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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

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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.[1]
First catalytic nucleophile identification
Laminaripentaose-producing beta-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[2]
First general acid/base residue identification
Laminaripentaose-producing beta-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[2]
First 3-D structure
Laminaripentaose-producing beta-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[2]

References

  1. 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]
  2. 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]

All Medline abstracts: PubMed