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

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First 3-D structure

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References

5. 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 |

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7. 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 |

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10. 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 |

11. pmid=