Carbamoyl-phosphate synthase I (pig liver) is modified at the cysteine residues 1327 and 1337 (numbered according to the rat sequence) in the presence of 5 mM-N-acetyl-L-glutamate with enhanced rate. ATP/Mg2+ (greater than or equal to 5 mM) protects against alkylation of these two cysteines and loss of activity. According to the results obtained by limited proteolysis of monobromobimane-modified carbamoyl-phosphate synthase I, the accessible cysteines 1327 and 1337 are located in the C-terminal 20 kDa domain D of the enzyme. N-Bromoacetyl-L-glutamate is an allosteric activator and inactivates carbamoyl-phosphate synthase in a slow reaction.
Research Article|June 01 1989
Identification of cysteine residues in carbamoyl-phosphate synthase I with reactivity enhanced by N-acetyl-l-glutamate
Biochem J (1989) 260 (2): 573-576.
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K Geschwill, L Lumper; Identification of cysteine residues in carbamoyl-phosphate synthase I with reactivity enhanced by N-acetyl-l-glutamate. Biochem J 1 June 1989; 260 (2): 573–576. doi: https://doi.org/10.1042/bj2600573
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