Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Saul, D.J.; Williams, L.C.; Grayling, R.A.; Chamley, L.W.; Love, D.R.; Bergquist, P.L.
    celB, a gene coding for a bifunctional cellulase from the extreme thermophile "Caldocellum saccharolyticum" (1990), Appl. Environ. Microbiol., 56, 3117-3124.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.4 expression in Escherichia coli Caldicellulosiruptor saccharolyticus
3.2.1.91 expression in Escherichia coli Caldicellulosiruptor saccharolyticus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.4 additional information construction of deletion mutants expressing solely the carboxyterminal domain containing the endoglucanase activity. Temperature optimum and stability of the deletion mutants are the same as wild-type Caldicellulosiruptor saccharolyticus
3.2.1.91 additional information construction of deletion mutants expressing solely the aminoterminal domain containing the exoglucanase activity. Temperature optimum and stability of the deletion mutants are the same as wild-type Caldicellulosiruptor saccharolyticus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.4 118000 120000 PAGE Caldicellulosiruptor saccharolyticus
3.2.1.91 118000 120000 PAGE Caldicellulosiruptor saccharolyticus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.4 Caldicellulosiruptor saccharolyticus P10474 bifunctional enzyme, shows both endoglucanase and exoglucanase activities, EC 3.2.1.4 and 3.2.1.91, respectively
-
3.2.1.91 Caldicellulosiruptor saccharolyticus P10474 bifunctional enzyme, shows both endoglucanase and exoglucanase activities, EC 3.2.1.4 and 3.2.1.91, respectively
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.4 carboxymethylcellulose + H2O
-
 Caldicellulosiruptor saccharolyticus ?
-
 ?
3.2.1.4 cellulose + H2O
-
 Caldicellulosiruptor saccharolyticus D-glucose + ? enzyme is able to degrade crystalline cellulose to glucose ?
3.2.1.91 4-methylumbelliferyl beta-D-cellobioside + H2O
-
 Caldicellulosiruptor saccharolyticus 4-methylumbelliferone + beta-D-cellobiose
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.4 More the exoglucanase activity is located in the amino-terminal domain of the enzyme and the endoglucanase activity is located in the carboxy-terminal domain Caldicellulosiruptor saccharolyticus
3.2.1.91 More the exoglucanase activity is located in the amino-terminal domain of the enzyme and the endoglucanase activity is located in the carboxy-terminal domain Caldicellulosiruptor saccharolyticus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.4 85
-
-
 Caldicellulosiruptor saccharolyticus
3.2.1.91 85
-
-
 Caldicellulosiruptor saccharolyticus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.4 70
-
 half-life 29 h Caldicellulosiruptor saccharolyticus
3.2.1.91 70
-
 half-life 29 h Caldicellulosiruptor saccharolyticus