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Product aspartate transcarbamylase, catalytic subunit
| aspartate transcarbamylase, catalytic subunit |
| aspartate carbamoyltransferase, catalytic subunit |
| Host Site | Page Links |
|---|---|
| EcoCyc | ASPCARBCAT-MONOMER |
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- Fetler, L., P. Vachette, G. Herve, M.M. Ladjimi 1995. Unlike the quaternary structure transition, the tertiary structure change of the 240s loop in allosteric aspartate transcarbamylase requires active site saturation by substrate for completion. Bioch
- Murata, L.B., H.K. Schachman 1996. Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: implications for domain switching. Protein Sci. 5:719-728
- Murata, L.B., H.K. Schachman 1996. Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase.