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Literature summary extracted from

  • Sode, K.; Shirahane, M.; Yoshida, H.
    Construction and characterization of a linked-dimeric pyrroloquinoline quinone glucose dehydrogenase (1999), Biotechnol. Lett., 21, 707-710.
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
1.1.5.2 additional information construction of a gene consisting of two identical subunits linked together by a DNA segment coding linker peptide region and production of a linked-dimeric enzyme, the linked-dimeric enzyme shows higher thermal stability than native dimeric enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.5.2 12
-
 lactose pH 7.0, 25°C, linked dimeric enzyme Escherichia coli
1.1.5.2 20
-
 D-glucose pH 7.0, 25°C, linked dimeric enzyme Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.2 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.5.2 linked-dimeric enzyme Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.2 lactose + ubiquinone
-
 Escherichia coli ? + ubiquinol
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.5.2 45
-
 20 min, 20% loss of activity of native enzyme, about 50% loss of activity of linked-dimeric enzyme Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.2 pyrroloquinoline quinone prosthetic group Escherichia coli