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Aspartate transcarbamylase allosteric effectors

Three-dimensional structure of E. coli aspartate transcarbamylase. Half of the native c6r6 molecule (see Fig. II-4) is shown. The catalytic (c) submit, which binds the substrates aspartate and carbamyl phosphate is shown in light shading. The regulatory (r) subunit, which binds the allosteric effectors CTP and ATP, is shown in dark shading. From Kantrowitz, E.R., et al. (1980). E. coli Aspartate Transcarbamylase. Part 11 Structure and Allosteric Interactions. Trends Biochem Sci 5 150 and Stryer, L. (1995). Biochemistry, 4th ed. New York Freeman, Figure 10-5, p. 240. Reprinted by permission. [Pg.151]


See other pages where Aspartate transcarbamylase allosteric effectors is mentioned: [Pg.177]   
See also in sourсe #XX -- [ Pg.276 ]

See also in sourсe #XX -- [ Pg.276 ]




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