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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Posttranslational Modification
Posttranslational Modification on EC 2.3.2.5 - glutaminyl-peptide cyclotransferase
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glycoprotein
proteolytic modification
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treatment of recombinant enzyme with endoglycosidase H results in decrease of mass by 2 kDa. Deglycosylated enzyme has similar kinetic parameters for conversion of Gln-Gln and Gln-7-amido-4-methylcoumarin as native enzyme
glycoprotein
sequence contain potential N-glycosylation sites at Asn53, Asn292, and Asn352
glycoprotein
sequence contain potential N-glycosylation sites at Asn53, Asn292, and Asn352
glycoprotein
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presence of terminal mannose residues, mannose and N-acetylglucosamine in a 3:1 molar ratio
glycoprotein
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N-glycan sugar moiety is bound to Asn49 in the recombinant enzyme. Presence or absence of glycan has no apparent effect on structure, stability, or enzymatic activity of the enzyme
glycoprotein
glycosylated structures of sQC are reported in PDB which exhibit divergence in the structures especially at the loop regions constituted by F146-V153 and Q295-I303. A disulfide bridge between C139 and C164 has also been observed in the glycosylated sQC. In the glycosylated structures, the position of W207 resembles the enzyme structure Conf-B
glycoprotein
treatment of recombinant enzyme with endoglycosidase H results in decrease of mass by 2 kDa. Deglycosylated enzyme has similar kinetic parameters for conversion of Gln-Gln and Gln-7-amido-4-methylcoumarin as native enzyme
sequence contains an ambiguous signal peptide cleavage site leading to a mature enzyme of 345, 340 or 335 amino acids
proteolytic modification
sequence contains an ambiguous signal peptide cleavage site leading to a mature enzyme of 345, 340 or 335 amino acids