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Literature summary for 1.1.5.9 extracted from

  • Shiota, M.; Yamazaki, T.; Yoshimatsu, K.; Kojima, K.; Tsugawa, W.; Ferri, S.; Sode, K.
    An Fe-S cluster in the conserved Cys-rich region in the catalytic subunit of FAD-dependent dehydrogenase complexes (2016), Bioelectrochemistry, 112, 178-183.
    View publication on PubMed
Search for more literature for 1.1.5.9

Protein Variants

Protein Variants Comment Organism
C212S inactive Burkholderia cepacia
C213S the mutant shows 68% of wild type activity Burkholderia cepacia
C218S inactive Burkholderia cepacia
C222S inactive Burkholderia cepacia

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.97
-
 D-glucose wild type enzyme, at pH 7.0, temperature not specified in the publication Burkholderia cepacia
0.99
-
 D-glucose mutant enzyme C213S, at pH 7.0, temperature not specified in the publication Burkholderia cepacia

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
-
 Burkholderia cepacia

Organism

Organism UniProt Comment Textmining
Burkholderia cepacia
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HisTrap nickel affinity chromatography Burkholderia cepacia

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + 2,6-dichlorophenolindophenol
-
 Burkholderia cepacia D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
 ?

Subunits

Subunits Comment Organism
? x * 59832, catalytic subunit, calculated from amino acid sequence Burkholderia cepacia

Synonyms

Synonyms Comment Organism
FAD dependent glucose dehydrogenase
-
 Burkholderia cepacia
FADGDH
-
 Burkholderia cepacia

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Burkholderia cepacia
[3Fe-4S]-center
-
 Burkholderia cepacia