EC Number   |
General Information |
Reference |
|---|
   2.3.2.5 | evolution |
glutaminyl cyclase (QC) and isoglutaminyl cyclase (isoQC) belong to the family of the metalloenzymes |
759074 |
| 2.3.2.5 | evolution |
glutaminyl cyclase (QC, glutaminyl-peptide cyclotransferase (QPCT)) and its isoenzyme isoQC (QPCTL) belong to a family of enzymes which catalyze the formation of pyroglutamate (pGlu, pE) at N-terminus of proteins by converting glutamate/glutamine to pGlu residue |
759031 |
| 2.3.2.5 | evolution |
glutaminyl cyclases (QCs) belong to the class of acyl transferases. Different types of QCs are identified in bacteria, plants and animals, including mammalian tissues |
759702 |
| 2.3.2.5 | malfunction |
glutaminyl cyclase inhibitors alter the CD47 protein by inhibiting QPCTL function and the resulting block in pGlu-modified CD47 is nearly complete. The expansion, differentiation, cytokine production and killing capacity of human T cells is compatible with small molecule inhibition of QPCTL. But QPCTL deficiency and QPCTL inhibition enhance tumor cell control by tumor-specific antibodies |
759839 |
| 2.3.2.5 | malfunction |
knockdown of enzyme-transcript results in lower enzymatic activity, and small, unviable egg masses |
736239 |
| 2.3.2.5 | malfunction |
knockout of isoQC dramatically reduces the binding of SIRPalpha to cell surface |
759031 |
| 2.3.2.5 | malfunction |
loss of the pE-modification and N-terminal charge leads to accelerated aggregation of Abeta3(pE) compared with unmodified Abeta |
759074 |
| 2.3.2.5 | metabolism |
evidence for an involvement of glutaminyl cyclase (QC) in Alzheimer's disease pathogenesis via QC-catalyzed pE-Abeta formation |
759804 |
| 2.3.2.5 | metabolism |
the activity of myeloid cells such as macrophages and neutrophils is likewise regulated by a balance between stimulatory and inhibitory signals. In particular, cell surface expression of the CD47 protein creates a 'don't eat me' signal on tumor cells by binding to SIRPalpha expressed on myeloid cells. CD47 is a broadly expressed inhibitory ligand for myeloid cells. The glutaminyl-peptide cyclotransferase-like protein (QPCTL) is a major component of the CD47-SIRPalpha checkpoint. Interference with QPCTL expression leads to a major increase in neutrophil-mediated killing of tumor cells in vivo. Diglutamate formation occurs early in the CD47 protein life cycle and fully depends on QPCTL. Synergy between blockade of CD47 diglutamate formation and tumor opsonization in tumor cell killing by macrophages and neutrophils |
759839 |
| 2.3.2.5 | metabolism |
the dipeptidyl-peptidase activity of meprin beta links N-truncation of Abeta with glutaminyl cyclase-catalyzed pGlu-Abeta formation |
759392 |
