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Literature summary for 2.3.2.5 extracted from

  • Hartlage-Ruebsamen, M.; Bluhm, A.; Piechotta, A.; Linnert, M.; Rahfeld, J.U.; Demuth, H.U.; Lues, I.; Kuhn, P.H.; Lichtenthaler, S.F.; Rossner, S.; Hoefling, C.
    Immunohistochemical evidence from APP-transgenic mice for glutaminyl cyclase as drug target to diminish pE-Abeta formation (2018), Molecules, 23, 924 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
drug development glutaminyl cyclase is a drug target to diminish pE-Abeta formation Mus musculus
pharmacology glutaminyl cyclase is a drug target to diminish pE-Abeta formation Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information generation of QC knock-out mice with no neuronal labeling of the enzyme. Deposition of pE-Abeta only in the brain regions of amyloid precursor protein (APP)-transgenic Tg2576 mice with detectable human APP and endogenous QC expression, such as the hippocampus, piriform cortex, and amygdala. Identification of brain regions with substantial expression of human APP and QC in the absence of pE-Abeta deposition (the Edinger-Westphal nucleus and locus coeruleus). In these brain regions, the enzymes required to generate N-truncated Abeta peptides as substrates for QC might be lacking. In APP-transgenic Tg2576 mice, pE-Abeta deposits concentrate in the neocortex and hippocampus and are not detected in the respective subcortical structures affected by this pathology in Alzheimer's disease brains Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutaminyl-Abeta(3-42) peptide Mus musculus a glutamate residue (E) is exposed at position 3 of Abeta(3-42) and can be converted by the enzymatic activity of glutaminyl cyclase (QC) to pE resulting in the peptide pE-Abeta(3-42). 5-Oxoproline ring formation under liberation of water. Slow conversion of N-terminal glutamate under slightly acidic pH conditions, as compared with the much faster pE formation from N-terminal glutamine 5-oxoprolyl-Abeta(3-42) peptide + NH3
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?
L-glutaminyl-peptide Mus musculus
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5-oxoprolyl-peptide + NH3
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?

Organism

Organism UniProt Comment Textmining
Mus musculus Q9CYK2
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-

Source Tissue

Source Tissue Comment Organism Textmining
amygdala
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Mus musculus
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brain
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Mus musculus
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Edinger-Westphal nucleus
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Mus musculus
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hippocampus in interneurons and pyramidal cells, not in granule cells Mus musculus
-
lateral hypothalamus
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Mus musculus
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locus ceruleus
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Mus musculus
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additional information not in anterodorsal thalamic nucleus, perifornical nucleus, and granule cells Mus musculus
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piriform area
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Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutaminyl-Abeta(3-42) peptide
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Mus musculus 5-oxoprolyl-Abeta(3-42) peptide + NH3
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?
L-glutaminyl-Abeta(3-42) peptide a glutamate residue (E) is exposed at position 3 of Abeta(3-42) and can be converted by the enzymatic activity of glutaminyl cyclase (QC) to pE resulting in the peptide pE-Abeta(3-42). 5-Oxoproline ring formation under liberation of water. Slow conversion of N-terminal glutamate under slightly acidic pH conditions, as compared with the much faster pE formation from N-terminal glutamine Mus musculus 5-oxoprolyl-Abeta(3-42) peptide + NH3
-
?
L-glutaminyl-peptide
-
Mus musculus 5-oxoprolyl-peptide + NH3
-
?

Synonyms

Synonyms Comment Organism
glutaminyl cyclase
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Mus musculus

General Information

General Information Comment Organism
metabolism evidence for an involvement of glutaminyl cyclase (QC) in Alzheimer's disease pathogenesis via QC-catalyzed pE-Abeta formation Mus musculus
physiological function the enzyme glutaminyl cyclase (QC) acts as glutamyl cyclase to catalyze pE-Abeta formation from N-terminal glutamate. A glutamate residue (E) is exposed at position 3 of Abeta(3-42) and can be converted by the enzymatic activity of glutaminyl cyclase (QC) to pE resulting in the peptide pE-Abeta(3-42). Slow conversion of N-terminal glutamate under slightly acidic pH conditions, as compared with the much faster pE formation from N-terminal glutamine Mus musculus