. The crystals (average dimensions, 22 x 5 x 0.8, m) were small enough to preclude diffusional rate limitation. They had the same habit as the triclinic crystals used for the determination of the spatial structure of the enzyme by x-ray crystallographic analysis (Ford, G. C., Eichele, G., andJansonius, J. N. (1980) Proc. Natl. Acad. Sci. USA 77, 2559-2563). Determination of the Michaelis-Menten parameters showed that the packing of the enzyme dimer into the crystal lattice not only decreases its activity but also induces a functional nonequivalence of the two subunits that behave iden- tically in solution. The crystalline enzyme possesses a high-affinity subunit with Km values similar to those of the enzyme in solution (K' = 0.5 mM for aspartate and 1.2 mM for 2-oxoglutarate) and a low-affinity subunit (K' = 5.5 mM and 14.5 mM, respectively). The catalytic activity of the high-affinity subunit is 3% and that of the low-affinity subunit is 15% of the activity of the enzyme in solution. The functional asymmetry of the crystalline enzyme di- mer could also be demonstrated by selective mechanism-based modification of either type of active sites. In view of the appar- ently identical conformation of the two subunits in the crystalline enzyme, its decreased catalytic efficiency and its functional asym- metry likely are due to constraints exerted by the crystal lattice on the conformational adaptability of the two subunits. In triclinic crystals the two subunits of the enzyme dimer have dissimilar lat- tice contacts." @default.
- W2510346937 created "2016-09-16" @default.
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- W2510346937 date "2016-01-01" @default.
- W2510346937 modified "2023-09-27" @default.
- W2510346937 title "Crystalline aspartate aminotransfe) asymmetry of the two subunits (activity of crystalline enzyme/microcrystals/crystal lattice effects/p<" @default.
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- W2510346937 hasPublicationYear "2016" @default.
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