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- W2024665625 abstract "The structure of aspartate transcarbamylase of Escherichia coli ligated to products (phosphate and N-carbamyl-l-aspartate) has been determined at 2.37 A resolution (R-factor = 0.23, R(free) = 0.27). Results might indicate a product release mode, rather than close analogues to the transition state like those found in our earlier studies of other ligands (N-phosphonacetyl-L-aspartate, carbamyl phosphate plus malonate, phosphonoacetamide plus malonate, or citrate plus phosphate). Ordered product release, first carbamylaspartate (CLA) and then phosphate, might be facilitated by a 4 A movement of phosphate from the substrate-analogue position to the product (phosphate) binding position, and by a somewhat similar release movement of the other product (CLA) relative to its analogue (citrate). This movement is consistent with earlier studies of binding of either pyrophosphate or phosphate alone [Honzatko, R. B., and Lipscomb, W. N. (1982) J. Mol. Biol. 160, 265-286]." @default.
- W2024665625 created "2016-06-24" @default.
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- W2024665625 date "2004-05-06" @default.
- W2024665625 modified "2023-10-13" @default.
- W2024665625 title "Products in the T-State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and <i>N</i>-Carbamyl-<scp>l</scp>-aspartate Ligated Enzyme<sup>,</sup>" @default.
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- W2024665625 doi "https://doi.org/10.1021/bi0302144" @default.
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