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Literature summary extracted from

  • Nakabayashi, M.; Kataoka, M.; Watanabe, M.; Ishikawa, K.
    Monomer structure of a hyperthermophilic beta-glucosidase mutant forming a dodecameric structure in the crystal form (2014), Acta Crystallogr. Sect. F, 70, 854-859.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.B28 recombinant mutant that lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449Kis expressed in Escherichia coli BL21 Pyrococcus furiosus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.B28 hanging-drop vapour-diffusion method, a monomeric form of the enzyme is constructed by removing the C-terminal region (the mutant lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K) of the enzyme and its crystal structure is solved at a resolution of 2.8 A in space group Pyrococcus furiosus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.B28 additional information a mutant lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K forms a unique dodecameric structure consisting of two hexameric rings in the asymmetric unit of the crystal. The lack of the C-terminal region does not affect the activity of the enzyme, but disrupts its oligomeric state and hyperthermostability Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.B28 Pyrococcus furiosus Q51723
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.B28
-
 Pyrococcus furiosus

Subunits

EC Number Subunits Comment Organism
3.2.1.B28 dodecamer a monomeric form of the enzyme is constructed by removing the C-terminal region of the enzyme (the mutant lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K). The mutant enzyme forms a unique dodecameric structure consisting of two hexameric rings in the asymmetric unit of the crystal Pyrococcus furiosus
3.2.1.B28 monomer a monomeric form of the enzyme is constructed by removing the C-terminal region of the enzyme (the mutant lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K). The mutant enzyme forms a unique dodecameric structure consisting of two hexameric rings in the asymmetric unit of the crystal Pyrococcus furiosus
3.2.1.B28 tetramer the native enzyme forms a stable tetrameric structure Pyrococcus furiosus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.B28 BGLPf
-
 Pyrococcus furiosus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.B28 75 80 the mutant enzyme that lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K is immediately inactivated between 75 and 80°C Pyrococcus furiosus
3.2.1.B28 85
-
 wild-type enzyme is stable beyond 85°C Pyrococcus furiosus
3.2.1.B28 110
-
 Tm-value of wild-type enzyme Pyrococcus furiosus