Abstract
Based on molecular modelling study, we propose that the reaction between L-aspartate an carbamoylphosphate, catalyzed by E. coli aspartate carbamoyltransferase, may proceed via a tetrahedral intermediate and that the breakdown of the intermediate is facilitated by an intramolecular proton transfer between the amino group of L-aspartate and a terminal phosphate oxygen of carbamoylphosphate.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Aspartate Carbamoyltransferase / metabolism*
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Aspartic Acid / analogs & derivatives
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Aspartic Acid / metabolism
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Binding Sites
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Carbamyl Phosphate / metabolism
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Chemical Phenomena
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Chemistry
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Escherichia coli / enzymology*
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Hydrogen Bonding
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Models, Chemical
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Molecular Conformation
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Phosphonoacetic Acid / analogs & derivatives
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Phosphonoacetic Acid / metabolism
Substances
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Aspartic Acid
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Carbamyl Phosphate
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sparfosic acid
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Aspartate Carbamoyltransferase
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Phosphonoacetic Acid