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Literature summary extracted from

  • Nakabayashi, M.; Kataoka, M.; Mishima, Y.; Maeno, Y.; Ishikawa, K.
    Structural analysis of beta-glucosidase mutants derived from a hyperthermophilic tetrameric structure (2014), Acta Crystallogr. Sect. D, 70, 877-888.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.21 expressed in Escherichia coli BL21 Pyrococcus furiosus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.21 mutant enzyme R170A/R220A/Y227F, hanging-drop vapour-diffusion method, the structure is determined at 2.35 A resolution, stable homotetrameric structure, a dimeric form of the enzyme is constructed and its crystal structure is solved at a resolution of 1.70 A Pyrococcus furiosus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.21 R170A/R220A/Y227F mutant enzyme occurs as dimer Pyrococcus furiosus
3.2.1.21 R170A/R220A/Y227F/R448E mutant enzyme occurs as monomer, melting temperature is decreased form 110°C for the wild-type enzyme to 73-75°C for the mutant enzyme Pyrococcus furiosus
3.2.1.21 R170A/R220A/Y227F/R449R mutant enzyme occurs as monomer, melting temperature is decreased form 110°C for the wild-type enzyme to 73-75°C for the mutant enzyme Pyrococcus furiosus
3.2.1.21 R170A/R220A/Y227F/R459G mutant enzyme occurs as monomer, melting temperature is decreased form 110°C for the wild-type enzyme to 73-75°C for the mutant enzyme Pyrococcus furiosus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.21 23600
-
 wild-type enzyme tetramer, gel filtration Pyrococcus furiosus
3.2.1.21 50000
-
 mutant enzyme R170A/R220A/Y227F/R459G, monomer, gel filtration Pyrococcus furiosus
3.2.1.21 55000
-
 2 * 55000, SDS-PAGE after heating at 95°C,mutant enzyme R170A/R220A/Y227F Pyrococcus furiosus
3.2.1.21 71000
-
 mutant enzyme R170A/R220A/Y227F/R448E, monomer, gel filtration Pyrococcus furiosus
3.2.1.21 96000
-
 mutant enzyme R170A/R220A/Y227F/R449R, monomer, gel filtration Pyrococcus furiosus
3.2.1.21 136000
-
 mutant enzyme R170A/R220A/Y227F, dimer, gel filtration Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.21 Pyrococcus furiosus Q51723
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.21 wild-type and mutant enzyme R170A/R220A/Y227F Pyrococcus furiosus

Subunits

EC Number Subunits Comment Organism
3.2.1.21 dimer 2 * 55000, SDS-PAGE after heating at 95°C,mutant enzyme R170A/R220A/Y227F Pyrococcus furiosus
3.2.1.21 monomer 1 * 50000, mutant enzyme R170A/R220A/Y227F/R459G, SDS-PAGE Pyrococcus furiosus
3.2.1.21 monomer 1 * 71000, mutant enzyme R170A/R220A/Y227F/R448E, SDS-PAGE Pyrococcus furiosus
3.2.1.21 monomer 1 * 96000, mutant enzyme R170A/R220A/Y227F/R449R, SDS-PAGE Pyrococcus furiosus
3.2.1.21 tetramer wild-type enzyme Pyrococcus furiosus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.21 BGLPf
-
 Pyrococcus furiosus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.21 additional information
-
 oligomerization contributes to thermostability Pyrococcus furiosus
3.2.1.21 70 80 mutant enzymes R170A/R220A/Y227F/R448E, R170A/R220A/Y227F/R449R or R170A/R220A/Y227F/R459G are immediately inactivated Pyrococcus furiosus
3.2.1.21 73 75 melting temperature of mutant enzymes R170A/R220A/Y227F/R448E, R170A/R220A/Y227F/R449R or R170A/R220A/Y227F/R459G Pyrococcus furiosus
3.2.1.21 102
-
 Tm-value of mutant enzyme R170A/R220A/Y227F Pyrococcus furiosus
3.2.1.21 110
-
 melting temperature of tetrameric wild-type enzyme Pyrococcus furiosus