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Cited by 13Glycosylation and Glycoproteins ResearchEndoplasmic Reticulum Stress and DiseaseLysosomal Storage Disorders Research

The DOI matches its Crossref record; 146 of the 146 references it cites were found in a registry or an index.

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

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Miao, Xiangguang, Wu, Jin, Chen, Hongping, Lu, Guanting·2022·Nutrients
DOI 10.3390/nu14091690PMC PMC9102325

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Abstract

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.

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Figures

Figure 1 Brief history of the discovery of PNGase.
Figure 1 Brief history of the discovery of PNGase.CC BY · PubMed Central
Figure 2 Predicted structures for non-animal Ngly1 and the core transglutaminase-like domain. (A) AlphaFold predicted structure of FmeNgly1; (B) AlphaFold predicted structure of SceNgly1; (C) AlphaFold predicted structure of AthNgly1; (D) Sequence alignment of the core transglutaminase-like domain. Fme, Flavobacterium meningosepticum; Sce, Saccharomyces cerevisiae; Ath, Arabidopsis thaliana; Osa, Oryza sativa Japonica; Zma, Zea mays; * represents conserved residuals; red * represents the three residuals of the catalytic triad.
Figure 2 Predicted structures for non-animal Ngly1 and the core transglutaminase-like domain. (A) AlphaFold predicted structure of FmeNgly1; (B) AlphaFold predicted structure of SceNgly1; (C) AlphaFold predicted structure of AthNgly1; (D) Sequence alignment of the core transglutaminase-like domain. Fme, Flavobacterium meningosepticum; Sce, Saccharomyces cerevisiae; Ath, Arabidopsis thaliana; Osa, Oryza sativa Japonica; Zma, Zea mays; * represents conserved residuals; red * represents the three residuals of the catalytic triad.CC BY · PubMed Central
Figure 3 Structural analysis of human NGLY1. (A) Three-dimensional structure predicted by AlphaFold; (B) Intrinsically-disordered region of NGLY1; (C) Alignment of the intrinsically-disordered region; (D) Secondary structure of NGLY1.
Figure 3 Structural analysis of human NGLY1. (A) Three-dimensional structure predicted by AlphaFold; (B) Intrinsically-disordered region of NGLY1; (C) Alignment of the intrinsically-disordered region; (D) Secondary structure of NGLY1.CC BY · PubMed Central
Figure 4 Evolutionary relationships of NGLY1 in 33 taxa. (A) Evolutionary phylogeny; (B) Protein structures of Ngly1.
Figure 4 Evolutionary relationships of NGLY1 in 33 taxa. (A) Evolutionary phylogeny; (B) Protein structures of Ngly1.CC BY · PubMed Central
Figure 5 Glc3Man9GlcNAc2 trimming process and ER-associated degradation pathway (ERAD) involving NGLY1. (A) Glc3Man9GlcNAc2 trimming process; (B) ERAD under normal physiological state; (C) ERAD with NGLY1 deficiency.
Figure 5 Glc3Man9GlcNAc2 trimming process and ER-associated degradation pathway (ERAD) involving NGLY1. (A) Glc3Man9GlcNAc2 trimming process; (B) ERAD under normal physiological state; (C) ERAD with NGLY1 deficiency.CC BY · PubMed Central
Figure 6 Variants of NGLY1 generated by alternative splicing in humans. (A) Transcripts; (B) Protein alignments. Red triangles represent peptide binding sites; Red stars the Cys-His-Asp catalytic triad.
Figure 6 Variants of NGLY1 generated by alternative splicing in humans. (A) Transcripts; (B) Protein alignments. Red triangles represent peptide binding sites; Red stars the Cys-His-Asp catalytic triad.CC BY · PubMed Central
Figure 7 Alternative splicing patterns of NGLY1 in different species.
Figure 7 Alternative splicing patterns of NGLY1 in different species.CC BY · PubMed Central
Figure 8 Protein network involving NLGY1 by STRING.
Figure 8 Protein network involving NLGY1 by STRING.CC BY · PubMed Central
Figure 9 Characterization of mutations of NGLY1. (A) mRNA locations; (B) Amino acid locations; (C) Different types of mutations.
Figure 9 Characterization of mutations of NGLY1. (A) mRNA locations; (B) Amino acid locations; (C) Different types of mutations.CC BY · PubMed Central

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Metadata

Authors
Miao, X., Wu, J., Chen, H., & Lu, G.
Affiliations
  • Nanchang University (CN)
  • Roswell Park Comprehensive Cancer Center (US)
  • Laboratory of Translational Medicine Research, Department of Pathology, Deyang People’s Hospital, No. 173 First Section of Taishanbei Road, Jingyang District, Deyang 618000, China
Corresponding author
  • Wu, Jin
  • Chen, Hongping
  • Lu, Guanting
ORCID
Venue
Nutrients
Publisher
MDPI AG
Published
2022-04-19
Volume
14
Issue
9
Pages
1690
ISSN
2072-6643 (ISSN-L)
DOI
10.3390/nu14091690
PMC
PMC9102325
OpenAlex
W4224244065
Cited by
13
References
146
Citations by year
2026: 2 · 2025: 2 · 2024: 6 · 2023: 2 · 2022: 1
FWCI
0.29
Type
journal article
Language
en
Open access
Licence
Locations
  • Nutrients (publishedVersion, cc-by)
  • Preprints.org (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Key Research and Development Project of Deyang City’s Science and Technology Bureau (21ZDYF0011)
  • Special Fund for Incubation Projects of Deyang People's Hospital (FHG202004)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
  • Health Sciences › Medicine › Genetics (clinical) › Lysosomal Storage Disorders Research
Keywords
NGLY1, congenital disorders of glycosylation, ER-associated degradation, N-glycosylation, deglycosylation, BMP signaling, AMPK signaling, NKCC1, glycoprotein quality control, protein structure
MeSH terms
Asparagine, Humans, Peptides, Congenital Disorders of Glycosylation, Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, Solute Carrier Family 12, Member 2

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CoChat. (2026). Citation check: Comprehensive Analysis of the Structure and Function of Peptide:N-Glycanase 1 and Relationship with Congenital Disorder of Deglycosylation. https://app.cochat.ai/papers/10.3390/nu14091690
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Miao, X., Wu, J., Chen, H., & Lu, G. (2022). Comprehensive Analysis of the Structure and Function of Peptide:N-Glycanase 1 and Relationship with Congenital Disorder of Deglycosylation. Nutrients. https://doi.org/10.3390/nu14091690

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