Biomaterial Database

Negative cooperativity in human liver argininosuccinase. 1982

N Carvajal, and M Fernández, and J P Rodríguez, and J Martínez

The kinetic properties of argininosuccinase (L-argininosuccinate arginine-lyase, EC 4.3.2.1.) were investigated. Negative cooperativity was observed in the response of the enzyme to the substrate argininosuccinate and GTP behaved as a positive allosteric effector. These effects were observed in 60 mM potassium phosphate but not in 50 mM Tris-HCl. Structural changes in the protein molecule are suggested to explain previous observations of Michaelis-Menten kinetics for this enzyme.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008099	Liver	A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.	Livers
D008190	Lyases	A class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4.	Desmolase,Desmolases,Lyase
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D006160	Guanosine Triphosphate	Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.	GTP,Triphosphate, Guanosine
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000494	Allosteric Regulation	The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES.	Regulation, Allosteric,Allosteric Regulations,Regulations, Allosteric
D001123	Argininosuccinate Lyase	An enzyme of the urea cycle which splits argininosuccinate to fumarate plus arginine. Its absence leads to the metabolic disease ARGININOSUCCINIC ACIDURIA in man. EC 4.3.2.1.	Argininosuccinase,Lyase, Argininosuccinate
D001125	Argininosuccinic Acid	This amino acid is formed during the urea cycle from citrulline, aspartate and ATP. This reaction is catalyzed by argininosuccinic acid synthetase.	N-(4-Amino-4-carboxybutyl)amidino-L-aspartic Acid,Acid, Argininosuccinic