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Literature summary for 1.1.5.2 extracted from

  • James, P.L.; Anthony, C.
    The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli (2003), Biochim. Biophys. Acta, 1647, 200-205.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D354N site-directed mutagenesis, 9% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme Escherichia coli
D354N/N355D site-directed mutagenesis, 10% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme Escherichia coli
N355D site-directed mutagenesis, 25% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Ba2+ competitive to Mg2+, wild-type enzyme Escherichia coli
Ca2+ competitive to Mg2+, wild-type enzyme Escherichia coli
Mg2+ competitive to Ca2+, Sr2+, or Ba2+, mutants D354N, N355D, and D354N/N355D Escherichia coli
Sr2+ competitive to Mg2+, wild-type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information metal binding kinetics, wild-type and mutant enzymes, Km for the different substrates of mutant enzymes with different metal ions bound, overview Escherichia coli
2.8
-
D-glucose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli
3.5
-
2-deoxy-D-glucose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli
17
-
D-xylose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli
17.5
-
D-galactose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli
31
-
L-arabinose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli
79
-
3-O-methyl-D-glucose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli
116
-
D-mannose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli
166
-
D-ribose recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Escherichia coli 16020
-
periplasm
-
Escherichia coli
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ba2+ mutants D354N, N355D, and D354N/N355D Escherichia coli
Ca2+ mutants D354N, N355D, and D354N/N355D Escherichia coli
Mg2+ required, bound at the active site, cannot be substituted by Ca2+, Sr2+, or Ba2+ Escherichia coli
Sr2+ mutants D354N, N355D, and D354N/N355D Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose + ubiquinone Escherichia coli transfers electrons to the cytochrome oxidase through ubiquinone in the electron transport chain D-glucono-1,5-lactone + ubiquinol
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P15877
-
-

Reaction

Reaction Comment Organism Reaction ID
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol active site structure Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-deoxy-D-glucose + ubiquinone
-
Escherichia coli 2-deoxy-D-glucono-1,5-lactone + ubiquinol
-
?
3-O-methyl-D-glucose + ubiquinone
-
Escherichia coli 3-O-methyl-D-glucono-1,5-lactone + ubiquinol
-
?
D-galactose + ubiquinone
-
Escherichia coli D-galactono-1,5-lactone + ubiquinol
-
?
D-glucose + ubiquinone
-
Escherichia coli D-glucono-1,5-lactone + ubiquinol
-
?
D-glucose + ubiquinone transfers electrons to the cytochrome oxidase through ubiquinone in the electron transport chain Escherichia coli D-glucono-1,5-lactone + ubiquinol
-
?
D-mannose + ubiquinone
-
Escherichia coli ? + ubiquinol
-
?
D-ribose + ubiquinone
-
Escherichia coli ? + ubiquinol
-
?
D-xylose + ubiquinone
-
Escherichia coli D-xylono-1,5-lactone + ubiquinol
-
?
L-arabinose + ubiquinone
-
Escherichia coli L-arabino-1,5-lactone + ubiquinol
-
?
additional information substrate specificity of recombinant wild-type and mutant enzymes Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
GDH
-
Escherichia coli
membrane glucose dehydrogenase
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40.5
-
10 min, 50% inactivation of recombinant mutant D354N apoenzyme Escherichia coli
40.8
-
10 min, 50% inactivation of recombinant wild-type apoenzyme Escherichia coli
41
-
10 min, 50% inactivation of recombinant mutant D354N/N355D apoenzyme Escherichia coli
43.2
-
10 min, 50% inactivation of recombinant mutant N355D apoenzyme Escherichia coli
48.6
-
10 min, 50% inactivation of recombinant mutant D354N/N355D holoenzyme Escherichia coli
49
-
10 min, 50% inactivation of recombinant mutant D354N holoenzyme Escherichia coli
51
-
10 min, 50% inactivation of recombinant wild-type holoenzyme Escherichia coli
55
-
10 min, 50% inactivation of recombinant mutant N355D holoenzyme Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone i.e. PQQ, dependent on, Escherichia coli needs to be reconstituted with PQQ for activity Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information inhibitory effects of the different metal ions on recombinant wild-type and mutant enzymes Escherichia coli