Literature DB >> 8525060

Are there biological functions for bacterial endo-N-acetyl-beta-D-glucosaminidases?

Y Karamanos1, S Bourgerie, J P Barreaud, R Julien.   

Abstract

The endo-N-acetyl-beta-D-glucosaminidases (ENGase) acting on the N-N'-diacetylchitobiosyl core of N-glycosylproteins are essential reagents for the investigation of the structure and the functions of glycoproteins. These enzymes were largely studied with the aim of offering more tools with new and broader substrate specificities to the community of glycobiologist. Conversely, little attention was given to their potential role in the physiology of bacteria, even though it had been shown that ENGases are important enzymes for the physiology of animal and plant cells. In this brief review, we present the main characteristics of the bacterial ENGases and confine our discussion to biological aspects of their action in bacterial systems.

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Year:  1995        PMID: 8525060     DOI: 10.1016/0923-2508(96)80289-0

Source DB:  PubMed          Journal:  Res Microbiol        ISSN: 0923-2508            Impact factor:   3.992


  3 in total

1.  Proteomic response in Streptococcus gordonii DL1 biofilm cells during attachment to salivary MUC5B.

Authors:  Carolina Robertsson; Gunnel Svensäter; Zoltan Blum; Magnus E Jakobsson; Claes Wickström
Journal:  J Oral Microbiol       Date:  2021-08-23       Impact factor: 5.474

2.  Novel β-N-acetylglucosaminidases from Vibrio harveyi 650: cloning, expression, enzymatic properties, and subsite identification.

Authors:  Wipa Suginta; Duangkamon Chuenark; Mamiko Mizuhara; Tamo Fukamizo
Journal:  BMC Biochem       Date:  2010-09-29       Impact factor: 4.059

3.  Structural basis of mammalian high-mannose N-glycan processing by human gut Bacteroides.

Authors:  Beatriz Trastoy; Jonathan J Du; Erik H Klontz; Chao Li; Javier O Cifuente; Lai-Xi Wang; Eric J Sundberg; Marcelo E Guerin
Journal:  Nat Commun       Date:  2020-02-14       Impact factor: 14.919

  3 in total

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