Literature DB >> 8789467

Do de-N-glycosylation enzymes have an important role in plant cells?

S Berger1, A Menudier, R Julien, Y Karamanos.   

Abstract

In this review de-N-glycosylation was defined as the removal of the glycan(s) from a N-glycosylprotein, by means of enzymes acting on the di-N-acetylchitobiosyl part of the invariant pentasaccharide inner-core of N-glycosylproteins. Peptide-N4-(N-acetyl-beta-D-glucosaminyl) asparagine amidases (PNGase) and endo-N-acetyl-beta-D-glucosaminidases (ENGase) were both considered as de-N-glycosylation enzymes. A detailed description of the characterization and the function of plant PNGases and ENGases is presented, together with a brief presentation on the occurrence and the current knowledge on the function of microbial and animal enzymes. De-N-glycosylation of plant glycoproteins was proposed as a possible mechanism for the release of oligosaccharides displaying biological activities and the removal of N-glycans could also explain the regulation of protein activity. Each enzyme seems to have a specific function during germination and post-germinative development. All the arguments concur that de-N-glycosylation enzymes have an important role in plant cells and confirm that the N-glycosylation/de-N-glycosylation system should occur more commonly than presently recognized in living organisms.

Entities:  

Mesh:

Substances:

Year:  1995        PMID: 8789467     DOI: 10.1016/0300-9084(96)88193-4

Source DB:  PubMed          Journal:  Biochimie        ISSN: 0300-9084            Impact factor:   4.079


  14 in total

1.  Identification and characterization of a novel prokaryotic peptide: N-glycosidase from Elizabethkingia meningoseptica.

Authors:  Guiqin Sun; Xiang Yu; Celimuge Bao; Lei Wang; Meng Li; Jianhua Gan; Di Qu; Jinbiao Ma; Li Chen
Journal:  J Biol Chem       Date:  2015-01-22       Impact factor: 5.157

2.  Purification and characterization of N-glycanase, a concanavalin A binding protein from jackbean (Canavalia ensiformis).

Authors:  P S Sheldon; J N Keen; D J Bowles
Journal:  Biochem J       Date:  1998-02-15       Impact factor: 3.857

Review 3.  Free N-linked oligosaccharide chains: formation and degradation.

Authors:  Tadashi Suzuki; Yoko Funakoshi
Journal:  Glycoconj J       Date:  2006-07       Impact factor: 2.916

4.  The N-Glycan cluster from Xanthomonas campestris pv. campestris: a toolbox for sequential plant N-glycan processing.

Authors:  Stéphanie Dupoiron; Claudine Zischek; Laetitia Ligat; Julien Carbonne; Alice Boulanger; Thomas Dugé de Bernonville; Martine Lautier; Pauline Rival; Matthieu Arlat; Elisabeth Jamet; Emmanuelle Lauber; Cécile Albenne
Journal:  J Biol Chem       Date:  2015-01-13       Impact factor: 5.157

5.  Occurrence of complex type free N-glycans with a single GlcNAc residue at the reducing termini in the fresh-water plant, Egeria densa.

Authors:  Megumi Maeda; Natsuki Ebara; Misato Tani; Christopher J Vavricka; Yoshinobu Kimura
Journal:  Glycoconj J       Date:  2017-01-14       Impact factor: 2.916

Review 6.  Generation and degradation of free asparagine-linked glycans.

Authors:  Yoichiro Harada; Hiroto Hirayama; Tadashi Suzuki
Journal:  Cell Mol Life Sci       Date:  2015-03-14       Impact factor: 9.261

7.  Genome-wide identification, expression and chromosomal location of the genes encoding chitinolytic enzymes in Zea mays.

Authors:  Michal Shoresh; Gary E Harman
Journal:  Mol Genet Genomics       Date:  2008-06-17       Impact factor: 3.291

8.  Regulation of De-N-Glycosylation Enzymes in Germinating Radish Seeds.

Authors:  S. Berger; A. Menudier; R. Julien; Y. Karamanos
Journal:  Plant Physiol       Date:  1996-09       Impact factor: 8.340

9.  The first crystal structures of a family 19 class IV chitinase: the enzyme from Norway spruce.

Authors:  Wimal Ubhayasekera; Reetika Rawat; Sharon Wing Tak Ho; Malgorzata Wiweger; Sara Von Arnold; Mee-Len Chye; Sherry L Mowbray
Journal:  Plant Mol Biol       Date:  2009-07-23       Impact factor: 4.076

10.  Solubility-insolubility interconversion of sophoragrin, a mannose/glucose-specific lectin in Sophora japonica (Japanese pagoda tree) bark, regulated by the sugar-specific interaction.

Authors:  Haruko Ueda; Hisako Fukushima; Yasumaru Hatanaka; Haruko Ogawa
Journal:  Biochem J       Date:  2004-09-15       Impact factor: 3.857

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.