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Difference between revisions of "Glycoside Hydrolase Family 110"
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== Substrate specificities == | == Substrate specificities == | ||
| − | + | This family of enzymes was recently discovered following an effort to isolate enzymes for the selective and efficient removal of the terminal alpha-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 (Gala1–3(Fuca1–2)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 exhibited a lower activity with pNP-a-Gal (0.3 U/mg) compared to the blood group B substrate (6.6 U/mg). 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 sufamily contained linkage specific a1,3-galactosidases that act equally well on both branched blood group B and linear a-1,3-Gal structures <cite>2</cite>. | |
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== Catalytic Residues == | == Catalytic Residues == | ||
| − | + | Unknown | |
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | Unknown | |
== Family Firsts == | == Family Firsts == | ||
| − | ;First sterochemistry determination: | + | ;First sterochemistry determination: The stereochemistry of hydrolysis has been monitored by 1H NMR using pNP-a-Gal as the substrate and B. fragilis BfGal110B as the enzyme. The results showed that the enzyme operates with overall inversion of the anomeric configuration, which is in striking contrast to all other known a-galactosidases that use a retaining mechanism (see glycoside hydrolase family GH4, GH27, GH36 and GH57) <cite>2</cite>. |
;First catalytic nucleophile identification: | ;First catalytic nucleophile identification: | ||
;First general acid/base residue identification: | ;First general acid/base residue identification: | ||
Revision as of 06:31, 7 July 2009
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...)
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| Glycoside Hydrolase Family GH110 | |
| Clan | none |
| Mechanism | inverting |
| Active site residues | not known |
| CAZy DB link | |
| http://www.cazy.org/fam/GH110.html | |
Substrate specificities
This family of enzymes was recently discovered following an effort to isolate enzymes for the selective and efficient removal of the terminal alpha-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 (Gala1–3(Fuca1–2)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 exhibited a lower activity with pNP-a-Gal (0.3 U/mg) compared to the blood group B substrate (6.6 U/mg). 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 sufamily contained linkage specific a1,3-galactosidases that act equally well on both branched blood group B and linear a-1,3-Gal structures [2].
Kinetics and Mechanism
Catalytic Residues
Unknown
Three-dimensional structures
Unknown
Family Firsts
- First sterochemistry determination
- The stereochemistry of hydrolysis has been monitored by 1H NMR using pNP-a-Gal as the substrate and B. fragilis BfGal110B as the enzyme. The results showed that the enzyme operates with overall inversion of the anomeric configuration, which is in striking contrast to all other known a-galactosidases that use a retaining mechanism (see glycoside hydrolase family GH4, GH27, GH36 and GH57) [2].
- First catalytic nucleophile identification
- First general acid/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 |
[[Category:Glycoside Hydrolase Families]]