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Glycoside Hydrolase Family 64

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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 β-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 β-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

GH64 enzymes follow an inverting mechanism, first shown by 1H-NMR during the hydrolysis of laminarin [4].

Catalytic Residues

Content is to be added here.

Three-dimensional structures

Content is to be added here.

Family Firsts

First stereochemistry determination
Laminaripentaose-producing β-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[4]
First catalytic nucleophile identification
Laminaripentaose-producing β-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[3]
First general acid/base residue identification
Laminaripentaose-producing β-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[3]
First 3-D structure
Laminaripentaose-producing β-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[3]

References

  1. Nakabayashi, M. (1998) Structure of the gene encoding laminaripentaose-producing β-1,3-glucanase (LPHase) of Streptomyces matensis DIC-108. J. Ferment. Bioengineer. 85, 459-464. DOI=10.1016/s0922-338x(98)80062-7

    [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