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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

Reaction

L-glutaminyl-peptide
=
5-Oxoprolyl-peptide
 +
NH3

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

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.5 glutaminyl-peptide cyclotransferase

Cloned

Cloned on EC 2.3.2.5 - glutaminyl-peptide cyclotransferase

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into the Escherichia coli expression vectors pMALc2 and pET19b. Expression of this cDNA in either vector results in the production of a glutaminyl cyclase fusion protein which is enzymatically active and reacts with anti-bovine glutaminyl cyclase antisera
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) CodonPlus-RIL cells
expressed in Escherichia coli M15 cells (isoform isoDromeQC)
expressed in HEK-293 cell, expressed in Pichia pastoris
expressed in Pichia pastoris
expressed in Pichia pastoris strain X33
expressed in Pichia pstoris strain X33 (isoform DromeQC)
expression in Drosophila S2 cells
-
expression in Escherichia coli
-
expression in Escherichia coli as either His-tagged enzyme with three different signal peptides and in fusions with three different signal peptides and in fusion with thioredoxin, glutathione S-transferase, and (pre-)maltose-binding protein. In all cases, the expressed protein is either undetectable or insoluble. Expression in Pichia pastoris of the enzyme fused to the alpha-factor leader results in low levels of activity. Extracellular expression of the enzyme in the insect cell/baculovirus system is sucessfull. Enzyme N-terminally fused to a combined secretion signal/His-tag peptide is correctly processed by the host signal peptidase and the His-tag can subsequently be removed with dipeptidyl peptidase I
expression in Pichia pastoris
expression in Pichia pastoris. In Escherichia coli only 50% of the protein does not contain a disulfide bond that is present in the enzyme expressed in Pichia pastoris
-
h-isoQC, lacking the N-terminal signal anchor and the short cytosolic tail, is expressed as a fusion protein in Escherichia coli
-
heterologously expressed in Pichia pastoris and Escherichia coli
modified N-terminal region, His-tagged version, expressed in Pichia pastoris
real-time PCR enzyme expression analysis
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of wild-type and mutant isoQC in isoQC-deficient HEK-293T cells
recombinant expression of wild-type and mutant isozyme sQC
sequence analysis, real-time PCR enzyme expression analysis
-
transcriptomic analysis, DNA and amino acid sequence determination and analysis, sequence comparisons