Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Uemura, R.; Ogura, M.; Matsumaru, C.; Akiyama, T.; Maeda, M.; Kimura, Y.
    Novel assay system for acidic peptide N-glycanase (aPNGase) activity in crude plant extract (2018), Biosci. Biotechnol. Biochem., 82, 1172-1175 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.52 recombinant expression in an Arabidopsis thaliana aPNGase-knockout line Solanum lycopersicum
3.5.1.52 recombinant expression in an Arabidopsis thaliana aPNGase-knockout line Prunus dulcis

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.52 additional information complete deletion of aPNGase activity Solanum lycopersicum
3.5.1.52 additional information generation of a At3g14920 gene knockout mutant, complete deletion of aPNGase activity in F1 self plants, screened for At3g14920/At5g05480 double-knockout, from Arabidopsis Columbia T-DNA insertion mutant lines SALK_011366 (At3g14920) and SALK_018420 (At5g05480) Arabidopsis thaliana
3.5.1.52 additional information generation of a At5g05480 gene knockout mutant, complete deletion of aPNGase activity in F1 self plants, screened for At3g14920/At5g05480 double-knockout, from Arabidopsis Columbia T-DNA insertion mutant lines SALK_011366 (At3g14920) and SALK_018420 (At5g05480) Arabidopsis thaliana

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.52 Arabidopsis thaliana Q9FFG6
-
-
3.5.1.52 Arabidopsis thaliana Q9LKB2
-
-
3.5.1.52 Arabidopsis thaliana Col-0 Q9FFG6
-
-
3.5.1.52 Arabidopsis thaliana Col-0 Q9LKB2
-
-
3.5.1.52 Prunus dulcis P81898
-
-
3.5.1.52 Solanum lycopersicum F8QR42
-
-
3.5.1.52 Solanum lycopersicum Micro-Tom F8QR42
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.52 fruit mature green tomato fruits Solanum lycopersicum
-
3.5.1.52 rosette leaf
-
 Arabidopsis thaliana
-
3.5.1.52 seed
-
 Prunus dulcis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.52 additional information development of an assay system for acidic peptide:N-glycanase (aPNGase) activity in crude plant extract using fluorescence-labeled N-glycopeptides as a substrates, overview Prunus dulcis ?
-
 ?
3.5.1.52 additional information development of an assay system for acidic peptide:N-glycanase (aPNGase) activity in crude plant extract using fluorescence-labeled N-glycopeptides as a substrates, overview. The enzyme produces free N-glycans Solanum lycopersicum ?
-
 ?
3.5.1.52 additional information development of an assay system for acidic peptide:N-glycanase (aPNGase) activity in crude plant extract using fluorescence-labeled N-glycopeptides as a substrates, overview. The enzyme produces free N-glycans Arabidopsis thaliana ?
-
 ?
3.5.1.52 additional information development of an assay system for acidic peptide:N-glycanase (aPNGase) activity in crude plant extract using fluorescence-labeled N-glycopeptides as a substrates, overview. The enzyme produces free N-glycans Solanum lycopersicum Micro-Tom ?
-
 ?
3.5.1.52 additional information development of an assay system for acidic peptide:N-glycanase (aPNGase) activity in crude plant extract using fluorescence-labeled N-glycopeptides as a substrates, overview. The enzyme produces free N-glycans Arabidopsis thaliana Col-0 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.52 aPNGase
-
 Solanum lycopersicum
3.5.1.52 aPNGase
-
 Prunus dulcis
3.5.1.52 aPNGase
-
 Arabidopsis thaliana
3.5.1.52 At3g14920
-
 Arabidopsis thaliana
3.5.1.52 At5g05480
-
 Arabidopsis thaliana
3.5.1.52 peptide:N-glycanase
-
 Solanum lycopersicum
3.5.1.52 peptide:N-glycanase
-
 Prunus dulcis
3.5.1.52 peptide:N-glycanase
-
 Arabidopsis thaliana
3.5.1.52 PNGase-A
-
 Prunus dulcis
3.5.1.52 PNGase-A
-
 Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
3.5.1.52 evolution PNGases are classified into two types based on their optimum pH: neutral or cytosolic PNGase (cPNGase) and acidic PNGase (aPNGase). cPNGase is found ubiquitously in eukaryotic cells, while aPNGase is found mainly in plants Solanum lycopersicum
3.5.1.52 evolution PNGases are classified into two types based on their optimum pH: neutral or cytosolic PNGase (cPNGase) and acidic PNGase (aPNGase). cPNGase is found ubiquitously in eukaryotic cells, while aPNGase is found mainly in plants Prunus dulcis
3.5.1.52 evolution PNGases are classified into two types based on their optimum pH: neutral or cytosolic PNGase (cPNGase) and acidic PNGase (aPNGase). cPNGase is found ubiquitously in eukaryotic cells, while aPNGase is found mainly in plants Arabidopsis thaliana
3.5.1.52 metabolism acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover Solanum lycopersicum
3.5.1.52 metabolism acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover Prunus dulcis
3.5.1.52 metabolism acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover Arabidopsis thaliana
3.5.1.52 physiological function the enzyme hydrolyzes the beta-aspartyl-glycosylamine bond of N-linked glycopeptides, and is involved in the degradation of misfolded or function-lost glycoproteins. cPNGase is believed to be involved in the protein quality control system, while aPNGase is involved in the release of N-glycan units from various glycopeptides produced in the degradation process of function-lost or aged glycoproteins Solanum lycopersicum
3.5.1.52 physiological function the enzyme hydrolyzes the beta-aspartyl-glycosylamine bond of N-linked glycopeptides, and is involved in the degradation of misfolded or function-lost glycoproteins. cPNGase is believed to be involved in the protein quality control system, while aPNGase is involved in the release of N-glycan units from various glycopeptides produced in the degradation process of function-lost or aged glycoproteins Prunus dulcis
3.5.1.52 physiological function the enzyme hydrolyzes the beta-aspartyl-glycosylamine bond of N-linked glycopeptides, and is involved in the degradation of misfolded or function-lost glycoproteins. cPNGase is believed to be involved in the protein quality control system, while aPNGase is involved in the release of N-glycan units from various glycopeptides produced in the degradation process of function-lost or aged glycoproteins Arabidopsis thaliana