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Comprehensive Analysis of the Structure and Function of Peptide:N-Glycanase 1 and Relationship with Congenital Disorder of Deglycosylation

by 1, 2,3,4, 5,* and 2,3,*
1
Queen Mary School, Nanchang University, No. 1299 Xuefu Avenue, Honggutan New District, Nanchang 330036, China
2
Laboratory of Translational Medicine Research, Department of Pathology, Deyang People’s Hospital, No. 173 First Section of Taishanbei Road, Jingyang District, Deyang 618000, China
3
Deyang Key Laboratory of Tumor Molecular Research, No. 173 First Section of Taishanbei Road, Jingyang District, Deyang 618000, China
4
Department of Molecular & Cellular Biology, Roswell Park Comprehensive Cancer Center, Elm and Carlton Streets, Buffalo, NY 14263, USA
5
Department of Histology and Embryology, Medical College of Nanchang University, Nanchang 330006, China
*
Authors to whom correspondence should be addressed.
Academic Editors: Emily Sonestedt and Marcellino Monda
Nutrients 2022, 14(9), 1690; https://doi.org/10.3390/nu14091690
Received: 25 February 2022 / Revised: 13 April 2022 / Accepted: 15 April 2022 / Published: 19 April 2022
(This article belongs to the Section Carbohydrates)
The cytosolic PNGase (peptide:N-glycanase), also known as peptide-N4-(N-acetyl-β-glucosaminyl)-asparagine amidase, is a well-conserved deglycosylation enzyme (EC 3.5.1.52) which catalyzes the non-lysosomal hydrolysis of an N(4)-(acetyl-β-d-glucosaminyl) asparagine residue (Asn, N) into a N-acetyl-β-d-glucosaminyl-amine and a peptide containing an aspartate residue (Asp, D). This enzyme (NGLY1) plays an essential role in the clearance of misfolded or unassembled glycoproteins through a process named ER-associated degradation (ERAD). Accumulating evidence also points out that NGLY1 deficiency can cause an autosomal recessive (AR) human genetic disorder associated with abnormal development and congenital disorder of deglycosylation. In addition, the loss of NGLY1 can affect multiple cellular pathways, including but not limited to NFE2L1 pathway, Creb1/Atf1-AQP pathway, BMP pathway, AMPK pathway, and SLC12A2 ion transporter, which might be the underlying reasons for a constellation of clinical phenotypes of NGLY1 deficiency. The current comprehensive review uncovers the NGLY1’ssdetailed structure and its important roles for participation in ERAD, involvement in CDDG and potential treatment for NGLY1 deficiency. View Full-Text
Keywords: N-glycosylation; NGLY1; ER associated degradation process; congenital disorder of deglycosylation; NFE2L1 N-glycosylation; NGLY1; ER associated degradation process; congenital disorder of deglycosylation; NFE2L1
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MDPI and ACS Style

Miao, X.; Wu, J.; Chen, H.; Lu, G. Comprehensive Analysis of the Structure and Function of Peptide:N-Glycanase 1 and Relationship with Congenital Disorder of Deglycosylation. Nutrients 2022, 14, 1690. https://doi.org/10.3390/nu14091690

AMA Style

Miao X, Wu J, Chen H, Lu G. Comprehensive Analysis of the Structure and Function of Peptide:N-Glycanase 1 and Relationship with Congenital Disorder of Deglycosylation. Nutrients. 2022; 14(9):1690. https://doi.org/10.3390/nu14091690

Chicago/Turabian Style

Miao, Xiangguang, Jin Wu, Hongping Chen, and Guanting Lu. 2022. "Comprehensive Analysis of the Structure and Function of Peptide:N-Glycanase 1 and Relationship with Congenital Disorder of Deglycosylation" Nutrients 14, no. 9: 1690. https://doi.org/10.3390/nu14091690

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