Limited proteolysis reveals low-affinity binding of N-acetyl-L-glutamate to rat-liver carbamoyl-phosphate synthetase (ammonia)
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1987.tb11207.x/fullpdf
Reference25 articles.
1. Characterization and derivation of the gene coding for mitochondrial carbamyl phosphate synthetase I of rat.
2. Carbamoyl phosphate synthetase I of human liver. Purification, some properties and immunological cross-reactivity with the rat liver enzyme
3. Purification, composition, and some properties of rat liver carbamyl phosphate synthetase (ammonia)
4. Mechanism of Carbamoyl-Phosphate Synthetase. Binding of ATP by the Rat-Liver Mitochondrial Enzyme
5. Mechanism of Carbamoyl-Phosphate Synthetase. Properties of the Two Binding Sites for ATP
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1. Gain of Glutaminase Function in Mutants of the Ammonia-specific Frog Carbamoyl Phosphate Synthetase;Journal of Biological Chemistry;2003-07
2. Limited proteolysis ofEscherichia colicytidine 5′-triphosphate synthase. Identification of residues required for CTP formation and GTP-dependent activation of glutamine hydrolysis;European Journal of Biochemistry;2003-04-16
3. Regulation of an Escherichia coli/Mammalian Chimeric Carbamoyl-phosphate Synthetase;Journal of Biological Chemistry;1998-11
4. The Smallest Carbamoyl-phosphate Synthetase;Journal of Biological Chemistry;1997-11
5. Crystallization, Characterization and Preliminary Crystallographic Studies of Carbamate Kinase of Streptococcus faecium;Journal of Molecular Biology;1994-01
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