CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article.
Totally new to the CAZy classification? Read this first.

Difference between revisions of "Glycoside Hydrolase Family 64"

From CAZypedia
Jump to navigation Jump to search
Line 29: Line 29:
  
 
== Substrate specificities ==
 
== 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.
+
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 beta-1,3-glucans, including curdlan <cite>Nakabayashi1998, Palumbo2003, Wu2009</cite>, colloidal pachyman <cite>Nakabayashi1998, Nishimura2001, Wu2009</cite>, laminarin <cite>Nakabayashi1998, Nishimura2001, Wu2009</cite>, and zymosan A <cite>Nakabayashi1998, Palumbo2003</cite>, a commercial preparation of partially-purified yeast cell walls (contains branched glucans).
+
Activity has been shown on insoluble and soluble &beta;-1,3-glucans, including curdlan <cite>Nakabayashi1998, Palumbo2003, Wu2009</cite>, colloidal pachyman <cite>Nakabayashi1998, Nishimura2001, Wu2009</cite>, laminarin <cite>Nakabayashi1998, Nishimura2001, Wu2009</cite>, and zymosan A <cite>Nakabayashi1998, Palumbo2003</cite>, a commercial preparation of partially-purified yeast cell walls (contains branched glucans).
  
 
== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
Line 43: Line 43:
  
 
== Family Firsts ==
 
== Family Firsts ==
;First stereochemistry determination: Laminaripentaose-producing beta-1,3-glucanase (LPHase) from ''Streptomyces matensis'' DIC-108.<cite>Nishimura2001</cite>  
+
;First stereochemistry determination: Laminaripentaose-producing &beta;-1,3-glucanase (LPHase) from ''Streptomyces matensis'' DIC-108.<cite>Nishimura2001</cite>  
;First catalytic nucleophile identification: Laminaripentaose-producing beta-1,3-glucanase (LPHase) from ''Streptomyces matensis'' DIC-108.<cite>Wu2009</cite>  
+
;First catalytic nucleophile identification: Laminaripentaose-producing &beta;-1,3-glucanase (LPHase) from ''Streptomyces matensis'' DIC-108.<cite>Wu2009</cite>  
;First general acid/base residue identification: Laminaripentaose-producing beta-1,3-glucanase (LPHase) from ''Streptomyces matensis'' DIC-108.<cite>Wu2009</cite>  
+
;First general acid/base residue identification: Laminaripentaose-producing &beta;-1,3-glucanase (LPHase) from ''Streptomyces matensis'' DIC-108.<cite>Wu2009</cite>  
;First 3-D structure: Laminaripentaose-producing beta-1,3-glucanase (LPHase) from ''Streptomyces matensis'' DIC-108.<cite>Wu2009</cite>  
+
;First 3-D structure: Laminaripentaose-producing &beta;-1,3-glucanase (LPHase) from ''Streptomyces matensis'' DIC-108.<cite>Wu2009</cite>  
  
 
== References ==
 
== References ==
 
<biblio>
 
<biblio>
#Nakabayashi1998 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. [http://www.sciencedirect.com/science/article/pii/S0922338X98800627?via%3Dihub DOI=10.1016/s0922-338x(98)80062-7]
+
#Nakabayashi1998 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. [http://www.sciencedirect.com/science/article/pii/S0922338X98800627?via%3Dihub DOI=10.1016/s0922-338x(98)80062-7]
 
#Palumbo2003 pmid=12867444
 
#Palumbo2003 pmid=12867444
 
#Wu2009 pmid=19640850
 
#Wu2009 pmid=19640850

Revision as of 08:17, 6 May 2020

Under construction icon-blue-48px.png

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 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

Content is to be added here.

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