Glutaminyl cyclase

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Function

Glutaminyl cyclase (QC) or glutaminyl-peptide cyclotransferase catalyzes the conversion of glutaminyl-peptide to 5-oxoprolyl-peptide and ammonia. Thus QC catalyzes the cyclization of an N-terminal glutamyl residue[1].

Relevance

The biological assembly of Human Glutaminyl cyclase is . QC is considered as a marker of thyroid tumors. QC acts on the generation of N-terminal pyroglutamyl groups of peptide hormones and amyloid-related plaque-forming peptides. The latter contributes to Alzheimer disease. Alzheimer patients show increased expression of QC[2] and QC inhibitors reduces the disease pathology and symptoms.

Structural highlights

The [3].

Structure of human glutaminyl cyclase complex with benzyimidazole and Zn+2 ion (PDB code 2afx).

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3D Structures of glutaminyl cyclase3D Structures of glutaminyl cyclase

Updated on 16-March-2023

ReferencesReferences

  1. Busby WH Jr, Quackenbush GE, Humm J, Youngblood WW, Kizer JS. An enzyme(s) that converts glutaminyl-peptides into pyroglutamyl-peptides. Presence in pituitary, brain, adrenal medulla, and lymphocytes. J Biol Chem. 1987 Jun 25;262(18):8532-6. PMID:3597387
  2. Valenti MT, Bolognin S, Zanatta C, Donatelli L, Innamorati G, Pampanin M, Zanusso G, Zatta P, Dalle Carbonare L. Increased glutaminyl cyclase expression in peripheral blood of Alzheimer's disease patients. J Alzheimers Dis. 2013;34(1):263-71. doi: 10.3233/JAD-120517. PMID:23207485 doi:http://dx.doi.org/10.3233/JAD-120517
  3. Huang KF, Liu YL, Cheng WJ, Ko TP, Wang AH. Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation. Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13117-22. Epub 2005 Aug 31. PMID:16135565

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