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Literature summary for 2.3.2.5 extracted from

  • Vijayasarathy, M.; Basheer, S.M.; Balaram, P.
    Cone snail glutaminyl cyclase sequences from transcriptomic analysis and mass spectrometric characterization of two pyroglutamyl conotoxins (2018), J. Proteome Res., 17, 2695-2703 .
    View publication on PubMed
Search for more literature for 2.3.2.5

Cloned(Commentary)

Cloned (Comment) Organism
transcriptomic analysis, DNA and amino acid sequence determination and analysis, sequence comparisons Conus araneosus
transcriptomic analysis, DNA and amino acid sequence determination and analysis, sequence comparisons Conus frigidus
transcriptomic analysis, DNA and amino acid sequence determination and analysis, sequence comparisons Conus litteratus
transcriptomic analysis, DNA and amino acid sequence determination and analysis, sequence comparisons Conus monile
transcriptomic analysis, DNA and amino acid sequence determination and analysis, sequence comparisons Conus amadis
transcriptomic analysis, DNA and amino acid sequence determination and analysis, sequence comparisons Conus miles

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Conus araneosus
-
-
extracellular the enzyme is secreted Conus frigidus
-
-
extracellular the enzyme is secreted Conus litteratus
-
-
extracellular the enzyme is secreted Conus monile
-
-
extracellular the enzyme is secreted Conus amadis
-
-
extracellular the enzyme is secreted Conus miles
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutaminyl-peptide Conus araneosus
-
 5-oxoprolyl-peptide + NH3
-
 ?
L-glutaminyl-peptide Conus frigidus
-
 5-oxoprolyl-peptide + NH3
-
 ?
L-glutaminyl-peptide Conus litteratus
-
 5-oxoprolyl-peptide + NH3
-
 ?
L-glutaminyl-peptide Conus monile
-
 5-oxoprolyl-peptide + NH3
-
 ?
L-glutaminyl-peptide Conus amadis
-
 5-oxoprolyl-peptide + NH3
-
 ?
L-glutaminyl-peptide Conus miles
-
 5-oxoprolyl-peptide + NH3
-
 ?

Organism

Organism UniProt Comment Textmining
Conus amadis A0A2D1P884
-
-
Conus araneosus A0A2D1P8A3
-
-
Conus frigidus A0A2D1P886
-
-
Conus litteratus A0A2D1P881
-
-
Conus miles A0A2D1P885
-
-
Conus monile A0A2D1P879
-
-

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Conus araneosus
-
venom
-
 Conus frigidus
-
venom
-
 Conus litteratus
-
venom
-
 Conus monile
-
venom
-
 Conus amadis
-
venom
-
 Conus miles
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutaminyl-peptide
-
 Conus araneosus 5-oxoprolyl-peptide + NH3
-
 ?
L-glutaminyl-peptide
-
 Conus frigidus 5-oxoprolyl-peptide + NH3
-
 ?
L-glutaminyl-peptide
-
 Conus litteratus 5-oxoprolyl-peptide + NH3
-
 ?
L-glutaminyl-peptide
-
 Conus monile 5-oxoprolyl-peptide + NH3
-
 ?
L-glutaminyl-peptide
-
 Conus amadis 5-oxoprolyl-peptide + NH3
-
 ?
L-glutaminyl-peptide
-
 Conus miles 5-oxoprolyl-peptide + NH3
-
 ?

Synonyms

Synonyms Comment Organism
glutaminyl cyclase
-
 Conus araneosus
glutaminyl cyclase
-
 Conus frigidus
glutaminyl cyclase
-
 Conus litteratus
glutaminyl cyclase
-
 Conus monile
glutaminyl cyclase
-
 Conus amadis
glutaminyl cyclase
-
 Conus miles

General Information

General Information Comment Organism
physiological function diglutamic acid (5-oxo-L-proline, pGlu, Z) formation at the N-terminus of proteins and peptides, a modification observed in both plant and animal kingdoms, requires the action of the enzyme glutaminyl cyclase (QC), which acts on amino terminus glutamine residues. The post-translational modification of N-terminal glutamine (Q) to a diglutamyl (Z) residue is observed in the conotoxins produced by marine cone snails. This conversion requires the action of the enzyme glutaminyl cyclase (QC). Mass spectrometric analysis of toxin peptide sequences and classification, overview Conus miles
physiological function diglutamic acid (5-oxo-L-proline, pGlu, Z) formation at the N-terminus of proteins and peptides, a modification observed in both plant and animal kingdoms, requires the action of the enzyme glutaminyl cyclase (QC), which acts on amino terminus glutamine residues. The post-translational modification of N-terminal glutamine (Q) to a diglutamyl (Z) residue is observed in the conotoxins produced by marine cone snails. This conversion requires the action of the enzyme glutaminyl cyclase (QC). Mass spectrometric analysis of toxxin peptide sequences and classification, overview Conus araneosus
physiological function diglutamic acid (5-oxo-L-proline, pGlu, Z) formation at the N-terminus of proteins and peptides, a modification observed in both plant and animal kingdoms, requires the action of the enzyme glutaminyl cyclase (QC), which acts on amino terminus glutamine residues. The post-translational modification of N-terminal glutamine (Q) to a diglutamyl (Z) residue is observed in the conotoxins produced by marine cone snails. This conversion requires the action of the enzyme glutaminyl cyclase (QC). Mass spectrometric analysis of toxxin peptide sequences and classification, overview Conus frigidus
physiological function diglutamic acid (5-oxo-L-proline, pGlu, Z) formation at the N-terminus of proteins and peptides, a modification observed in both plant and animal kingdoms, requires the action of the enzyme glutaminyl cyclase (QC), which acts on amino terminus glutamine residues. The post-translational modification of N-terminal glutamine (Q) to a diglutamyl (Z) residue is observed in the conotoxins produced by marine cone snails. This conversion requires the action of the enzyme glutaminyl cyclase (QC). Mass spectrometric analysis of toxxin peptide sequences and classification, overview Conus litteratus
physiological function diglutamic acid (5-oxo-L-proline, pGlu, Z) formation at the N-terminus of proteins and peptides, a modification observed in both plant and animal kingdoms, requires the action of the enzyme glutaminyl cyclase (QC), which acts on amino terminus glutamine residues. The post-translational modification of N-terminal glutamine (Q) to a diglutamyl (Z) residue is observed in the conotoxins produced by marine cone snails. This conversion requires the action of the enzyme glutaminyl cyclase (QC). Mass spectrometric analysis of toxxin peptide sequences and classification, overview Conus monile
physiological function diglutamic acid (5-oxo-L-proline, pGlu, Z) formation at the N-terminus of proteins and peptides, a modification observed in both plant and animal kingdoms, requires the action of the enzyme glutaminyl cyclase (QC), which acts on amino terminus glutamine residues. The post-translational modification of N-terminal glutamine (Q) to a diglutamyl (Z) residue is observed in the conotoxins produced by marine cone snails. This conversion requires the action of the enzyme glutaminyl cyclase (QC). Mass spectrometric analysis of toxxin peptide sequences and classification, overview Conus amadis