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Literature summary for 3.5.1.52 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
Search for more literature for 3.5.1.52

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
additional information complete deletion of aPNGase activity Solanum lycopersicum
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
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

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

Source Tissue

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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

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

General Information

General Information Comment Organism
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
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
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
metabolism acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover Solanum lycopersicum
metabolism acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover Prunus dulcis
metabolism acidic peptide:N-glycanase (aPNGase) plays a pivotal role in plant glycoprotein turnover Arabidopsis thaliana
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
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
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