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Glycoside Hydrolase Family 64

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This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


Glycoside Hydrolase Family GH64
Clan GH-x
Mechanism inverting
Active site residues known
CAZy DB link
http://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. issn=0922-338X

    [Nakabayashi1998]
  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 | PubMed ID:12867444 [Palumbo2003]
  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 | PubMed ID:19640850 [Wu2009]
  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 | PubMed ID:11418137 [Nishimura2001]

All Medline abstracts: PubMed