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Literature summary extracted from

  • Cozier, G.E.; Salleh, R.A.; Anthony, C.
    Characterization of the membrane quinoprotein glucose dehydrogenase from Escherichia coli and characterization of a site-directed mutant in which histidine-262 has been changed to tyrosine (1999), Biochem. J., 340, 639-647.
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
1.1.5.2 H262Y greatly diminished catalytic efficiency for all substrates, rate of electron transfer to oxygen is unaffected, 230fold increased Km value for glucose Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.5.2 1.3
-
6-deoxy-D-glucose wild-type enzyme Escherichia coli
1.1.5.2 1.6
-
2-deoxy-D-glucose wild-type enzyme Escherichia coli
1.1.5.2 2.1
-
D-glucose wild-type enzyme Escherichia coli
1.1.5.2 2.5
-
D-allose wild-type enzyme Escherichia coli
1.1.5.2 8.3
-
D-fucose wild-type enzyme Escherichia coli
1.1.5.2 9.5
-
2-amino-D-glucose wild-type enzyme Escherichia coli
1.1.5.2 10.8
-
3-deoxy-D-glucose wild-type enzyme Escherichia coli
1.1.5.2 17.7
-
D-melibiose wild-type enzyme Escherichia coli
1.1.5.2 22
-
D-xylose wild-type enzyme Escherichia coli
1.1.5.2 32
-
2-deoxy-D-glucose mutant enzyme H262 Escherichia coli
1.1.5.2 39
-
D-galactose wild-type enzyme Escherichia coli
1.1.5.2 46
-
L-arabinose wild-type enzyme Escherichia coli
1.1.5.2 78
-
D-mannose wild-type enzyme Escherichia coli
1.1.5.2 79
-
3-O-methyl-D-glucose wild-type enzyme Escherichia coli
1.1.5.2 100
-
L-Lyxose wild-type enzyme Escherichia coli
1.1.5.2 110
-
D-ribose wild-type enzyme Escherichia coli
1.1.5.2 460
-
D-glucose mutant enzyme H262Y Escherichia coli
1.1.5.2 810
-
D-allose mutant enzyme H262Y Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.2 membrane
-
Escherichia coli 16020
-

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.5.2 wild-type and mutant enzyme H262Y Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.2 2-amino-D-glucose + pyrroloquinoline quinone
-
Escherichia coli 2-amino-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
?
1.1.5.2 2-deoxy-D-glucose + pyrroloquinoline quinone
-
Escherichia coli 2-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
?
1.1.5.2 3-deoxy-D-glucose + pyrroloquinoline quinone
-
Escherichia coli 3-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
?
1.1.5.2 3-O-methyl-D-glucose + pyrroloquinoline quinone
-
Escherichia coli 3-O-methyl-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
?
1.1.5.2 6-deoxy-D-glucose + pyrroloquinoline quinone
-
Escherichia coli 6-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
?
1.1.5.2 D-allose + pyrroloquinoline quinone
-
Escherichia coli D-allono-1,5-lactone + pyrroloquinoline quinol
-
?
1.1.5.2 D-fucose + pyrrolquinoline quinone
-
Escherichia coli 6-deoxy-D-galactono-1,5-lactone + pyrroloquinoline quinol
-
?
1.1.5.2 D-galactose + pyrroloquinoline quinone
-
Escherichia coli D-galactono-1,5-lactone + pyrroloquinoline quinol
-
?
1.1.5.2 D-glucose + pyrroloquinoline quinone
-
Escherichia coli D-glucono-1,5-lactone + pyrroloquinoline quinol
-
?
1.1.5.2 D-mannose + pyrroloquinoline quinone
-
Escherichia coli D-mannono-1,5-lactone + pyrroloquinoline quinol
-
?
1.1.5.2 D-melibiose + pyrroloquinoline quinone
-
Escherichia coli ?
-
?
1.1.5.2 D-ribose + pyrroloquinoline quinone
-
Escherichia coli D-ribono-1,5-lactone + pyrroloquinoline quinol
-
?
1.1.5.2 D-xylose + pyrroloquinoline quinone
-
Escherichia coli D-xylono-1,5-lactone + pyrroloquinoline quinol
-
?
1.1.5.2 L-arabinose + pyrroloquinoline quinone
-
Escherichia coli L-arabino-1,5-lactone + pyrroloquinoline quinol
-
?
1.1.5.2 L-lyxose + pyrroloquinoline quinone
-
Escherichia coli ?
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.2 pyrroloquinoline quinone prosthetic group Escherichia coli
1.1.5.2 pyrroloquinoline quinone during the processing of pyrroloquinoline quinone into the apoenzyme to give active enzyme, its affinity is markedly dependent on the pH, four groups with pK values between pH 7 and pH 8 are involved Escherichia coli