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Information on EC 2.3.2.5 - glutaminyl-peptide cyclotransferase and Organism(s) Mus musculus and UniProt Accession Q9CYK2

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     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.5 glutaminyl-peptide cyclotransferase
IUBMB Comments
Involved in the formation of thyrotropin-releasing hormone and other biologically active peptides containing N-terminal pyroglutamyl residues. The enzyme from papaya also acts on glutaminyl-tRNA.
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This record set is specific for:
Mus musculus
UNIPROT: Q9CYK2
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
glutaminyl cyclase, isoqc, qpctl, glutaminyl-peptide cyclotransferase, isodromeqc, glutamine cyclotransferase, golgi resident enzyme, dromeqc, golgi-resident enzyme, h-isoqc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutaminyl cyclase
-
cyclotransferase, glutaminyl-transfer ribonucleate
-
-
-
-
glutaminyl cyclase
glutaminyl-tRNA cyclotransferase
-
-
-
-
isoQC
-
isozyme
QC
-
-
-
-
Qpct1
-
isozyme
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminoacyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutaminyl-peptide gamma-glutamyltransferase (cyclizing)
Involved in the formation of thyrotropin-releasing hormone and other biologically active peptides containing N-terminal pyroglutamyl residues. The enzyme from papaya also acts on glutaminyl-tRNA.
CAS REGISTRY NUMBER
COMMENTARY hide
37257-21-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
show the reaction diagram
-
-
-
?
L-Gln-2-naphthylamide
L-pyroglutamyl-2-naphthylamide + NH3
show the reaction diagram
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
show the reaction diagram
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
L-pyroglutamyl-4-methylcoumarin-7-amide + NH3
show the reaction diagram
-
-
-
?
L-Gln-Gly
5-oxoprolyl-Gly + NH3
show the reaction diagram
-
-
-
?
L-Gln-Gly
L-pyroglutamyl-Gly + NH3
show the reaction diagram
-
-
-
?
L-Gln-Gly-L-Pro
5-oxoprolyl-Gly-L-Pro + NH3
show the reaction diagram
-
-
-
?
L-Gln-Gly-L-Pro
pyroglutamyl-Gly-L-Pro + NH3
show the reaction diagram
-
-
-
?
L-Gln-L-Ala
L-pyroglutamyl-L-Ala + NH3
show the reaction diagram
-
-
-
?
L-Gln-L-Arg-Gly-L-Ile-NH2
pyroglutamyl-L-Arg-Gly-L-Ile-NH2 + NH3
show the reaction diagram
-
-
-
?
L-Gln-L-Asn-Gly-L-Ile-NH2
L-pyroglutamyl-L-Asn-Gly-L-Ile-NH2 + NH3
show the reaction diagram
-
-
-
?
L-Gln-L-Gln
L-pyroglutamyl-L-Gln + NH3
show the reaction diagram
-
-
-
?
L-Gln-L-Gln-OH
5-oxoprolyl-L-Gln + NH3
show the reaction diagram
-
-
-
?
L-Gln-L-Glu
L-pyroglutamyl-L-Glu + NH3
show the reaction diagram
-
-
-
?
L-Gln-L-Glu-L-Asp-L-Leu-NH2
5-oxoprolyl-L-Glu-L-Asp-L-Leu-NH2 + NH3
show the reaction diagram
-
-
-
?
L-Gln-L-Glu-OH
5-oxoprolyl-L-Glu + NH3
show the reaction diagram
-
-
-
?
L-Gln-L-Lys-L-Arg-L-Leu-NH2
5-oxoprolyl-L-Lys-L-Arg-L-Leu-NH2 + NH3
show the reaction diagram
-
-
-
?
L-Gln-L-Phe-L-Ala-NH2
5-oxoprolyl-L-Phe-L-Ala-NH2 + NH3
show the reaction diagram
-
-
-
?
L-Gln-L-Thr-Gly-L-Ile-NH2
L-pyroglutamyl-L-Thr-Gly-L-Ile-NH2 + NH3
show the reaction diagram
-
-
-
?
L-Gln-L-Trp-L-Ala-NH2
L-pyroglutamyl-L-Trp-L-Ala-NH2 + NH3
show the reaction diagram
-
-
-
?
L-glutaminyl-Abeta(3-42) peptide
5-oxoprolyl-Abeta(3-42) peptide + NH3
show the reaction diagram
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
show the reaction diagram
-
-
-
?
EFRH-NH2
pEFRH-NH2 + H2O
show the reaction diagram
-
-
-
-
?
EFRHHDSGYE-NH2
pEFRHHDSGYE-NH2 + H2O
show the reaction diagram
-
-
-
-
?
Gln-Gln
pGlu-Gln + NH3
show the reaction diagram
-
-
-
-
?
Gln-Glu
pGlu-Glu + NH3
show the reaction diagram
-
-
-
-
?
Gln-Gly
pGlu-Gly + NH3
show the reaction diagram
-
-
-
-
?
Gln-Gly-Pro
pGlu-Gly-Pro + NH3
show the reaction diagram
-
-
-
-
?
Gln-Phe-Ala
pGlu-Phe-Ala + NH3
show the reaction diagram
-
-
-
-
?
Gln-Tyr-Ala
pGlu-Tyr-Ala + NH3
show the reaction diagram
-
-
-
-
?
L-Gln(3)-amyloid-beta peptide 3-42
L-pyroglutamyl(3)-amyloid-beta peptide 3-42 + NH3
show the reaction diagram
-
-
-
-
?
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
show the reaction diagram
-
-
-
-
?
L-Gln-2-naphthylamide
L-pyroglutamyl-2-naphthylamide + NH3
show the reaction diagram
-
reaction in cell supernatant is exclusively enzyme-catalyzed
-
-
?
L-Glu(3)-amyloid-beta peptide 3-42
L-pyroglutamyl(3)-amyloid-beta peptide 3-42 + H2O
show the reaction diagram
-
-
-
-
?
L-Glu-2-naphthylamide
5-oxo-L-prolinyl-2-naphthylamide + NH3
show the reaction diagram
-
-
-
-
?
L-Glu-2-naphthylamide
5-oxo-L-prolyl-2-naphthylamide + NH3
show the reaction diagram
-
-
-
-
?
L-glutaminyl-7-amido-4-methylcoumarin
pGlu-7-amido-4-methylcoumarin + NH3
show the reaction diagram
-
-
-
-
?
L-glutaminyl-beta-naphthylamide
pGlu-beta-naphthylamide + NH3
show the reaction diagram
-
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
show the reaction diagram
-
-
-
-
?
QEDL
pEEDL + NH3
show the reaction diagram
-
-
-
-
?
QEYF
pEEYF + NH3
show the reaction diagram
-
-
-
-
?
QFRH-NH2
pEFRH-NH2 + NH3
show the reaction diagram
-
-
-
-
?
thyrotropin-releasing hormone
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme is important during cellular maturation of L-pyroglutamyl-containing peptides
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutaminyl-Abeta(3-42) peptide
5-oxoprolyl-Abeta(3-42) peptide + NH3
show the reaction diagram
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
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
show the reaction diagram
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
show the reaction diagram
-
-
-
-
?
thyrotropin-releasing hormone
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme is important during cellular maturation of L-pyroglutamyl-containing peptides
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
stoichiometric amounts of zinc bound to protein. Depletion of zinc has no significant effect on protein structure, metal has a catalytic role
Zn2+
the enzyme contains a catalytic zinc ion
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
time-dependent inactivation
1-Methylimidazole
-
2,6-dipicolinic acid
time-dependent inactivation
2-mercaptoethanol
-
8-hydroxyquinoline
time-dependent inactivation
benzimidazole
-
benzylimidazole
-
Citric acid
inactivation at pH 5.5, Zn2+ protects
cysteamine
ethanolamine
-
ethylamine
-
ethylenediamine
-
ethylmercaptane
-
methylimidazole
-
N-diethylcysteamine
-
N-dimethylcysteamine
-
Nomega-acetylhistamine
-
PBD150
1-(3,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
i.e. P150/03, complete inhibition at 0.01 mM
benzimidazole
-
competitive
benzylimidazole
-
competitive
cysteamine
-
-
EFRH-NH2
-
competitive inhibitor with L-glutaminyl-7-amido-4-methylcumarin as substrate
EFRHHDSGYE-NH2
-
competitive inhibitor with L-glutaminyl-7-amido-4-methylcumarin as substrate
imidazole
-
-
L-glutaminyl-beta-naphthylamide
-
substrate inhibition
methylimidazole
-
-
N,N-dimethylcysteamine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
L-Gln-2-naphthylamide
pH 8.0, 30°C
0.048
L-Gln-7-amido-4-methylcoumarin
pH 8.0, 30°C
0.41
L-Gln-Gly
pH 8.0, 30°C
0.17
L-Gln-Gly-L-Pro
pH 8.0, 30°C
0.4
L-Gln-L-Ala
pH 8.0, 30°C
0.32
L-Gln-L-Arg-Gly-L-Ile-NH2
pH 8.0, 30°C
0.36
L-Gln-L-Asn-Gly-L-Ile-NH2
pH 8.0, 30°C
0.15
L-Gln-L-Gln
pH 8.0, 30°C
0.8
L-Gln-L-Glu
pH 8.0, 30°C
0.16
L-Gln-L-Thr-Gly-L-Ile-NH2
pH 8.0, 30°C
0.072
L-Gln-L-Trp-L-Ala-NH2
pH 8.0, 30°C
0.092
Gln-Gln
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.47
Gln-Glu
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.16
Gln-Gly
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.102
Gln-Gly-Pro
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.06
Gln-Phe-Ala
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.058
Gln-Tyr-Ala
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.03
L-glutaminyl-7-amido-4-methylcoumarin
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.032
L-glutaminyl-beta-naphthylamide
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.16
QEDL
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.029
QEYF
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22
L-Gln-2-naphthylamide
pH 8.0, 30°C
6
L-Gln-7-amido-4-methylcoumarin
pH 8.0, 30°C
12.4
L-Gln-Gly
pH 8.0, 30°C
21.6
L-Gln-Gly-L-Pro
pH 8.0, 30°C
42
L-Gln-L-Ala
pH 8.0, 30°C
34
L-Gln-L-Arg-Gly-L-Ile-NH2
pH 8.0, 30°C
68
L-Gln-L-Asn-Gly-L-Ile-NH2
pH 8.0, 30°C
32
L-Gln-L-Gln
pH 8.0, 30°C
29
L-Gln-L-Glu
pH 8.0, 30°C
23
L-Gln-L-Thr-Gly-L-Ile-NH2
pH 8.0, 30°C
41
L-Gln-L-Trp-L-Ala-NH2
pH 8.0, 30°C
8.66
Gln-Gln
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
7.79
Gln-Glu
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
4.57
Gln-Gly
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
11.4
Gln-Gly-Pro
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
24.1
Gln-Phe-Ala
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
22.9
Gln-Tyr-Ala
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
6.98
L-glutaminyl-7-amido-4-methylcoumarin
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
17.48
L-glutaminyl-beta-naphthylamide
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
6.4
QEDL
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
11.78
QEYF
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
40
QFRH-NH2
-
at pH 6.5
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000019
EFRH-NH2
-
at pH 6.5
95
Gln-Gln
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
16
Gln-Glu
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
28
Gln-Gly
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
111
Gln-Gly-Pro
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
403
Gln-Phe-Ala
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
394
Gln-Tyr-Ala
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
311
L-glutaminyl-7-amido-4-methylcoumarin
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
554
L-glutaminyl-beta-naphthylamide
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
104
QEDL
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
413
QEYF
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
135
QFRH-NH2
-
at pH 6.5
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.58
2-mercaptoethanol
-
0.192
benzimidazole
pH 8.0, 30°C
0.0064
benzylimidazole
pH 8.0, 30°C
0.042
cysteamine
pH 8.0, 30°C
19.3
ethanolamine
-
22
ethylenediamine
-
0.16
imidazole
pH 8.0, 30°C
0.023
methylimidazole
pH 8.0, 30°C
0.0109
N-diethylcysteamine
-
0.029
N-dimethylcysteamine
-
0.000114
PBD150
wild type enzyme, in 50 mM Tris, pH 8.0, at 30°C
0.124
benzimidazole
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.0039
benzylimidazole
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.069
cysteamine
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
8.33 - 35.75
EFRH-NH2
6.1 - 10.4
EFRHHDSGYE-NH2
0.103
imidazole
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
3.55
L-glutaminyl-beta-naphthylamide
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.052
methylimidazole
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
0.027
N,N-dimethylcysteamine
-
protein expressed in Pichia pastoris, pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.2
pH 8.0, 30°C, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
-
for kcat/KM
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
in interneurons and pyramidal cells, not in granule cells
Manually annotated by BRENDA team
-
very low expression
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
very low expression
Manually annotated by BRENDA team
additional information
not in anterodorsal thalamic nucleus, perifornical nucleus, and granule cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
evidence for an involvement of glutaminyl cyclase (QC) in Alzheimer's disease pathogenesis via QC-catalyzed pE-Abeta formation
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
physiological function
-
glutaminyl cyclase contributes to the formation of focal and diffuse diglutamate-Abeta peptide deposits in hippocampus
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
QPCT_MOUSE
362
0
41119
Swiss-Prot
Secretory Pathway (Reliability: 2)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 100 mM sodium acetate (pH 5.3), 200 mM ammonium sulfate, and 12% (w/v) 2000 MME-PEG
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I74N
-
artificial glycosylation site
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
stable for at least 30 min at 30°C, both native and recombinant enzyme. At pH values below or above, rapid inactivation. 0.02 mM ZnSO4 partially prevents denaturation in the acidic range
671982
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
hydrophobic interaction chromatography, ion exchange chromatography, gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
-
modified N-terminal region, His-tagged version, expressed in Pichia pastoris
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
glutaminyl cyclase is a drug target to diminish pE-Abeta formation
pharmacology
glutaminyl cyclase is a drug target to diminish pE-Abeta formation
medicine
-
the enzyme is a pharmacological target for Alzheimer’s disease therapy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schilling, S.; Cynis, H.; von Bohlen, A.; Hoffmann, T.; Wermann, M.; Heiser, U.; Buchholz, M.; Zunkel, K.; Demuth, H.U.
Isolation, catalytic properties, and competitive inhibitors of the zinc-dependent murine glutaminyl cyclase
Biochemistry
44
13415-13424
2005
Mus musculus (Q9CYK2), Mus musculus
Manually annotated by BRENDA team
Cynis, H.; Schilling, S.; Bodnar, M.; Hoffmann, T.; Heiser, U.; Saido, T.C.; Demuth, H.
Inhibition of glutaminyl cyclase alters pyroglutamate formation in mammalian cells
Biochim. Biophys. Acta
1764
1618-1625
2006
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Seifert, F.; Schulz, K.; Koch, B.; Manhart, S.; Demuth, H.U.; Schilling, S.
Glutaminyl cyclases display significant catalytic proficiency for glutamyl substrates
Biochemistry
48
11831-11833
2009
Carica papaya, Homo sapiens, Mus musculus, Solanum tuberosum
Manually annotated by BRENDA team
Stephan, A.; Wermann, M.; Von Bohlen, A.; Koch, B.; Cynis, H.; Demuth, H.; Schilling, S.
Mammalian glutaminyl cyclases and their isoenzymes have identical enzymatic characteristics
FEBS J.
276
6522-6536
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Hartlage-Ruebsamen, M.; Staffa, K.; Waniek, A.; Wermann, M.; Hoffmann, T.; Cynis, H.; Schilling, S.; Demuth, H.U.; Rossner, S.
Developmental expression and subcellular localization of glutaminyl cyclase in mouse brain
Int. J. Dev. Neurosci.
27
825-835
2009
Mus musculus
Manually annotated by BRENDA team
Hartlage-Ruebsamen, M.; Morawski, M.; Waniek, A.; Jaeger, C.; Zeitschel, U.; Koch, B.; Cynis, H.; Schilling, S.; Schliebs, R.; Demuth, H.U.; Rossner, S.
Glutaminyl cyclase contributes to the formation of focal and diffuse pyroglutamate (pGlu)-Abeta deposits in hippocampus via distinct cellular mechanisms
Acta Neuropathol.
121
705-719
2011
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Ruiz-Carrillo, D.; Koch, B.; Parthier, C.; Wermann, M.; Dambe, T.; Buchholz, M.; Ludwig, H.H.; Heiser, U.; Rahfeld, J.U.; Stubbs, M.T.; Schilling, S.; Demuth, H.U.
Structures of glycosylated mammalian glutaminyl cyclases reveal conformational variability near the active center
Biochemistry
50
6280-6288
2011
Homo sapiens (Q16769), Mus musculus (Q9CYK2)
Manually annotated by BRENDA team
Koch, B.; Buchholz, M.; Wermann, M.; Heiser, U.; Schilling, S.; Demuth, H.U.
Probing secondary glutaminyl cyclase (QC) inhibitor interactions applying an in silico-modeling/site-directed mutagenesis approach: implications for drug development
Chem. Biol. Drug Des.
80
937-946
2012
Homo sapiens (Q16769), Mus musculus (Q9CYK2)
Manually annotated by BRENDA team
Waniek, A.; Hartlage-Ruebsamen, M.; Hoefling, C.; Kehlen, A.; Schilling, S.; Demuth, H.U.; Rossner, S.
Identification of thyrotropin-releasing hormone as hippocampal glutaminyl cyclase substrate in neurons and reactive astrocytes
Biochim. Biophys. Acta
1852
146-155
2015
Mus musculus
Manually annotated by BRENDA team
Becker, A.; Eichentopf, R.; Sedlmeier, R.; Waniek, A.; Cynis, H.; Koch, B.; Stephan, A.; Baeuscher, C.; Kohlmann, S.; Hoffmann, T.; Kehlen, A.; Berg, S.; Freyse, E.J.; Osmand, A.; Plank, A.C.; Rossner, S.; von Hoersten, S.; Graubner, S.; Demuth, H.U.; Schilling, S.
IsoQC (QPCTL) knock-out mice suggest differential substrate conversion by glutaminyl cyclase isoenzymes
Biol. Chem.
397
45-55
2016
Mus musculus
Manually annotated by BRENDA team
Hoefling, C.; Indrischek, H.; Hoepcke, T.; Waniek, A.; Cynis, H.; Koch, B.; Schilling, S.; Morawski, M.; Demuth, H.U.; Rossner, S.; Hartlage-Ruebsamen, M.
Mouse strain and brain region-specific expression of the glutaminyl cyclases QC and isoQC
Int. J. Dev. Neurosci.
36
64-73
2014
Mus musculus
Manually annotated by BRENDA team
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
Molecules
23
924
2018
Mus musculus (Q9CYK2)
Manually annotated by BRENDA team