Glycoside Hydrolase Family 58

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!::

---

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.

• Author: ^^^Warren Wakarchuk^^^
• Responsible Curator: ^^^Warren Wakarchuk^^^

---

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

               Normal   0         false   false   false                                    This enzyme is specific for polysialic acid and is one of a unique family of endo-sialidases, all others previously reported being exo-sialidases. The recently determined structure of an endosialidase derived from bacteriophage K1F (endoNF)  revealed the active site to lack a number of the residues that are conserved in other sialidases, implying a new, endosialidase-specific catalytic mechanism.

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

3. 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 |
5. 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 |
6. 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 |
7. 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
8. 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 |

[[Category:Glycoside Hydrolase Families|GHnnn]]