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Literature summary for 1.1.5.2 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

Protein Variants Comment Organism
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]

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

Localization

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone prosthetic group Escherichia coli
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