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Enzyme Nomenclature
Information on EC 2.3.2.5 - glutaminyl-peptide cyclotransferase
for references in articles please use BRENDA:EC2.3.2.5
Word Map on EC 2.3.2.5
- 2.3.2.5
- pyroglutamate
- alzheimer
-
cyclization
-
amyloid
-
pyroglutamyl
-
cyclases
- papaya
-
abeta
-
pyroglutamate-modified
-
carica
- beta-secretase
- medicine
- drug development
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.3.2.5
-
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RECOMMENDED NAME
GeneOntology No.
glutaminyl-peptide cyclotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3
-
-
-
-
L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3
general acid/base working mechanism, pivoting around a strictly conserved glutamate
-
L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3
DFT theoretical investigation on the catalytic mechanism of glutaminyl cyclase
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aminoacyl group transfer
aminoacyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
37257-21-9
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
G3MGU0;
knockdown of enzyme-transcript results in lower enzymatic activity, and small, unviable egg masses
malfunction
-
knockdown of enzyme-transcript results in lower enzymatic activity, and small, unviable egg masses
physiological function
-
glutaminyl cyclase contributes to the formation of focal and diffuse diglutamate-Abeta peptide deposits in hippocampus
physiological function
-
glutaminyl cyclase contributes to the formation of focal and diffuse diglutamate-Abeta peptide deposits in hippocampus
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amyloid peptide Abeta(3-40/42)
pGluAbeta(3-40/42) + H2O
-
-
significant portion of Abeta peptides of amyloid plaques in Alzheimer's disease brains
-
?
Gln-7-amido-4-methylcoumarin
L-pyroglutamyl-4-methylcoumarin-7-amide + NH3
-
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
pyroglutamate-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
L-Gln-L-Arg-Gly-L-Ile-NH2
pyroglutamyl-L-Arg-Gly-L-Ile-NH2 + NH3
-
-
-
?
L-Gln-L-Asn-Gly-L-Ile-NH2
L-pyroglutamyl-L-Asn-Gly-L-Ile-NH2 + NH3
-
-
-
?
L-Gln-L-Glu-L-Tyr-L-Ala-NH2
pyroglutamic acid-L-Glu-L-Tyr-L-Ala-NH2 + NH3
M1AKD0;
-
-
-
?
L-Gln-L-Lys-L-Arg-L-Leu
5-oxoprolyl-L-Lys-L-Arg-L-Leu + NH3
-
-
-
?
L-Gln-L-Phe-L-Ala
5-oxoprolyl-L-Phe-L-Ala + NH3
-
-
-
?
L-Gln-L-Ser-L-Tyr-L-Phe-NH2
pyroglutamic acid-L-Ser-L-Tyr-L-Phe-NH2 + NH3
M1AKD0;
-
-
-
?
L-Gln-L-Thr-Gly-L-Ile-NH2
L-pyroglutamyl-L-Thr-Gly-L-Ile-NH2 + NH3
-
-
-
?
L-glutamine tert-butyl ester
L-pyroglutamate tert-butyl ester + NH3
-
-
-
-
?
L-glutaminyl-4-methylcoumarinylamide
L-5-oxoprolyl-4-methylcoumarinylamide + NH3
-
-
-
-
-
Nepsilon-(L-gamma-glutamyl)-L-lysine
5-oxoprolyl-L-lysine + NH3
-
-
-
-
?
[Gln1]-fertilization promoting peptide
[pyroglutamyl]-fertilization promoting peptide + NH3
[Gln1]-thyrotropin releasing-hormone
[pyroglutamyl]-thyrotropin releasing-hormone + NH3
-
-
-
-
?
Gln-7-amido-4-methylcoumarin
pyroglutamic acid-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
Gln-7-amido-4-methylcoumarin
pyroglutamic acid-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
Gln-Ala-Ala-Ser-Ala-Ala-NH2
pyroglutamic acid-Ala-Ala-Ser-Ala-Ala-NH2 + NH3
-
-
-
-
?
Gln-Ala-Ala-Ser-Ala-Ala-NH2
pyroglutamic acid-Ala-Ala-Ser-Ala-Ala-NH2 + NH3
-
-
-
-
?
Gln-tert-butyl ester
pyroglutamyl-tert-butyl ester + NH3
-
-
-
-
?
H-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
H-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
H-Gln-Asp-Glu-Leu-NH2
5-oxoprolyl-Asp-Glu-Leu-NH2 + NH3
-
-
-
?
H-Gln-Asp-Glu-Leu-NH2
5-oxoprolyl-Asp-Glu-Leu-NH2 + NH3
isoDromeQC
-
-
?
H-Gln-beta-naphthylamide
5-oxoprolyl-beta-naphthylamide + NH3
-
-
-
?
H-Gln-beta-naphthylamide
5-oxoprolyl-beta-naphthylamide + NH3
isoDromeQC
-
-
?
H-Gln-beta-naphthylamide
5-oxoprolyl-beta-naphthylamide + NH3
M1AKD0;
-
-
-
?
H-Gln-Glu-Ala-Phe-NH2
5-oxoprolyl-Glu-Ala-Phe-NH2 + NH3
-
-
-
?
H-Gln-Glu-Ala-Phe-NH2
5-oxoprolyl-Glu-Ala-Phe-NH2 + NH3
isoDromeQC
-
-
?
H-Gln-Glu-Tyr-Phe-NH2
5-oxoprolyl-Glu-Tyr-Phe-NH2 + NH3
-
-
-
?
H-Gln-Glu-Tyr-Phe-NH2
5-oxoprolyl-Glu-Tyr-Phe-NH2 + NH3
isoDromeQC
-
-
?
H-Gln-Gly-Pro-OH
5-oxoprolyl-Gly-Pro-OH + NH3
isoDromeQC
-
-
?
H-Gln-Lys-Arg-Leu-NH2
5-oxoprolyl-Lys-Arg-Leu-NH2 + NH3
-
-
-
?
H-Gln-Lys-Arg-Leu-NH2
5-oxoprolyl-Lys-Arg-Leu-NH2 + NH3
isoDromeQC
-
-
?
H-Gln-Phe-Ala-OH
5-oxoprolyl-Phe-Ala-OH + NH3
isoDromeQC
-
-
?
H-Gln-Tyr-Ala-OH
5-oxoprolyl-Tyr-Ala-OH + NH3
isoDromeQC
-
-
?
H-Gln-Val-Ala-OH
5-oxoprolyl-Val-Ala-OH + NH3
isoDromeQC
-
-
?
L-Gln(3)-amyloid-beta peptide 3-42
L-pyroglutamyl(3)-amyloid-beta peptide 3-42 + NH3
-
-
-
-
?
L-Gln(3)-amyloid-beta peptide 3-42
L-pyroglutamyl(3)-amyloid-beta peptide 3-42 + NH3
-
-
-
-
?
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
-
-
-
?
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
-
-
-
?
L-Gln-2-naphthylamide
5-oxoprolyl-2-naphthylamide + NH3
-
-
-
?
L-Gln-2-naphthylamide
L-pyroglutamyl-2-naphthylamide + NH3
-
reaction in cell supernatant is exclusively enzyme-catalyzed
-
-
?
L-Gln-2-naphthylamide
L-pyroglutamyl-2-naphthylamide + NH3
-
reaction in cell supernatant is exclusively enzyme-catalyzed
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-4-methylcoumarin-7-amide + NH3
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-4-methylcoumarin-7-amide + NH3
isoDromeQC
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
5-oxoprolyl-7-amido-4-methylcoumarin + NH3
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
L-pyroglutamyl-4-methylcoumarin-7-amide + NH3
-
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
L-pyroglutamyl-4-methylcoumarin-7-amide + NH3
-
-
-
?
L-Gln-7-amido-4-methylcoumarin
L-pyroglutamyl-4-methylcoumarin-7-amide + NH3
M1AKD0;
-
-
-
?
L-Gln-L-Asp-L-Glu-L-Leu-NH2
pyroglutamyl-L-Asp-L-Glu-L-Leu-NH2 + NH3
-
-
-
-
?
L-Gln-L-Asp-L-Glu-L-Leu-NH2
pyroglutamyl-L-Asp-L-Glu-L-Leu-NH2 + NH3
M1AKD0;
-
-
-
?
L-Gln-L-Glu-L-Ala-L-Phe-NH2
pyroglutamyl-L-Glu-L-Ala-L-Phe-NH2 + NH3
-
-
-
-
?
L-Gln-L-Glu-L-Ala-L-Phe-NH2
pyroglutamyl-L-Glu-L-Ala-L-Phe-NH2 + NH3
M1AKD0;
-
-
-
?
L-Gln-L-Glu-L-Asp-L-Leu-NH2
5-oxoprolyl-L-Glu-L-Asp-L-Leu-NH2 + NH3
-
-
-
?
L-Gln-L-Glu-L-Tyr-L-Phe-NH2
pyroglutamyl-L-Glu-L-Tyr-L-Phe-NH2 + NH3
-
-
-
-
?
L-Gln-L-Glu-L-Tyr-L-Phe-NH2
pyroglutamyl-L-Glu-L-Tyr-L-Phe-NH2 + NH3
M1AKD0;
-
-
-
?
L-Gln-L-Lys-L-Arg-L-Leu-NH2
pyroglutamyl-L-Lys-L-Arg-L-Leu-NH2 + NH3
-
-
-
-
?
L-Gln-L-Lys-L-Arg-L-Leu-NH2
pyroglutamyl-L-Lys-L-Arg-L-Leu-NH2 + NH3
M1AKD0;
-
-
-
?
L-Gln-tert-butyl ester
L-pyroglutamyl-tert-butyl ester + NH3
M1AKD0;
-
-
-
?
L-Glu(3)-amyloid-beta peptide 3-42
L-pyroglutamyl(3)-amyloid-beta peptide 3-42 + H2O
-
-
-
-
?
L-Glu(3)-amyloid-beta peptide 3-42
L-pyroglutamyl(3)-amyloid-beta peptide 3-42 + H2O
-
-
-
-
?
L-Glu-2-naphthylamide
5-oxo-L-prolyl-2-naphthylamide + NH3
G3MGU0;
-
-
-
?
L-glutaminyl-7-amido-4-methylcoumarin
pGlu-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
L-glutaminyl-7-amido-4-methylcoumarin
pGlu-7-amido-4-methylcoumarin + NH3
-
-
-
-
?
L-glutaminyl-amyloid beta peptide
5-oxoprolyl-amyloid beta peptide + NH3
-
-
-
-
?
L-glutaminyl-amyloid beta peptide
5-oxoprolyl-amyloid beta peptide + NH3
-
-
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
thyrotropin-releasing hormone
-
-
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
thyrotropin-releasing hormone
-
-
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
Gln-His-Pro-Glythyrotropin-releasing hormone, gonadotropin-releasing hormone and L-Gln-Tyr-Ala
-
-
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
the enzyme may participate in the posttranslational processing of hormonal precursors to pyroglutamyl peptides
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
involved in posttranslational modification of the N-terminal glutamine of peptide hormones or neurotransmitters, such as thyrotropin releasing hormone, luteinizing hormone releasing hormone, gastrin, heavy chain of gamma-globulin
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
simple intramolecular cyclization. The mechanism consists of the following main steps: 1. intramolecular nucleophilic attack on the gamma-C=O carbon by the nitrogen of the alpha-amino group, 2. transfer of a proton from the alpha-amino group to the nitrogen of the amide group, facilitated by an acidic group of the enzyme, 3. expulsion of the ammonia-leaving group promoted by this or another acidic enzyme group
-
-
-
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
thyrotropin-releasing hormone
-
-
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
the N-terminal formation of 5-oxoproline is a common post-translational event during biosynthesis of a number of peptides
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
involved in posttranslational modification of the N-terminal glutamine of peptide hormones or neurotransmitters, such as thyrotropin releasing hormone, luteinizing hormone releasing hormone, gastrin, heavy chain of gamma-globulin
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
thyrotropin-releasing hormone
-
-
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
thyrotropin-releasing hormone
-
-
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
Gln-His-Pro-Glythyrotropin-releasing hormone, gonadotropin-releasing hormone and L-Gln-Tyr-Ala
-
-
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
involved in posttranslational modification of the N-terminal glutamine of peptide hormones or neurotransmitters, such as thyrotropin releasing hormone, luteinizing hormone releasing hormone, gastrin, heavy chain of gamma-globulin
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
thyrotropin-releasing hormone
-
-
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
involved in posttranslational modification of the N-terminal glutamine of peptide hormones or neurotransmitters, such as thyrotropin releasing hormone, luteinizing hormone releasing hormone, gastrin, heavy chain of gamma-globulin
-
-
?
[Gln1]-fertilization promoting peptide
[pyroglutamyl]-fertilization promoting peptide + NH3
-
-
-
-
?
[Gln1]-fertilization promoting peptide
[pyroglutamyl]-fertilization promoting peptide + NH3
-
-
-
-
?
[Gln1]-gonadotropin releasing-hormone
[pyroglutamyl]-gonadotropin releasing-hormone + NH3
-
-
-
-
?
[Gln1]-gonadotropin releasing-hormone
[pyroglutamyl]-gonadotropin releasing-hormone + NH3
-
-
-
-
?
additional information
?
-
-
highest specificities are observed with substrates possessing large hydrophobic residues adjacent to the N-terminal glutamine and for fluorogenic dipeptide surrogates. Enzyme also catalyzes the conversion of N-terminal glutamic acid residues to pyroglutamic acid, but with about 100000fold lower specificity
-
-
-
additional information
?
-
enzyme is involved in N-terminal pyroglutamate formation of snake venom toxins
-
-
-
additional information
?
-
-
enzyme is involved in N-terminal pyroglutamate formation of snake venom toxins
-
-
-
additional information
?
-
enzyme is involved in N-terminal pyroglutamate formation of snake venom toxins
-
-
-
additional information
?
-
-
enzyme is involved in N-terminal pyroglutamate formation of snake venom toxins
-
-
-
additional information
?
-
-
no substrates are D-Gln-Tyr-Ala and Lys-Arg-Gln-His-Pro-Gly-Lys-Arg, i.e. thyrotropin releasing hormone precursor
-
-
-
additional information
?
-
-
Cys residues do not participate to the catalytic events
-
-
-
additional information
?
-
-
the second amino acid residue in N-terminal glutaminyl peptides significantly accelerates activity while the third residue provides no further rate enhancement. Substrate binding is the main specificity-determining step
-
-
-
additional information
?
-
-
the enzyme may play a key role in posttranslational modification
-
-
-
additional information
?
-
-
the enzyme may play a key role in posttranslational modification
-
-
-
additional information
?
-
-
enzyme is important during cellular maturation of L-pyroglutamyl-containing peptides
-
-
-
additional information
?
-
-
catalyzes the formation of amyloid-beta3(pE)-40/42 after amyloidogenic processing of amyloid precursor protein
-
-
-
additional information
?
-
-
enzyme is important during cellular maturation of L-pyroglutamyl-containing peptides
-
-
-
additional information
?
-
the enzyme shows no activity towards L-Gln-Gly
-
-
-
additional information
?
-
-
the enzyme does not act on L-2-amino-3-(3-n-butylureido)-propionic acid, L-glutamine, L-gamma-glutamyl-L-lysine, L-gamma-glutamyl-L-methionine, or L-gamma-glutamyl-L-glutamine
-
-
-
additional information
?
-
-
no substrates are D-Gln-Tyr-Ala and Lys-Arg-Gln-His-Pro-Gly-Lys-Arg, i.e. thyrotropin releasing hormone precursor
-
-
-
additional information
?
-
M1AKD0;
highest specificities are observed with substrates possessing large hydrophobic residues adjacent to the N-terminal glutamine and for fluorogenic dipeptide surrogates. Enzyme also catalyzes the conversion of N-terminal glutamic acid residues to pyroglutamic acid, but with about 100000fold lower specificity
-
-
-
additional information
?
-
-
highest specificities are observed with substrates possessing large hydrophobic residues adjacent to the N-terminal glutamine and for fluorogenic dipeptide surrogates. Enzyme also catalyzes the conversion of N-terminal glutamic acid residues to pyroglutamic acid, but with about 100000fold lower specificity
-
-
-
additional information
?
-
the enzyme shows no activity towards QAAR
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
the enzyme may participate in the posttranslational processing of hormonal precursors to pyroglutamyl peptides
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
involved in posttranslational modification of the N-terminal glutamine of peptide hormones or neurotransmitters, such as thyrotropin releasing hormone, luteinizing hormone releasing hormone, gastrin, heavy chain of gamma-globulin
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
the N-terminal formation of 5-oxoproline is a common post-translational event during biosynthesis of a number of peptides
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
involved in posttranslational modification of the N-terminal glutamine of peptide hormones or neurotransmitters, such as thyrotropin releasing hormone, luteinizing hormone releasing hormone, gastrin, heavy chain of gamma-globulin
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
involved in posttranslational modification of the N-terminal glutamine of peptide hormones or neurotransmitters, such as thyrotropin releasing hormone, luteinizing hormone releasing hormone, gastrin, heavy chain of gamma-globulin
-
-
?
L-glutaminyl-peptide
5-oxoprolyl-peptide + NH3
-
involved in posttranslational modification of the N-terminal glutamine of peptide hormones or neurotransmitters, such as thyrotropin releasing hormone, luteinizing hormone releasing hormone, gastrin, heavy chain of gamma-globulin
-
-
?
additional information
?
-
A7ISW2
enzyme is involved in N-terminal pyroglutamate formation of snake venom toxins
-
-
-
additional information
?
-
-
enzyme is involved in N-terminal pyroglutamate formation of snake venom toxins
-
-
-
additional information
?
-
A7ISW1
enzyme is involved in N-terminal pyroglutamate formation of snake venom toxins
-
-
-
additional information
?
-
-
enzyme is involved in N-terminal pyroglutamate formation of snake venom toxins
-
-
-
additional information
?
-
-
the enzyme may play a key role in posttranslational modification
-
-
-
additional information
?
-
-
the enzyme may play a key role in posttranslational modification
-
-
-
additional information
?
-
-
enzyme is important during cellular maturation of L-pyroglutamyl-containing peptides
-
-
-
additional information
?
-
-
enzyme is important during cellular maturation of L-pyroglutamyl-containing peptides
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
enzyme inactivated by 1,10-phenanthroline or dipicolinic acid can be restored partially by Co2+ or Mn2+
Mn2+
-
enzyme inactivated by 1,10-phenanthroline or dipicolinic acid can be restored partially by Co2+ or Mn2+
Zinc
Zn2+
additional information
Zinc
stoichiometric amounts of zinc bound to protein. Depletion of zinc has no significant effect on protein structure, metal has a catalytic role
Zn2+
-
enzyme inactivated by 1,10-phenanthroline or dipicolinic acid can be fully restored by addition of Zn2+ in the presence of equimolar concentrations of EDTA
Zn2+
-
the active site is coordinated to three conserved residues and one water molecule, which is replaced by an imidazole nitrogen upon binding of inhibitor
additional information
-
substrate specificity for substrates with uncharged backbone and for Gln-Ala and Gln-Glu, does not change significantly by salt addition. With the positively charged substrates Gln-Arg-Gly-Ile-NH2 and Gln-Lys-Arg-Leu-NH2 addition of salt reveals a positive effect on catalysis
additional information
-
substrate specificity for substrates with uncharged backbone does not change significantly by salt addition. For substrates such as Gln-Ala and Gln-Glu, addition of KCl decreases specificity. With the positively charged substrates Gln-Arg-Gly-Ile-NH2 and Gln-Lys-Arg-Leu-NH2 addition of salt reveals a positive effect on catalysis
additional information
-
human glutaminyl cyclase and bacterial zinc aminopeptidase share a common fold and active site. Glutaminyl cyclase does not appear to require zinc for enzymatic activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3,4-dichlorophenyl)-2-cyano-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)guanidine
-
-
(3-(1H-imidazol-1-yl)propyl)-2-cyano-3-(2,3-dihydrobenzo[b][1,4]dioxin-7-yl)guanidine
-
-
(3-(4-methyl-1H-imidazol-1-yl)propyl)-2-cyano-3-(2,3-dihydrobenzo[b][1,4]dioxin-7-yl)guanidine
-
-
(3-(5-methyl-1H-imidazol-1-yl)propyl)-2-cyano-3-(2,3-dihydrobenzo[b][1,4]dioxin-7-yl)guanidine
-
-
1-(3,4-dimethoxyphenyl)-3-(2-[1-(1H-imidazol-1-yl)cyclopropyl]ethyl)thiourea
-
-
1-(3,4-dimethoxyphenyl)-N-(3-(4-methyl-1H-imidazol-1-yl)propyl)cyclopropanecarbothioamide
-
-
1-(3,4-dimethoxyphenyl)-N-(3-(5-methyl-1H-imidazol-1-yl)propyl)cyclopropanecarbothioamide
-
-
2,3-dihydro-3-(3-(4-methyl-1H-imidazol-1-yl)propyl)-2-thioxoquinazolin-4(1H)-one
-
-
2,3-dihydro-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)-2-thioxoquinazolin-4(1H)-one
-
-
2,3-dihydro-6-methyl-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)-5-phenyl-2-thioxothieno[2,3-d]pyrimidin-4(1H)-one
-
-
2-cyano(3,4,5-trimethoxyphenyl)-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)guanidine
-
-
2-cyano(3-(5-methyl-1H-imidazol-1-yl)propyl)-3-(3,4-dimethylphenyl)guanidine
-
-
3-(3-(1H-imidazol-1-yl)propyl)-2,3-dihydro-7-methyl-2-thioxothieno[3,2-d]pyrimidin-4(1H)-one
-
-
3-[3-(1H-imidazol-1-yl)propyl]-2-thioxo-1,2,3,5,6,7-hexahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-4-one
-
-
3-[3-(1H-imidazol-1-yl)propyl]-2-thioxo-2,3,5,6,7,8,9,10-octahydrocycloocta[4,5]thieno[2,3-d]pyrimidin-4(1H)-one
-
-
3-[3-(1H-imidazol-1-yl)propyl]-2-thioxo-2,3,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-4(1H)-one
-
-
3-[3-(5-methyl-1H-imidazol-1-yl)propyl]-2-thioxo-2,3,5,6,7,8,9,10-octahydrocycloocta[4,5]-thieno[2,3-d]pyrimidin-4(1H)-one
-
-
3-[3-(5-methyl-1H-imidazol-1-yl)propyl]-2-thioxo-2,3,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-4(1H)-one
-
-
6-benzyl-2,3-dihydro-3-(3-(5-methyl-1H-imidazol-1-yl)propyl)-2-thioxothieno[2,3-d]pyrimidin-4(1H)-one
-
-
diethyl dicarbonate
-
rapid inactivation by modification of three essential His residues, at neutral pH, partial reactivation with hydroxylamine
L-glutamine-4-nitroanilide
substrate inhibition; substrate inhibition, isoDromeQC
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-2,3-dihydrobenzo[b][1,4]-dioxin-6-amine
-
-
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-3,4-dimethoxy-benzenamine
-
-
N-(1-(3-(1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-4-(trifluoromethyl)-benzenamine
-
-
N-(1-(3-(4-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-2,3-dihydrobenzo[b][1,4]-dioxin-6-amine
-
-
N-(1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-2,3-dihydrobenzo[b][1,4]-dioxin-6-amine
-
-
N-(1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-4-(trifluoromethyl)benzenamine
-
-
N-(1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)-4-chloro-benzenamine
-
-
N-(1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)cyclohexanamine
-
-
N-(1-(3-(5-methyl-1H-imidazol-1-yl)propylamino)-2-nitrovinyl)naphthalen-1-amine
-
-
N-(4-chlorophenyl)-N'-[2-(1H-imidazol-1-yl)propyl]-2-thioxoimidazolidin-4-one
-
-
1,10-phenanthroline
-
inactivated enzyme can be fully restored by addition of Zn2+ in the presence of equimolar concentrations of EDTA, little reactivation by Co2+ and Mn2+
1-(3,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
i.e. P150/03, complete inhibition at 0.01 mM
1-(3,4-dimethoxyphenyl)-3-[3-(1H-imidazol-1-yl)propyl]thiourea
-
i.e. P150/03, complete inhibition at 0.01 mM
dipicolinic acid
-
inactivated enzyme can be fully restored by addition of Zn2+ in the presence of equimolar concentrations of EDTA, little reactivation by Co2+ and Mn2+
EFRH-NH2
-
competitive inhibitor with L-glutaminyl-7-amido-4-methylcumarin as substrate
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
EFRHHDSGYE-NH2
-
competitive inhibitor with L-glutaminyl-7-amido-4-methylcumarin as substrate
PBD150
potent competitive inhibitor, i.e. 1-(3,4-dimethoxyphenyl)-3-(3-imidazol-1-ylpropyl)thiourea; potent competitive inhibitor, i.e. 1-(3,4-dimethoxyphenyl)-3-(3-imidazol-1-ylpropyl)thiourea
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
the enzymatic activity increases by about 55% in the presence of 1 mM EDTA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.24
2-amino-5-(butan-2-ylamino)-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.32
2-amino-5-(cyclohexylamino)-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.22
2-amino-5-(cyclopropylamino)-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.69
2-amino-5-oxo-5-(propan-2-ylamino)pentanoic acid
-
pH and temperature not specified in the publication
0.44
2-amino-5-oxo-5-[(2-phenylethyl)amino]pentanoic acid
-
pH and temperature not specified in the publication
0.38
2-amino-5-[(2-methylbutyl)amino]-5-oxopentanoic acid
-
pH and temperature not specified in the publication
1.62
2-amino-5-[(2S)-butan-2-ylamino]-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.38
2-amino-5-[[(2S)-2-methylbutyl]amino]-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.14
L-gamma-glutamyl-(+)-3-aminobutyric acid
-
pH and temperature not specified in the publication
0.33
L-gamma-glutamyl-(+)-3-aminoisobutyric acid
-
pH and temperature not specified in the publication
0.91
L-gamma-glutamyl-beta-alanine
-
pH and temperature not specified in the publication
0.36
L-gamma-glutamyl-ethylamine
-
pH and temperature not specified in the publication
0.25
L-gamma-glutamyl-n-butylamine
-
pH and temperature not specified in the publication
0.32
L-gamma-glutamyl-n-propylamine
-
pH and temperature not specified in the publication
0.1
L-gamma-glutamylaniline
-
pH and temperature not specified in the publication
0.56
L-gamma-glutamylbenzylamine
-
pH and temperature not specified in the publication
0.084
L-gamma-glutamylcyclopentylamine
-
pH and temperature not specified in the publication
1.9
L-gamma-glutamylglycine
-
pH and temperature not specified in the publication
0.12
L-gamma-glutamylneohexylamine
-
pH and temperature not specified in the publication
0.61
L-gamma-glutamylneopentylamine
-
pH and temperature not specified in the publication
0.06
L-glutaminyl-2-naphthylamide
-
30°C, recombinant enzyme, expressed in Pichia pastoris
0.051
L-glutaminyl-4-methylcoumarinylamide
-
30°C, recombinant enzyme, expressed in Pichia pastoris
0.27
Nepsilon-(L-gamma-glutamyl)-D-lysine
-
pH and temperature not specified in the publication
0.26
Nepsilon-(L-gamma-glutamyl)-L-lysine
-
pH and temperature not specified in the publication
20
O-(n-butylcarbamyl)-L-serine
-
pH and temperature not specified in the publication
0.4
QAAR
in 0.1 M MES, pH 7.5, temperature not specified in the publication
0.19
S-(cyclohexylamine)-L-cysteine
-
pH and temperature not specified in the publication
0.091
S-(n-butylcarbamyl)-L-cysteine
-
pH and temperature not specified in the publication
0.093
S-(n-propylcarbamyl)-L-cysteine
-
pH and temperature not specified in the publication
0.087
Gln(3)-amyloid-beta peptide 3-11 amide
-
pH 6.0, 30°C, in absence of DMSO
-
0.11
Gln-Gln
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions
0.61
Gln-Glu
-
protein version: shortened N-terminus, I73N/C369A, His-tagged, pH 8.0, 30°C, similar value with other protein versions