Are there biological functions for bacterial endo-N-acetyl-beta-D-glucosaminidases?
- PMID: 8525060
- DOI: 10.1016/0923-2508(96)80289-0
Are there biological functions for bacterial endo-N-acetyl-beta-D-glucosaminidases?
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.
Similar articles
-
Endo-N-acetyl-beta-D-glucosaminidases and their potential substrates: structure/function relationships.Res Microbiol. 1997 Nov;148(8):661-71. doi: 10.1016/S0923-2508(99)80065-5. Res Microbiol. 1997. PMID: 9765851 Review.
-
Structural basis for the specific cleavage of core-fucosylated N-glycans by endo-β-N-acetylglucosaminidase from the fungus Cordyceps militaris.J Biol Chem. 2019 Nov 8;294(45):17143-17154. doi: 10.1074/jbc.RA119.010842. Epub 2019 Sep 23. J Biol Chem. 2019. PMID: 31548313 Free PMC article.
-
Do de-N-glycosylation enzymes have an important role in plant cells?Biochimie. 1995;77(9):751-60. doi: 10.1016/0300-9084(96)88193-4. Biochimie. 1995. PMID: 8789467 Review.
-
Differential release of high mannose structural isoforms by fungal and bacterial endo-β-N-acetylglucosaminidases.Mol Biosyst. 2012 Apr;8(5):1472-81. doi: 10.1039/c2mb05455h. Epub 2012 Feb 28. Mol Biosyst. 2012. PMID: 22373601
-
Secretion kinetics of endo-N-acetyl-beta-D-glucosaminidase during vegetative growth of Myxococcus xanthus.Res Microbiol. 1996 May;147(4):217-24. doi: 10.1016/0923-2508(96)81382-9. Res Microbiol. 1996. PMID: 8763609
Cited by
-
Structural basis of mammalian high-mannose N-glycan processing by human gut Bacteroides.Nat Commun. 2020 Feb 14;11(1):899. doi: 10.1038/s41467-020-14754-7. Nat Commun. 2020. PMID: 32060313 Free PMC article.
-
Novel β-N-acetylglucosaminidases from Vibrio harveyi 650: cloning, expression, enzymatic properties, and subsite identification.BMC Biochem. 2010 Sep 29;11:40. doi: 10.1186/1471-2091-11-40. BMC Biochem. 2010. PMID: 20920218 Free PMC article.
-
Proteomic response in Streptococcus gordonii DL1 biofilm cells during attachment to salivary MUC5B.J Oral Microbiol. 2021 Aug 23;13(1):1967636. doi: 10.1080/20002297.2021.1967636. eCollection 2021. J Oral Microbiol. 2021. PMID: 34447490 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources