Glycoside Hydrolase Family 73

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• Author: ^^^Florence Vincent^^^
• Responsible Curator: ^^^Bernard Henrissat^^^

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Glycoside Hydrolase Family GH73
Clan	none, α+β "lysozyme fold"
Mechanism	not known
Active site residues	partially known
CAZy DB link
https://www.cazy.org/GH73.html

Substrate specificities

         Normal.dotm  0  0  1  42  240  CNRS  2  1  294  12.0         0  false    21    18 pt  18 pt  0  0    false  false  false

The Three enzyme activities have been reported in family GH73, peptidoglycan hydrolase with endo-b-N-acetylglucosaminidase specificity ; lysozyme ; and mannosyl-glycoprotein endo-b-N-acetylglucosaminidase specificity. The GH73 family is comprised of bacterial or prokaryotic viral members.

Kinetics and Mechanism

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Catalytic Residues

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Three-dimensional structures

Figure 1. Ribbon diagram of Auto structure (orange) and its surface, superimposed on FlgJ structure (green).

Crystal structure of GH73 are available and have been coincidently reported, FlgJ from Sphingomonas sp. (SPH1045-C) [1] and Auto a virulence associated peptigoglycan hydrolase from Listeria monocytogenes [2]. A structure for a catalytic mutant (E185A) of FlgJ has been solved by Maruyama et al [3] but doesn’t show any conformational changes. The two GH73 show the same fold, with two subdomains consisting of a β-lobe and an α-lobe that together create an extended substrate binding groove (Figure 1). With a typical lysozyme (α+β) fold, the catalytic domain of Auto is structurally related to the catalytic domain of Slt70 from E. coli [4], the family GH19 chitinases and goose egg-white lysozyme (GEWL, GH23)[5]. FlgJ is structurally related to a peptidoglycan degrading enzyme from the bacteriophage phi 29 [6] and also to family GH22 and GH23 lysozymes.

Family Firsts

First stereochemistry determination

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First catalytic nucleophile identification

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First general acid/base residue identification

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First 3-D structure

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References

1. Hashimoto W, Ochiai A, Momma K, Itoh T, Mikami B, Maruyama Y, and Murata K. (2009). Crystal structure of the glycosidase family 73 peptidoglycan hydrolase FlgJ. Biochem Biophys Res Commun. 2009;381(1):16-21. DOI:10.1016/j.bbrc.2009.01.186 |
2. Bublitz M, Polle L, Holland C, Heinz DW, Nimtz M, and Schubert WD. (2009). Structural basis for autoinhibition and activation of Auto, a virulence-associated peptidoglycan hydrolase of Listeria monocytogenes. Mol Microbiol. 2009;71(6):1509-22. DOI:10.1111/j.1365-2958.2009.06619.x |
3. Maruyama Y, Ochiai A, Itoh T, Mikami B, Hashimoto W, and Murata K. (2010). Mutational studies of the peptidoglycan hydrolase FlgJ of Sphingomonas sp. strain A1. J Basic Microbiol. 2010;50(4):311-7. DOI:10.1002/jobm.200900249 |
4. van Asselt EJ, Thunnissen AM, and Dijkstra BW. (1999). High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment. J Mol Biol. 1999;291(4):877-98. DOI:10.1006/jmbi.1999.3013 |
5. Weaver LH, Grütter MG, and Matthews BW. (1995). The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue. J Mol Biol. 1995;245(1):54-68. DOI:10.1016/s0022-2836(95)80038-7 |
6. Xiang Y, Morais MC, Cohen DN, Bowman VD, Anderson DL, and Rossmann MG. (2008). Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail. Proc Natl Acad Sci U S A. 2008;105(28):9552-7. DOI:10.1073/pnas.0803787105 |