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Literature summary for 1.1.3.4 extracted from

  • Petrovic, D.; Frank, D.; Kamerlin, S.C.L.; Hoffmann, K.; Strodel, B.
    Shuffling active site substate populations affects catalytic activity the case of glucose oxidase (2017), ACS Catal., 7, 6188-6197 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.3.4

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Pichia pastoris KM71H Aspergillus niger

Crystallization (Commentary)

Crystallization (Comment) Organism
vapor diffusion sitting drop method Aspergillus niger

Protein Variants

Protein Variants Comment Organism
T30V/I94V/A162T 2.9fold increase in kcat/Km, decrease in t1/2(60°C) by 1.5°C Aspergillus niger
T30V/I94V/A162T/R537K/M556V 4.0fol2.6fold increase in kcat/Km, increase in t1/2(60°C) by 5.25°C Aspergillus niger

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
14.98
-
 beta-D-glucose pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T Aspergillus niger
18.54
-
 beta-D-glucose pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T/R537K/M556V Aspergillus niger
19.76
-
 beta-D-glucose pH 5.5, temperature not specified in the publication, mutant enzyme T30V/R37K/I94V/V106I/A162T/M556V Aspergillus niger
28.26
-
 beta-D-glucose pH 5.5, temperature not specified in the publication, wild-type enzyme Aspergillus niger

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
beta-D-glucose + O2 Aspergillus niger
-
 D-glucono-1,5-lactone + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Aspergillus niger P13006
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Aspergillus niger

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-glucose + O2
-
 Aspergillus niger D-glucono-1,5-lactone + H2O2
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 t1/2: 10.5 min (wild-type enzyme), 9.0 (mutant enzyme T30V/I94V/A162T), 11.74 (mutant enzyme T30V/I94V/A162T/R537K/M556V), 15.75 (mutant enzyme T30V/R37K/I94V/V106I/A162T/M556V) Aspergillus niger

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
189.38
-
 beta-D-glucose pH 5.5, temperature not specified in the publication, wild-type enzyme Aspergillus niger
291.82
-
 beta-D-glucose pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T Aspergillus niger
345.16
-
 beta-D-glucose pH 5.5, temperature not specified in the publication, mutant enzyme T30V/R37K/I94V/V106I/A162T/M556V Aspergillus niger
498.34
-
 beta-D-glucose pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T/R537K/M556V Aspergillus niger

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.7
-
 beta-D-glucose pH 5.5, temperature not specified in the publication, wild-type enzyme Aspergillus niger
17.5
-
 beta-D-glucose pH 5.5, temperature not specified in the publication, mutant enzyme T30V/R37K/I94V/V106I/A162T/M556V Aspergillus niger
19.5
-
 beta-D-glucose pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T Aspergillus niger
26.9
-
 beta-D-glucose pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T/R537K/M556V Aspergillus niger