Replacement of Asp‐162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase
The available crystal structures of Escherichia coli aspartate transcarbamoylase (ATCase) show that the conserved residue Asp‐162 from the catalytic chain interacts with essentially the same residues in both the T‐ and R‐states. To study the role of Asp‐162 in the regulatory properties of the enzyme...
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Veröffentlicht in: | Protein science 2002-05, Vol.11 (5), p.1074-1081 |
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