CAZypedia needs your help! We have many unassigned GH, PL, CE, AA, GT, and CBM pages in need of Authors and Responsible Curators.
Scientists at all career stages, including students, are welcome to contribute to CAZypedia. Read more here, and in the 10th anniversary article in Glycobiology.
New to the CAZy classification? Read this first.
*
Consider attending the 15th Carbohydrate Bioengineering Meeting in Ghent, 5-8 May 2024.

Glycoside Hydrolase Family 58

From CAZypedia
Jump to navigation Jump to search


The text below is a template to help you create a consistent layout for GH entries. To get an idea of what to put in each field, save this edit and have a look at any of the GH families by following this link: Category:Glycoside Hydrolase Families (TIP: Right click with your mouse and open the link in a new browser window...)

Make sure to delete this text and the four dashes (line) below when you are done with your page!::


Under construction icon-blue-48px.png

This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


Glycoside Hydrolase Family GH58
Clan none
Mechanism inverting
Active site residues known/not known
CAZy DB link
http://www.cazy.org/fam/GHnn.html


Substrate specificities

endo-N-acetylneuraminidase or endo-sialidase


This is an example of how to make references to a journal article [1]. (See the References section below). Multiple references can go in the same place like this [1, 2]. You can even cite books using just the ISBN [3]. References that are not in PubMed can be typed in by hand [4].

Kinetics and Mechanism

Content is to be added here.


Catalytic Residues

Content is to be added here.


Three-dimensional structures

Content is to be added here.


Family Firsts

First sterochemistry determination
Cite some reference here, with a short (1-2 sentence) explanation [1].
First catalytic nucleophile identification
Cite some reference here, with a short (1-2 sentence) explanation [4].
First general acid/base residue identification
Cite some reference here, with a short (1-2 sentence) explanation [2].
First 3-D structure
Cite some reference here, with a short (1-2 sentence) explanation [3].

References

  1. Kwiatkowski B, Boschek B, Thiele H, and Stirm S. (1982). Endo-N-acetylneuraminidase associated with bacteriophage particles. J Virol. 1982;43(2):697-704. DOI:10.1128/JVI.43.2.697-704.1982 | PubMed ID:7109038 [3]
  2. Stummeyer K, Dickmanns A, Mühlenhoff M, Gerardy-Schahn R, and Ficner R. (2005). Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F. Nat Struct Mol Biol. 2005;12(1):90-6. DOI:10.1038/nsmb874 | PubMed ID:15608653 [1]
  3. Morley TJ, Willis LM, Whitfield C, Wakarchuk WW, and Withers SG. (2009). A new sialidase mechanism: bacteriophage K1F endo-sialidase is an inverting glycosidase. J Biol Chem. 2009;284(26):17404-10. DOI:10.1074/jbc.M109.003970 | PubMed ID:19411257 [2]
  4. Hallenbeck PC, Vimr ER, Yu F, Bassler B, and Troy FA. (1987). Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-alpha-2,8-sialosyl carbohydrate units. J Biol Chem. 1987;262(8):3553-61. | Google Books | Open Library PubMed ID:3546309 [4]
  5. Petter JG and Vimr ER. (1993). Complete nucleotide sequence of the bacteriophage K1F tail gene encoding endo-N-acylneuraminidase (endo-N) and comparison to an endo-N homolog in bacteriophage PK1E. J Bacteriol. 1993;175(14):4354-63. DOI:10.1128/jb.175.14.4354-4363.1993 | PubMed ID:8331067 [5]

All Medline abstracts: PubMed

[[Category:Glycoside Hydrolase Families|GHnnn]]