EC 2.1.3.2: aspartate carbamoyltransferase
TransferasesOpen in Browse
CatLog read 2 records for EC 2.1.3.2 from 1 paper, for 1 organism. Names in these papers: aspartate transcarbamylase (ATC domain of CAD).
Read from the paper by an AI model and checked against the paper by a second, separate AI run; code converted the units.
CatLog also holds 10 records for EC 2.1.3.2 that are not yet re-read: from its earlier version, built from the enzyme databases and partly checked against the papers. All records for EC 2.1.3.2 in Browse.
Papers
| Paper | Organisms | Records |
|---|---|---|
| The isolation and characterization of the aspartate transcarbamylase domain of the multifunctional protein, CAD | Mesocricetus auratus | 2 |
Records
| Enzyme | Organism | Substrate | kcat (s⁻¹) | Km (mM) | kcat/Km (mM⁻¹ s⁻¹) | Conditions | Paper | Open record |
|---|---|---|---|---|---|---|---|---|
| aspartate transcarbamylase (ATC domain of CAD) | Mesocricetus auratus | carbamoyl phosphate | 35.88 | 0.02073 | 1731 calc. | pH 7.7, 37 °C | PMID 6300078 | Open record: aspartate transcarbamylase (ATC domain of CAD), carbamoyl phosphate |
| aspartate transcarbamylase (ATC domain of CAD) | Mesocricetus auratus | L-aspartate | 79.7 | 21.34 | 3.73 calc. | pH 7.7, 37 °C | PMID 6300078 | Open record: aspartate transcarbamylase (ATC domain of CAD), L-aspartate |