Abstract:
:N-Terminal glutaminyl and glutamyl residues of peptides and proteins tend to form pyroglutamic acid (pGlu) by intramolecular cylization. The rate constants for spontaneous cyclization of glutamine (10(-6) s(-1)) and glutamic acid (10(-9) s(-1)) in aqueous solution differ by approximately 3 orders of magnitude at pH 6.5. Glutaminyl cyclases (QCs) from plants and mammals accelerate pGlu formation. Human QC exhibits a rate enhancement of 2.2 x 10(5) for glutamate cyclization, approximately 2 orders of magnitude lower than that of the corresponding N-terminal glutaminyl reaction. Thus, glutaminyl cyclases are enzymes with only modest specificity for cyclization of their primary glutaminyl substrates and may provide a link between glutamate cyclization and pathophysiology.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Seifert F,Schulz K,Koch B,Manhart S,Demuth HU,Schilling Sdoi
10.1021/bi9018835subject
Has Abstractpub_date
2009-12-22 00:00:00pages
11831-3issue
50eissn
0006-2960issn
1520-4995journal_volume
48pub_type
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