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

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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

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Catalytic Residues

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Three-dimensional structures

         Normal.dotm  0  0  1  123  705  CNRS  5  1  865  12.0         0  false    21    18 pt  18 pt  0  0    false  false  false

Two crystal structure of GH73 are available and have been coincidently reported, FlgJ from Sphingomonas sp. (SPH1045-C) [5] and Auto a virulence associated peptigoglycan hydrolase from Listeria monocytogenes [6]. A structure for a catalytic mutant (E185A) of FlgJ has been solved by Maruyama et al [7] 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. With a typical lysozyme (α+β) fold, the catalytic domain of Auto is structurally related to the catalytic domain of Slt70 from E. coli[8], the family GH19 chitinases and goose egg-white lysozyme (GEWL, GH23)[9]. FlgJ is structurally related to a peptidoglycan degrading enzyme from the bacteriophage phi 29 [10] 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

Cite some reference here, with a short (1-2 sentence) explanation [2].

First 3-D structure

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References

1. Comfort DA, Bobrov KS, Ivanen DR, Shabalin KA, Harris JM, Kulminskaya AA, Brumer H, and Kelly RM. (2007). Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases. Biochemistry. 2007;46(11):3319-30. DOI:10.1021/bi061521n |
2. He S and Withers SG. (1997). Assignment of sweet almond beta-glucosidase as a family 1 glycosidase and identification of its active site nucleophile. J Biol Chem. 1997;272(40):24864-7. DOI:10.1074/jbc.272.40.24864 |

4. Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006