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Peptide:N-glycosidase F, commonly referred to as PNGase F, is an amidase of the peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase class. PNGase F works by
PNGase_F
Small non-coding RNA
direct glycosylation of RNA bases. The sensitivity of glycoRNA moieties to PNGase F, which cleaves the glycosidic linkage between asparagine and the proximal
GlycoRNA
Biochemical process
enzyme cleaves serine- or threonine-linked unsubstituted Galβ1,3GalNAc PNGase F: cleaves asparagine-linked oligosaccharides unless α1,3-core fucosylated
Glycosylation
N-oligosaccharide glycopeptidase, N-glycanase, Jack-bean glycopeptidase, PNGase A, and PNGase F The enzyme uses a catalytic triad of cysteine-histidine-aspartate
Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase
Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine_amidase
American life sciences company
and function of human glycans. NEB will supply a version of its Rapid PNGase F technology to aid in increased sample preparation and improve process throughput
New_England_Biolabs
Type of beta barrel protein domain structure
peptide:N-glycosidase F (PNGases F) and peptidylglycine alpha-amidating monooxygenase. A notable difference between PNGases F and the other double jelly
Jelly_roll_fold
Realm of viruses
related to the DJR-MCP and DUF2961 proteins include peptide:N-glycosidase F (PNGase F) and peptidylglycine α-hydroxylating monooxygenase (PHM). The two jelly
Varidnaviria
Protein-coding gene in the species Homo sapiens
from other “reagent” PNGases from almond (glycoamidase/PNGase A), or bacteria (N-glycanase/PNGase F), that is often used for structural/functional studies
NGLY1
processing a protein of interest has undergone. Endoglycosidases F and D, cleave Glc-Nac PNGase F (Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine_amidase)
Endoglycosidase_H
Protein-coding gene in the species Homo sapiens
(February 1995). "Purification and structure-function analysis of native, PNGase F-treated, and endo-beta-galactosidase-treated CHIP28 water channels". Biochemistry
Aquaporin-1
Protein-coding gene in the species Homo sapiens
cofactors that interact with the carboxy-terminal tail of VCP are PLAA, PNGase, and Ufd2. The molecular basis for cofactor binding has been studied for
Valosin-containing_protein
Protein-coding gene in the species Homo sapiens
Medicine. van der Spek PJ, Smit EM, Beverloo HB, Sugasawa K, Masutani C, Hanaoka F, Hoeijmakers JH, Hagemeijer A (Oct 1994). "Chromosomal localization of three
RAD23B
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PNGASE F
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