Glycoside Hydrolase Family 64

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• Author: ^^^Julie Grondin^^^
• Responsible Curator: ^^^Harry Brumer^^^

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Glycoside Hydrolase Family GH64
Clan	GH-x
Mechanism	inverting
Active site residues	known
CAZy DB link
https://www.cazy.org/GH64.html

Substrate specificities

All characterized members of the GH64 family are laminaripentaose-producing beta-1,3-glucanases (EC 3.2.1.39) from the GH64-TLP (thaumatin-like protein) superfamily. They are found in bacteria and fungal species, and are particularly abundant in the genomes of various Streptomyces and Fusarium species.

Activity has been shown on insoluble and soluble beta-1,3-glucans, including curdlan [1, 2, 3], colloidal pachyman [1, 3, 4], laminarin [1, 3, 4], and zymosan A [1, 2], a commercial preparation of partially-purified yeast cell walls (contains branched glucans).

Kinetics and Mechanism

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Catalytic Residues

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Three-dimensional structures

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Family Firsts

First stereochemistry determination

Laminaripentaose-producing beta-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[4]

First catalytic nucleophile identification

Laminaripentaose-producing beta-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[3]

First general acid/base residue identification

Laminaripentaose-producing beta-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[3]

First 3-D structure

Laminaripentaose-producing beta-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[3]

References

1. Nakabayashi, M. (1998) Structure of the gene encoding laminaripentaose-producing beta-1,3-glucanase (LPHase) of Streptomyces matensis DIC-108. J. Ferment. Bioengineer. 85, 459-464.

2. Palumbo JD, Sullivan RF, and Kobayashi DY. (2003). Molecular characterization and expression in Escherichia coli of three beta-1,3-glucanase genes from Lysobacter enzymogenes strain N4-7. J Bacteriol. 2003;185(15):4362-70. DOI:10.1128/JB.185.15.4362-4370.2003 |
3. Wu HM, Liu SW, Hsu MT, Hung CL, Lai CC, Cheng WC, Wang HJ, Li YK, and Wang WC. (2009). Structure, mechanistic action, and essential residues of a GH-64 enzyme, laminaripentaose-producing beta-1,3-glucanase. J Biol Chem. 2009;284(39):26708-15. DOI:10.1074/jbc.M109.010983 |
4. Nishimura T, Bignon C, Allouch J, Czjzek M, Darbon H, Watanabe T, and Henrissat B. (2001). Streptomyces matensis laminaripentaose hydrolase is an 'inverting' beta-1,3-glucanase. FEBS Lett. 2001;499(1-2):187-90. DOI:10.1016/s0014-5793(01)02551-0 |