2.3.2.5: glutaminyl-peptide cyclotransferase
This is an abbreviated version!
For detailed information about glutaminyl-peptide cyclotransferase, go to the full flat file.
Word Map on EC 2.3.2.5
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2.3.2.5
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pyroglutamate
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alzheimer
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cyclases
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pyroglutamyl
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papaya
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pyroglutamate-modified
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pglu-a
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medicine
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drug development
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antivenomics
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pharmacology
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n-truncated
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cd47-sirp
- 2.3.2.5
- pyroglutamate
- alzheimer
- cyclases
-
pyroglutamyl
- papaya
-
pyroglutamate-modified
-
pglu-a
- medicine
- drug development
-
antivenomics
- pharmacology
-
n-truncated
-
cd47-sirp
Reaction
Synonyms
AtQC, cyclotransferase, glutaminyl-transfer ribonucleate, DromeQC, gamma-glutamylamine cyclotransferase, GGACT, glutamine cyclotransferase, glutaminyl cyclase, glutaminyl-peptide cyclotransferase-like protein, glutaminyl-tRNA cyclotransferase, golgi resident enzyme, Golgi resident glutaminyl cyclase, Golgi-resident enzyme, Golgi-resident glutaminyl cyclase, gQC, h-isoQC, h-QC, hQC, isoDromeQC, isoGlutaminyl cyclase, isoQC, PgQC, QC, QCT, Qpct, Qpct1, QPCTL, secretory glutaminyl cyclase, sQC, StQC
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Metals Ions
Metals Ions on EC 2.3.2.5 - glutaminyl-peptide cyclotransferase
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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
Zn2+
involved in catalysis, the Zn2+ ion located at the active site of QC polarizes the gamma-amide group of the substrate Gln residue and stabilizes the oxyanion formed by the nucleophilic attack of the alpha-nitrogen on the scissile gamma-carbonyl carbon
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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
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
additional information
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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
additional information
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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