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Information on EC 2.3.2.5 - glutaminyl-peptide cyclotransferase and Organism(s) Boiga dendrophila and UniProt Accession A7ISW2

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EC Tree
     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:
Boiga dendrophila
UNIPROT: A7ISW2
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Word Map
The taxonomic range for the selected organisms is: Boiga dendrophila
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
cyclotransferase, glutaminyl-transfer ribonucleate
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glutaminyl cyclase
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glutaminyl-tRNA cyclotransferase
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QC
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminoacyl group transfer
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PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
37257-21-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
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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
additional information
?
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
QPCT_BOIDE
368
0
41990
Swiss-Prot
Secretory Pathway (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
sequence contain potential N-glycosylation sites at Asn53, Asn292, and Asn352
proteolytic modification
sequence contains an ambiguous signal peptide cleavage site leading to a mature enzyme of 345, 340 or 335 amino acids
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pawlak, J.; Manjunatha Kini, R.
Snake venom glutaminyl cyclase
Toxicon
48
278-286
2006
Boiga dendrophila (A7ISW2), Boiga dendrophila, Boiga irregularis (A7ISW1), Boiga irregularis
Manually annotated by BRENDA team