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Literature summary for 3.2.1.91 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)

Cloned (Comment) Organism
expression in Escherichia coli Caldicellulosiruptor saccharolyticus

Protein Variants

Protein Variants Comment Organism
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]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
118000 120000 PAGE Caldicellulosiruptor saccharolyticus

Organism

Organism UniProt Comment Textmining
Caldicellulosiruptor saccharolyticus P10474 bifunctional enzyme, shows both endoglucanase and exoglucanase activities, EC 3.2.1.4 and 3.2.1.91, respectively
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methylumbelliferyl beta-D-cellobioside + H2O
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Caldicellulosiruptor saccharolyticus 4-methylumbelliferone + beta-D-cellobiose
-
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Subunits

Subunits Comment Organism
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]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
85
-
-
Caldicellulosiruptor saccharolyticus

Temperature Stability [°C]

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