Glycoside Hydrolase Family 110

• Author: Bernard Henrissat
• Responsible Curator: Bernard Henrissat

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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 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 sufamily contained linkage specific α1,3-galactosidases that act equally well on both branched blood group B and linear α-1,3-Gal structures [2].

Catalytic Residues

Unknown

Three-dimensional structures

Unknown

Family Firsts

First sterochemistry determination

the stereochemistry of hydrolysis has been monitored by ¹H NMR using pNP-α-Gal 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 GH4, GH27, GH36 and GH57) [2].

First catalytic nucleophile identification

First general acid/base residue identification

First 3-D structure

References

1. 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 |
2. 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 |