Identification and characterization of a chondroitinase ABC with a novel carbohydrate-binding module.
Int J Biol Macromol
; 271(Pt 1): 132518, 2024 Jun.
Article
in En
| MEDLINE
| ID: mdl-38777025
ABSTRACT
Chondroitinases play important roles in structural and functional studies of chondroitin sulfates. Carbohydrate-binding module (CBM) is generally considered as an accessory module in carbohydrate-active enzymes, which promotes the association of the appended enzyme with the substrate and potentiates the catalytic activity. However, the role of natural CBM in chondroitinases has not been investigated. Herein, a novel chondroitinase ChABC29So containing an unknown domain with a predicted ß-sandwich fold was discovered from Segatella oris. Recombinant ChABC29So showed enzyme activity towards chondroitin sulfates and hyaluronic acid and acted in a random endo-acting manner. The unknown domain exhibited a chondroitin sulfate-binding capacity and was identified as a CBM. Biochemical characterization of ChABC29So and the CBM-truncated enzyme revealed that the CBM enhances the catalytic activity, thermostability, and disaccharide proportion in the final enzymatic products of ChABC29So. These findings demonstrate the role of the natural CBM in a chondroitinase and will guide future modification of chondroitinases.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Chondroitin Sulfates
/
Chondroitin ABC Lyase
Language:
En
Journal:
Int J Biol Macromol
/
Int. j. biol. macromol
/
International journal of biological macromolecules
Year:
2024
Document type:
Article
Affiliation country:
China
Country of publication:
Países Bajos