Abstract:
BACKGROUND:Peptide: N-glycanase is a deglycosylation enzyme releasing N-glycan from glycoproteins. Although glycan specificity analysis of this enzyme has been reported, recognition requirements for the peptide sequence have not been precisely elucidated. OBJECTIVE:In this study, we carried out peptide specificity analysis of several peptide:N-glycanases. METHODS:Using synthetic chitobiose-pentapeptide substrates having a systematic series of amino acid sequences composed of hydrophobic leucine and hydrophilic serine, we examined the peptide specificities of peptide: N-glycanases comprising yeast cytoplasmic PNGase, bacterial PNGase F, and plant PNGase A by ultra-performance liquid chromatography combined with electrospray ionization mass spectrometry. RESULTS:We found that each of the PNGases had higher activity for the more hydrophobic (leucinerich) chitobiose-pentapeptides, although the sensitivities of the PNGases for hydrophobicity varied. Cytoplasmic PNGase showed broad specificity. In contrast, PNGase A showed moderate specificity. PNGase F showed the highest specificity. CONCLUSION:PNGases from different origins had similar but significantly independent peptide specificities.
journal_name
Protein Pept Lettjournal_title
Protein and peptide lettersauthors
Kuribara T,Ishihara T,Kudo T,Hirano M,Totani Kdoi
10.2174/0929866524666170818160159subject
Has Abstractpub_date
2017-01-01 00:00:00pages
723-728issue
8eissn
0929-8665issn
1875-5305pii
PPL-EPUB-85362journal_volume
24pub_type
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