EC Number |
Reaction |
Reference |
---|
6.3.4.5 | ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate |
- |
- |
6.3.4.5 | ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate |
catalytic mechanism |
-, 652242 |
6.3.4.5 | ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate |
detailed catalytic mechanism |
652231 |
6.3.4.5 | ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate |
detailed catalytic mechanism, stereochemistry |
-, 652404 |
6.3.4.5 | ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate |
essential Arg in the active site participates in the binding of ATP and diphosphate. The binding of ATP and diphosphate at the same site is mutually exclusive |
1589 |
6.3.4.5 | ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate |
it is found that argininosuccinate synthetase is the major lipid A-interacting protein in liver. Argininosuccinate synthetase also inhibits the biological activities of natural lipid A and rough-type lipopolysaccharide and but not smooth-type lipopolysaccharide. Argininosuccinate synthetase enzyme activity is inhibited by lipid A and rough-type lipopolysaccharide and smooth-type lipopolysaccharide. |
675096 |
6.3.4.5 | ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate |
mechanism |
1574 |
6.3.4.5 | ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate |
ordered addition of MgATP2-, citrulline, and aspartate, followed by ordered release of argininosuccinate, magnesiumdiphosphate and AMP |
1587 |
6.3.4.5 | ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate |
rapid-equilibrium random mechanism |
-, 1579 |