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Last update 08 May 2025

ENGASE

Last update 08 May 2025

Basic Info

Synonyms

Cytosolic endo-beta-N-acetylglucosaminidase, endo-beta-N-acetylglucosaminidase, ENGASE

+ [1]

Introduction

Endoglycosidase that releases N-glycans from glycoproteins by cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose core. Involved in the processing of free oligosaccharides in the cytosol.

Drugs associated with ENGASE

TPH-101

Target

ENGASE

Mechanism

ENGASE inhibitors

Active Org.

Telephus Medical LLC

Originator Org.

Telephus Medical LLC

Active Indication

Osteomyelitis [+1]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with ENGASE

100 Translational Medicine associated with ENGASE

0 Patents (Medical) associated with ENGASE

685

Literatures (Medical) associated with ENGASE

01 Feb 2025·Carbohydrate Research

Transglycosylation behavior of Mucor hiemalis endo-β-N-acetylglucosaminidase to β-cyclodextrin derivatives with multivalent glucose moieties for synthesizing cyclodextrin-based oligosaccharide clusters

Article

Author: Tomabechi, Yusuke ; Yamamoto, Kenji ; Yamanoi, Takashi ; Oda, Yoshiki

We investigated the transglycosylation reaction of two types of oligosaccharide acceptors, i.e., β-cyclodextrin (CD) derivatives 1 and 2 conjugated with multiple glucose (Glc) units, catalyzed by endo-β-N-acetyl-glucosaminidase from Mucor hiemalis (Endo-M) using the oligosaccharide donor sialoglycopeptide (SGP). The acceptor specificity of the enzyme transglycosylation of 1 and 2 having seven Glc moieties within small nanoscale spatial regions on the β-CDs was investigated on the basis of the effect of the molar ratios of SGP to acceptors 1 or 2 with different spatial configurations on the transglycosylation behavior. The formation of the corresponding CD-based oligosaccharide clusters from Endo-M was also evaluated.

01 Jan 2025·Pest Management Science

Identification and functional characterization of the chitinase and chitinase‐like gene family in Myzus persicae (Sulzer) during molting

Article

Author: Ding, Bo ; He, Li ; Yang, Hong ; Zhang, Chao

AbstractBACKGROUNDThe crucial role of insect chitinase in molting, pupation, and emergence renders it a promising target for pest control strategies. Despite the extensive investigation of chitinase genes in various pests, there is still a lack of systematic identification and functional analysis related to aphid chitinase.RESULTSWe systematically identified a total of nine chitinase/chitinase‐like genes and one ENGase gene, which included eight Cht genes, one IDGF gene, and one ENGase gene. Through phylogenetic analysis, the chitinase proteins were classified into nine distinct groups (I, II, III, V, VI, VIII, X, other, and ENGase). The expression profile revealed that the epidermis exhibited relatively high expression levels for three chitinase genes: MpCht5, MpCht7, and MpCht10. Furthermore, transcriptional levels of nine chitinase genes were up‐regulated following treatment with 20‐hydroxyecdysone (20E) hormone. Silencing MpCht3, MpCht5, MpCht7, MpCht10, and MpCht11‐2 via RNA interference (RNAi) during the molting stage resulted in nymph shrinking, hindering normal molting and leading to death. Additionally, it was observed that silencing of MpIDGF induced the body color of the aphids to change from reddish brown to colorless after molting, culminating in eventual mortality.CONCLUSIONOur findings suggest that chitinase/chitinase‐like genes play a crucial role in the molting process of Myzus persicae. Utilizing RNAi technology, we aimed to elucidate the precise function of MpCht genes in the molting mechanism of M. persicae, this discovery establishes a significant theoretical foundation for future research on aphid control, with chitinase as the target. © 2024 Society of Chemical Industry.

01 Nov 2024·Cell

Potent efficacy of an IgG-specific endoglycosidase against IgG-mediated pathologies

Article

Author: Ravetch, Jeffrey V. ; Du, Jonathan ; Chernova, Tatiana A ; Sultana, Nazneen ; Ravetch, Jeffrey V ; Sastre, Diego E ; Sundberg, Eric J ; Edgar, Julia E ; Boder, E Josephine ; Huliciak, Maros ; Xu, Ting ; Sundberg, Eric J. ; Sastre, Diego E. ; Bournazos, Stylianos ; Azzam, Tala ; Flowers, Maria ; Yoza, Lea ; Edgar, Julia E. ; Boder, E. Josephine ; Chernova, Tatiana A.

Endo-β-N-acetylglucosaminidases (ENGases) that specifically hydrolyze the Asn297-linked glycan on immunoglobulin G (IgG) antibodies, the major molecular determinant of fragment crystallizable (Fc) γ receptor (FcγR) binding, are exceedingly rare. All previously characterized IgG-specific ENGases are multi-domain proteins secreted as an immune evasion strategy by Streptococcus pyogenes strains. Here, using in silico analysis and mass spectrometry techniques, we identified a family of single-domain ENGases secreted by pathogenic corynebacterial species that exhibit strict specificity for IgG antibodies. By X-ray crystallographic and surface plasmon resonance analyses, we found that the most catalytically efficient IgG-specific ENGase family member recognizes both protein and glycan components of IgG. Employing in vivo models, we demonstrated the remarkable efficacy of this IgG-specific ENGase in mitigating numerous pathologies that rely on FcγR-mediated effector functions, including T and B lymphocyte depletion, autoimmune hemolytic anemia, and antibody-dependent enhancement of dengue disease, revealing its potential for treating and/or preventing a wide range of IgG-mediated diseases in humans.

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