CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article.
Totally new to the CAZy classification? Read this first.
Difference between revisions of "Glycoside Hydrolase Family 110"
(New page: <!-- Sourced from the Template:Biolerplate page by the preloader.php script --> '''The text below is a template to help you create a consistent layout for GH entries. To get an idea of w...) |
|||
| (13 intermediate revisions by 3 users not shown) | |||
| Line 1: | Line 1: | ||
| − | + | {{CuratorApproved}} | |
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
* [[Author]]: [[User:Bernie|Bernard Henrissat]] | * [[Author]]: [[User:Bernie|Bernard Henrissat]] | ||
* [[Responsible Curator]]: [[User:Bernie|Bernard Henrissat]] | * [[Responsible Curator]]: [[User:Bernie|Bernard Henrissat]] | ||
| Line 29: | Line 20: | ||
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
|- | |- | ||
| − | | colspan="2" | | + | | colspan="2" |{{CAZyDBlink}}GH110.html |
|} | |} | ||
</div> | </div> | ||
== Substrate specificities == | == Substrate specificities == | ||
| − | + | This family of [[glycoside hydrolases]] was recently discovered following an effort to isolate enzymes for the selective and efficient removal of the terminal α-galactose residue on B antigen for the enzyme conversion of blood group B to universal group O <cite>#1</cite>. The activity of several enzymes has been studied and they display narrow substrate specificity for the branched blood group B oligosaccharide (Galα1–3(Fucα1–2)Gal). Interestingly and in contrast to many cases where glycosidases display a higher apparent activity on pNP-substrates than on oligosaccharides, the enzyme from ''B. fragilis'' NCTC 9343 (BfGal110A) exhibited a lower activity with pNP-α-Gal (0.3 U/mg) compared to the blood group B substrate (6.6 U/mg). The substrate specificity was remarkably stringent for α-1,3-linked galactose in the branched blood group B structure. The enzyme cleaved neither α4Gal linkages found in P1 and Pk blood group antigens nor the α3Gal linkage in the linear B structure without fucose (the so-called Galili antigen)<cite>1</cite>. In a subsequent study Liu et al. have shown the existence of two distinct subfamilies, one subfamily being exclusively active on the branched blood group B structures, whereas the other subfamily contained linkage specific α1,3-galactosidases that act equally well on both branched blood group B and linear α-1,3-Gal structures <cite>#2</cite>. | |
| − | |||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | The enzymes of this family are classified as [[inverting]] enzymes. The stereochemistry of hydrolysis has been monitored by <sup>1</sup>H NMR using p-nitrophenyl α-galactoside as the substrate and ''B. fragilis''BfGal110B as the enzyme. The results showed that the enzyme initially produces β-galactose, i.e. operates with overall inversion of the anomeric configuration, which is in striking contrast to all other known α-galactosidases that use a [[retaining]] mechanism (see [[Glycoside Hydrolase Family 4]], [[Glycoside Hydrolase Family 27]], [[Glycoside Hydrolase Family 36]] and [[Glycoside Hydrolase Family 57]]) <cite>2</cite>. | |
== Catalytic Residues == | == Catalytic Residues == | ||
| − | + | Unknown | |
== Three-dimensional structures == | == Three-dimensional structures == | ||
| + | Unknown | ||
| + | == Family Firsts == | ||
| + | ;First sterochemistry determination: ''B. fragilis''BfGal110B by <sup>1</sup>H NMR <cite>2</cite>. | ||
| − | + | ;First [[general acid]] identification: | |
| − | ;First | + | ;First [[general base]] residue identification: |
| − | + | ;First 3-D structure: | |
| − | ;First general | ||
| − | ;First 3-D structure: | ||
== References == | == References == | ||
| Line 62: | Line 53: | ||
</biblio> | </biblio> | ||
| − | + | [[Category:Glycoside Hydrolase Families|GH110]] | |
| − | |||
Latest revision as of 19:16, 13 June 2011
This page has been approved by the Responsible Curator as essentially complete. CAZypedia is a living document, so further improvement of this page is still possible. If you would like to suggest an addition or correction, please contact the page's Responsible Curator directly by e-mail.
| Glycoside Hydrolase Family GH110 | |
| Clan | none |
| Mechanism | inverting |
| Active site residues | not known |
| CAZy DB link | |
| https://www.cazy.org/GH110.html | |
Substrate specificities
This family of glycoside hydrolases was recently discovered following an effort to isolate enzymes for the selective and efficient removal of the terminal α-galactose residue on B antigen for the enzyme conversion of blood group B to universal group O [1]. The activity of several enzymes has been studied and they display narrow substrate specificity for the branched blood group B oligosaccharide (Galα1–3(Fucα1–2)Gal). Interestingly and in contrast to many cases where glycosidases display a higher apparent activity on pNP-substrates than on oligosaccharides, the enzyme from B. fragilis NCTC 9343 (BfGal110A) exhibited a lower activity with pNP-α-Gal (0.3 U/mg) compared to the blood group B substrate (6.6 U/mg). The substrate specificity was remarkably stringent for α-1,3-linked galactose in the branched blood group B structure. The enzyme cleaved neither α4Gal linkages found in P1 and Pk blood group antigens nor the α3Gal linkage in the linear B structure without fucose (the so-called Galili antigen)[1]. In a subsequent study Liu et al. have shown the existence of two distinct subfamilies, one subfamily being exclusively active on the branched blood group B structures, whereas the other subfamily contained linkage specific α1,3-galactosidases that act equally well on both branched blood group B and linear α-1,3-Gal structures [2].
Kinetics and Mechanism
The enzymes of this family are classified as inverting enzymes. The stereochemistry of hydrolysis has been monitored by 1H NMR using p-nitrophenyl α-galactoside as the substrate and B. fragilisBfGal110B as the enzyme. The results showed that the enzyme initially produces β-galactose, i.e. operates with overall inversion of the anomeric configuration, which is in striking contrast to all other known α-galactosidases that use a retaining mechanism (see Glycoside Hydrolase Family 4, Glycoside Hydrolase Family 27, Glycoside Hydrolase Family 36 and Glycoside Hydrolase Family 57) [2].
Catalytic Residues
Unknown
Three-dimensional structures
Unknown
Family Firsts
- First sterochemistry determination
- B. fragilisBfGal110B by 1H NMR [2].
- First general acid identification
- First general base residue identification
- First 3-D structure
References
- Liu QP, Sulzenbacher G, Yuan H, Bennett EP, Pietz G, Saunders K, Spence J, Nudelman E, Levery SB, White T, Neveu JM, Lane WS, Bourne Y, Olsson ML, Henrissat B, and Clausen H. (2007). Bacterial glycosidases for the production of universal red blood cells. Nat Biotechnol. 2007;25(4):454-64. DOI:10.1038/nbt1298 |
- Liu QP, Yuan H, Bennett EP, Levery SB, Nudelman E, Spence J, Pietz G, Saunders K, White T, Olsson ML, Henrissat B, Sulzenbacher G, and Clausen H. (2008). Identification of a GH110 subfamily of alpha 1,3-galactosidases: novel enzymes for removal of the alpha 3Gal xenotransplantation antigen. J Biol Chem. 2008;283(13):8545-54. DOI:10.1074/jbc.M709020200 |