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Difference between revisions of "Carbohydrate Binding Module Family 19"

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== Family Firsts ==
== Family Firsts ==
;First Identified
;First Identified
:Insert archetype here, possibly including ''very brief'' synopsis.
:The chitin-binding CBM11 from CTS1 in ''Saccharomyces cerevisiae'' was first described by Kuranda and Robbins in 1991 <cite>Kuranda1991</cite>.
;First Structural Characterization
;First Structural Characterization
:There is no 3D structural data on the CBM19 family.
:There is no 3D structural data on the CBM19 family.

Revision as of 05:48, 21 January 2021

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Ligand specificities

The CBM19 found in the CTS1 chitinase produced by Saccharomyces cerevisiae has been characterized as a chitin-binding CBM [1]. The authors used several genetically manipulated constructs to demonstrate chitin binding including making a C-terminal deletion mutant, controlled proteolysis of the wild-type enzyme, production of only the C-terminal CBM11 with the N-terminal signal sequence, fusion of the CBM11 with the yeast invertase SUC2 [1]. These different constructs were tested for their chitin-binding capabilities [1].

Structural Features

Two alleles of the cts1 gene have been identified, they are referred to as cts1-1 and cts1-2 [1]. The predicted full length protein is likely divided into four domains [1]. The first domain (amino acids 1-20) is the cleavable signal sequence, the second domain is the chitinase GH18 catalytic domain (amino acids 21-327), the third domain is a highly glycosylated serine/threonine-rich domain (amino acids 328-480) and the fourth domain is the high affinity chitin binding CBM19 [1, 2].

Content in this section should include, in paragraph form, a description of:

  • Fold: Structural fold (beta trefoil, beta sandwich, etc.)
  • Type: Include here Type A, B, or C and properties
  • Features of ligand binding: Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.


Chitin is an important component of the cell wall of Saccharomyces cerevisiae. It is specifically located at the junction of mother and daughter cells providing mechanical stability. The CTS1 enzyme produced by S. cerevisiae hydrolyses chitin [3, 4] and has a role in cell separation [1].

Content in this section should include, in paragraph form, a description of:

  • Functional role of CBM: Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.
  • Most Common Associated Modules: 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)
  • Novel Applications: Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.

Family Firsts

First Identified
The chitin-binding CBM11 from CTS1 in Saccharomyces cerevisiae was first described by Kuranda and Robbins in 1991 [1].
First Structural Characterization
There is no 3D structural data on the CBM19 family.


  1. Kuranda MJ and Robbins PW. (1991). Chitinase is required for cell separation during growth of Saccharomyces cerevisiae. J Biol Chem. 1991;266(29):19758-67. | Google Books | Open Library PubMed ID:1918080 [Kuranda1991]
  2. Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, and Henrissat B. (2014). The carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res. 2014;42(Database issue):D490-5. DOI:10.1093/nar/gkt1178 | PubMed ID:24270786 [Lombard2014]
  3. Correa JU, Elango N, Polacheck I, and Cabib E. (1982). Endochitinase, a mannan-associated enzyme from Saccharomyces cerevisiae. J Biol Chem. 1982;257(3):1392-7. | Google Books | Open Library PubMed ID:6799506 [Correa1982]
  4. Kuranda MJ and Robbins PW. (1987). Cloning and heterologous expression of glycosidase genes from Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1987;84(9):2585-9. DOI:10.1073/pnas.84.9.2585 | PubMed ID:3033651 [Kuranda1987]

All Medline abstracts: PubMed