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Literature summary for 4.2.2.14 extracted from

  • Konno, N.; Igarashi, K.; Habu, N.; Samejima, M.; Isogai, A.
    Cloning of the Trichoderma reesei cDNA encoding a glucuronan lyase belonging to a novel polysaccharide lyase family (2009), Appl. Environ. Microbiol., 75, 101-107.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Pichia pastoris Trichoderma reesei

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
Trichoderma reesei

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activity and thermostability increases in the presence of Ca2+ Trichoderma reesei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27000
-
SDS-PAGE Trichoderma reesei

Organism

Organism UniProt Comment Textmining
Trichoderma reesei B6F143
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cellouronate substrate specificity of recombinant TrGL is examined using various polyuronates, including alginate, hyaluronate, pectin, polygalacturonic acid, amylouronate, and carboxymethyl cellulose. Results indicate that there is high substrate specificity of the enzyme for cellouronate Trichoderma reesei ?
-
?

Synonyms

Synonyms Comment Organism
glucuronan lyase
-
Trichoderma reesei
TrGL
-
Trichoderma reesei

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
assay at Trichoderma reesei

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
10 40 enzyme activity remains after incubation at 10 to 40°C for 10 min, but approximately 60% of the activity is lost at 50°C Trichoderma reesei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
assay at Trichoderma reesei

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 9 stable over a broad when treated at 4°C for 24 h Trichoderma reesei