Pyroglutamate aminopeptidase

Pyroglutamate aminopeptidase is a type of enzyme that cleaves the peptide bond linking the N-terminal end of a polypeptide forming a cyclical lactam to the next amino acid residue. This cyclic structure protects the polypeptide from degradation but renders the protein difficult to analyze in the laboratory. Pyroglutamate aminopeptidase may be used to cleave the cyclical lactam and will therefore leave the next amino acid with a free N-terminal.^[1]

References[edit]

^ Mozdzanowski, Jacek; Bongers, Jacob; Anumula, Kalyan (1 July 1998). "High-Yield Deblocking of Amino Termini of Recombinant Immunoglobulins with Pyroglutamate Aminopeptidase". Analytical Biochemistry. 260 (2): 183–187. doi:10.1006/abio.1998.2690. PMID 9657876.

[1] Mozdzanowski, Jacek; Bongers, Jacob; Anumula, Kalyan (1 July 1998). "High-Yield Deblocking of Amino Termini of Recombinant Immunoglobulins with Pyroglutamate Aminopeptidase". Analytical Biochemistry. 260 (2): 183–187. doi:10.1006/abio.1998.2690. PMID 9657876.

[1]

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

See also[edit]

References[edit]