Pyroglutamate aminopeptidase is a type of
enzyme that cleaves the
peptide bond
In organic chemistry, a peptide bond is an amide type of covalent chemical bond linking two consecutive alpha-amino acids from C1 (carbon number one) of one alpha-amino acid and N2 (nitrogen number two) of another, along a peptide or protein cha ...
linking the N-terminal end of a polypeptide forming a cyclical
lactam
A lactam is a cyclic amide, formally derived from an amino alkanoic acid. The term is a portmanteau of the words ''lactone'' + ''amide''.
Nomenclature
Greek prefixes in alphabetical order indicate ring size:
* α-Lactam (3-atom rings)
* β-Lacta ...
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.
See also
*
Pyroglutamyl-peptidase I
Pyroglutamyl-peptidase I (, also known as Pyrrolidonyl peptidase, is an enzyme (a cysteine peptidase) found in bacteria, plants and animals.
It can be used to distinguish certain Streptococcal organisms.
Other names are ''5-oxoprolyl-peptidase'', ...
*
Pyroglutamyl-peptidase II
Pyroglutamyl-peptidase II (, ''thyroliberinase'', ''pyroglutamyl aminopeptidase II'', ''thyrotropin-releasing factor pyroglutamate aminopeptidase'', ''pyroglutamate aminopeptidase II'', ''pyroglutamyl peptidase II'', ''thyroliberin-hydrolyzing pyro ...
References
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Proteases
EC 3.4