The function of Glu338 in the catalytic triad of the carbamoyl phosphate synthetase amidotransferase domain.

doi:10.1016/s0167-4838(98)00212-x

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Article

The function of Glu338 in the catalytic triad of the carbamoyl phosphate synthetase amidotransferase domain.

Biochimica et biophysica acta - 10 Nov 1998

Hewagama A, Guy H I, Chaparian M, Evans D R

Abstract excerpt

The synthesis of carbamoyl phosphate by the mammalian multifunctional protein, CAD, involves the concerted action of the 40 kDa amidotransferase domain (GLN), that hydrolyzes glutamine and the 120 kDa synthetase (CPS) domain that uses the ammonia, thus produced, ATP and bicarbonate to make carbam...

Topics

Ammonia
Animals
Carbamoyl-Phosphate Synthase (Ammonia)
Cells, Cultured
Cricetinae
Escherichia coli
Glutaminase
Glutamine
Kinetics
Mesocricetus
Mutagenesis, Site-Directed
Mutation
Recombinant Fusion Proteins

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