Unique peptide:N-glycanase of Caenorhabditis elegans has activity of protein disulphide reductase as well as of deglycosylation.

Abstract:

:Peptide:N-glycanase (PNGase) is the enzyme responsible for de-N-glycosylation of misfolded glycoproteins in the cytosol. Here, we report the molecular identification and characterization of PNGase (png-1, F56G4.5) from Caenorhabditis elegans. This enzyme released both high mannose- and complex-type N-glycans from glycopeptides and denatured glycoproteins. Deglycosylation activity was inhibited by Zn(2+) and z-VAD-fmk, but not by EDTA. PNG-1 has a thioredoxin-like domain in addition to a transglutaminase domain, the core domain of PNGases, and exhibited protein disulphide reductase activity in vitro. Our biochemical studies revealed that PNG-1 is a unique bifunctional protein possessing two enzyme activities.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Kato T,Kawahara A,Ashida H,Yamamoto K

doi

10.1093/jb/mvm117

subject

Has Abstract

pub_date

2007-08-01 00:00:00

pages

175-81

issue

2

eissn

0021-924X

issn

1756-2651

pii

mvm117

journal_volume

142

pub_type

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