Pseudomonas aeruginosa Aspartate Transcarbamoylase

Purification of aspartate transcarbamoylase from Pseudomonas syringae.

The aspartate transcarbamoylase (ATCase) from Pseudomonas syringae has been purified. The purified enzyme was shown by SDS-PAGE to give two bands. Unambiguous results from N-terminal sequencing suggested that each band represented a homogeneous polypeptide. The M(r) (relative molecular mass) of the polypeptides was estimated to be 47 kDa and 34 kDa. The M(r) of the holoenzyme determined by gel ...

Aspartate Transcarbamoylase of Aeromonas Hydrophila

The thiol group in the catalytic chains of aspartate transcarbamoylase.

The allosteric enzyme aspartate transcarbamoylase (EC 2.1.3.2) was previously shown to consist of two functionally distinct types of polypeptide chains. X-ray diffraction and chemical studies showed that there are six copies of both catalytic (C) and regulatory (R) chains, and that the intact molecular complex (C(6)R(6)) has D(3) symmetry. Organomercurials react preferentially with the four thi...

Thermodynamics of assembly of Escherichia coli aspartate transcarbamoylase.

Reaction microcalorimetry and potentiometry have been used to define the thermodynamics of assembly of Escherichia coli aspartate transcarbamoylase (aspartate carbamoyltransferase, carbamoylphosphate:L-aspartate carbamoyltransferase, EC 2.1.3.2) from its catalytic and regulatory subunits and the linkage between assembly and proton binding. Over the pH range 7-9.5 and the temperature range 15-30...

Encapsulated Pseudomonas Aeruginosa (pseudomonas Aeruginosa Mucosus) Strains.