Substrate specificity of human metallocarboxypeptidase D: Comparison of the two active carboxypeptidase domains

• Published in: PloS one Vol. 12; no. 11; p. e0187778
• Main Authors: Garcia-Pardo, Javier, Tanco, Sebastian, Díaz, Lucía, Dasgupta, Sayani, Fernandez-Recio, Juan, Lorenzo, Julia, Aviles, Francesc X, Fricker, Lloyd D
• Format: Journal Article Publication
• Language: English
• Published: United States Public Library of Science 13.11.2017; Public Library of Science (PLoS)
• Subjects: Amino Acid Sequence; Amino acids; Biochemistry; Biology; Biology and Life Sciences; Bortezomib - chemistry; Carboxypeptidase D; Carboxypeptidase domains; Catalytic Domain; Cell surface; Compounds; Drosophila; Enginyeria biomèdica; Enginyeria de proteïnes; Enzymes; Genetic aspects; Geographical variations; Golgi apparatus; HEK293 Cells; Humans; Hydrogen ions; Hydrogen-Ion Concentration; Insects; Kinetics; Life sciences; Mammals; Metallocarboxypeptidase D (CPD); Molecular docking; Molecular Docking Simulation; Mutation; Peptides; Peptides - chemistry; pH effects; Physical Sciences; Physiological aspects; Point Mutation; Polypeptides; Properties; Proteases; Protein engineering; Proteins; Proteins - chemistry; Proteins - genetics; Proteins - metabolism; Research and Analysis Methods; Substrate Specificity; Substrates; Àrees temàtiques de la UPC; Belgium; United States; Spain; New York; United States > US

Metallocarboxypeptidase D (CPD) is a membrane-bound component of the trans-Golgi network that cycles to the cell surface through exocytic and endocytic pathways. Unlike other members of the metallocarboxypeptidase family, CPD is a multicatalytic enzyme with three carboxypeptidase-like domains, altho...