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- W1542740774 abstract "In aspartate transcarbamylase (ATCase) each regulatory chain interacts with two catalytic chains each one belonging to a different trimeric catalytic subunit (R1-C1 and R1-C4 types of interactions as defined in Fig. 1). In order to investigate the interchain contacts that are involved in the co-operative interactions between the catalytic sites, a series of modified forms of the enzyme was prepared by site-directed mutagenesis. The amino acid replacements were devised on the basis of the previously described properties of an altered form of ATCase (pAR5-ATCase) which lacks the homotropic co-operative interactions between the catalytic sites. The results obtained (enzyme kinetics, bisubstrate analog influence and pH studies) show that the R1-C4 interaction is essential for the establishment of the enzyme conformation that has a low affinity for aspartate (T state), and consequently for the existence of co-operativity between the catalytic sites. This interaction involves the 236-250 region of the aspartate binding domain of the catalytic chain (240s loop) and the 143-149 region of the regulatory chain which comprises helix H3'." @default.
- W1542740774 created "2016-06-24" @default.
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- W1542740774 date "1990-11-01" @default.
- W1542740774 modified "2023-10-18" @default.
- W1542740774 title "Co-operative interactions between the catalytic sites in Escherichia coli aspartate transcarbamylase" @default.
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- W1542740774 doi "https://doi.org/10.1016/s0022-2836(05)80328-6" @default.
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