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Literature summary for 3.5.1.52 extracted from

  • Jeong, H.Y.; Lee, J.Y.; Park, T.H.
    Specificity of enzymatic in vitro glycosylation by PNGase F: a comparison of enzymatic and non-enzymatic glycosylation (2004), Enzyme Microb. Technol., 35, 587-591.
No PubMed abstract available

Application

Application Comment Organism
synthesis PNGase F can be utilized for glycosylation of non-glycosylated recombinant proteins produced in prokaryotic cells Elizabethkingia meningoseptica

Organism

Organism UniProt Comment Textmining
Elizabethkingia meningoseptica
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation recombinantly expressed in Escherichia coli Elizabethkingia meningoseptica
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PNGase F is responsible for deglycosylation of misfolded proteins, the reverse reaction, glycosylation of peptides RKDVY and EILDVPST by PNGase F, is also possible in vitro, determination of glycosylation sites by MALDI-TOF mass spectrometry, overview, in addition non-enzymatic glycosylation of sugars, which are more than two units long, occurs Elizabethkingia meningoseptica ?
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Synonyms

Synonyms Comment Organism
peptide-N-glycosidase F
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Elizabethkingia meningoseptica
PNGase F
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Elizabethkingia meningoseptica