Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Holland, J.T.; Lau, C.; Brozik, S.; Atanassov, P.; Banta, S.
    Engineering of glucose oxidase for direct electron transfer via site-specific gold nanoparticle conjugation (2011), J. Am. Chem. Soc., 133, 19262-19265.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.3.4 analysis the enzyme is useful as biosensor for glucose detection Aspergillus niger

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.4 A449C site-directed mutagenesis, the mutation results in almost completely diminished activity compared to the wild-type enzyme Aspergillus niger
1.1.3.4 E84C site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity Aspergillus niger
1.1.3.4 H447C site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity Aspergillus niger
1.1.3.4 additional information engineering of glucose oxidase by site-specific attachment of a maleimide-modified gold nanoparticle to the enzyme for enabling direct electrical communication between the conjugated enzyme and an electrode required for using the enzyme as biosensor, evaluation, overview Aspergillus niger
1.1.3.4 S307C site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity Aspergillus niger
1.1.3.4 T56V/T132S site-directed mutagenesis, the mutant shows improved catalytic efficiency. The protein has three native cysteines, of which two are involved in a disulfide bond and the third is a free cysteine, Cys 521 Aspergillus niger
1.1.3.4 T56V/T132S/C521S site-directed mutagenesis, the mutant shows improved catalytic efficiency, mutation C521S does not alter enzyme activity, but the attachment of AuNPs to the native free thiol is prevented Aspergillus niger
1.1.3.4 Y435C site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.4 additional information
-
 additional information steady-state kinetics, overview Aspergillus niger
1.1.3.4 6.3
-
 beta-D-glucose wild-type enzyme conjugated to gold nanoparticles, pH and temperature not specified in the publication Aspergillus niger
1.1.3.4 8.2
-
 beta-D-glucose mutant H447C conjugated to gold nanoparticles, pH and temperature not specified in the publication Aspergillus niger
1.1.3.4 15
-
 beta-D-glucose mutant H447C, pH and temperature not specified in the publication Aspergillus niger
1.1.3.4 96.4
-
 beta-D-glucose wild-type enzyme, pH and temperature not specified in the publication Aspergillus niger

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.4 beta-D-glucose + O2 Aspergillus niger GOx enzyme catalyzes the oxidation of glucose to gluconolactone via reduction of the FAD cofactor to FADH2. The reoxidation of FADH2 in the ping-pong mechanism is normally achieved using oxygen as the electron acceptor D-glucono-1,5-lactone + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.4 Aspergillus niger
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.4 beta-D-glucose + O2 GOx enzyme catalyzes the oxidation of glucose to gluconolactone via reduction of the FAD cofactor to FADH2. The reoxidation of FADH2 in the ping-pong mechanism is normally achieved using oxygen as the electron acceptor Aspergillus niger D-glucono-1,5-lactone + H2O2
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.4 22.8
-
 beta-D-glucose wild-type enzyme conjugated to gold nanoparticles, pH and temperature not specified in the publication Aspergillus niger
1.1.3.4 55.3
-
 beta-D-glucose mutant H447C conjugated to gold nanoparticles, pH and temperature not specified in the publication Aspergillus niger
1.1.3.4 152
-
 beta-D-glucose wild-type enzyme, pH and temperature not specified in the publication Aspergillus niger
1.1.3.4 425
-
 beta-D-glucose mutant H447C, pH and temperature not specified in the publication Aspergillus niger

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.4 FAD
-
 Aspergillus niger