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Literature summary extracted from

  • Lafond, M.; Sulzenbacher, G.; Freyd, T.; Henrissat, B.; Berrin, J.G.; Garron, M.L.
    The quaternary structure of a glycoside hydrolase dictates specificity toward beta-glucans (2016), J. Biol. Chem., 291, 7183-7194.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.73 the structure of Gluc5_26A adopts a stable trimeric quaternary structure also observable in solution. The N-terminal region protrudes into the active site of an adjacent monomer. The N-terminus governs the substrate specificity of Gluc5_26A. Its deletion opens the enzyme cleft at the -3 subsite and turns the enzyme into an endo-beta(1,4)-glucanase Saccharophagus degradans

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.73 additional information deletion of the N-terminal sequence up to residue Ser38. The mutant is devoid of the helix-turn motif interacting with residues of the substrate-binding cleft at the level of subsite -3. The mutation uncovers the enzyme cleft at the -3 subsite and turns the enzyme into an endo-beta(1,4)-glucanase Saccharophagus degradans

General Stability

EC Number General Stability Organism
3.2.1.73 the enzyme is able to conserve its activity after a drastic treatment with 500 mM NaOH, and the only way to stop enzyme activity is treatment with 8 M urea Saccharophagus degradans

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.73 Saccharophagus degradans Q21KE5
-
-
3.2.1.73 Saccharophagus degradans DSM 17024 Q21KE5
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.73 barley beta-glucan + H2O
-
Saccharophagus degradans Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH final products ?
3.2.1.73 barley beta-glucan + H2O
-
Saccharophagus degradans DSM 17024 Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH final products ?
3.2.1.73 cellopentaose + H2O
-
Saccharophagus degradans cellobiose + D-glucose with N-terminal deletion mutant, products are cellotriose and cellobiose ?
3.2.1.73 cellopentaose + H2O
-
Saccharophagus degradans DSM 17024 cellobiose + D-glucose with N-terminal deletion mutant, products are cellotriose and cellobiose ?
3.2.1.73 Glc-beta(1,4)-Glc-beta(1,4)-Glc-beta(1,3)-Glc + H2O
-
Saccharophagus degradans cellobiose + laminaribiose with N-terminal deletion mutant, products are cellotriose and D-glucose ?
3.2.1.73 Glc-beta(1,4)-Glc-beta(1,4)-Glc-beta(1,3)-Glc + H2O
-
Saccharophagus degradans DSM 17024 cellobiose + laminaribiose with N-terminal deletion mutant, products are cellotriose and D-glucose ?
3.2.1.73 lichenan + H2O
-
Saccharophagus degradans cellobiose + Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH final products ?
3.2.1.73 lichenan + H2O
-
Saccharophagus degradans DSM 17024 cellobiose + Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH final products ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.73 Cel5F
-
Saccharophagus degradans
3.2.1.73 Gluc5_26A
-
Saccharophagus degradans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.73 30
-
-
Saccharophagus degradans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.73 7
-
-
Saccharophagus degradans