Exopolygalacturonate lyase from Thermotoga maritima: cloning, characterization and organic synthesis application.
Carbohydr Res
; 337(16): 1427-33, 2002 Sep 09.
Article
in En
| MEDLINE
| ID: mdl-12204603
ABSTRACT
A new exopolygalacturonate lyase (Pel) gene of the hyperthermophilic bacterium Thermotoga maritima was cloned and overexpressed in Escherichia coli cells. A 42 kDa monomeric Pel was shown to undergo N-terminal processing by cleavage at a putative site between alanine and serine residues. The enzyme catalyzes selectively a beta-4,5 elimination at the third galacturonic unit from the reducing end of polygalacturonic acid by producing (4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid)-(1-->4)-(alpha-D-galactopyranosyluronic acid)-(1-->4)-alpha-D-galactopyranuronic acid (3) with a 60% yield. The optimum activity of the enzyme was detected at pH 9.5 and T> or=95 degrees C. The highly thermostable enzyme constitutes a useful catalyst for a simplified synthesis of 4,5-unsaturated trigalacturonic acid 3, a trisaccharide which is extremely difficult to obtain via chemical synthesis.
Search on Google
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Polysaccharide-Lyases
/
Sugar Acids
/
Trisaccharides
/
Thermotoga maritima
Language:
En
Journal:
Carbohydr Res
Year:
2002
Document type:
Article
Affiliation country:
France