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Literature summary for 1.1.5.2 extracted from

  • Igarashi, S.; Sode, K.
    Stabilization of quaternary structure of water-soluble quinoprotein glucose dehydrogenase (2003), Mol. Biotechnol., 24, 97-104.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
S145C site-directed mutagenesis, introduction of a Cys residue in each monomer of the enzyme leads to formation of an intersubunit disulfide bridge at the dimer interface resulting in 30fold increased thermal stability at 55°C compared to the wild-type enzyme Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble isozyme PQQGDH-B, water-soluble quinoprotein Escherichia coli
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-

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Subunits

Subunits Comment Organism
dimer
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Escherichia coli

Synonyms

Synonyms Comment Organism
glucose dehydrogenase
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Escherichia coli
PQQGDH-B
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Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
10 min, mutant S145C retaines 90% of wild-type activity Escherichia coli