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Literature summary extracted from

  • Pauly, H.E.; Pfleiderer, G.
    D-Glucose dehydrogenase from Bacillus megaterium M1286: purification, properties and structure (1975), Hoppe-Seyler's Z. Physiol. Chem., 356, 1613-1623.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.1.1.47 purified enzyme is indefinitely stable in the frozen state or in solution at pH 6.5 containing 3 M NaCl and a protein concentration of more than 0.5 mg/ml. Diluted enzyme solutions can be stabilized to the same degree by adding 0.5% polyvinylpyrrolidone. Any reduction of the ionic strength of enzyme solution leads to an irreversible inactivation which can be only partially prevented by additrion of polyvinylpyrrolidone Priestia megaterium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.47 4.5
-
NAD+ pH 9.0, 25°C Priestia megaterium
1.1.1.47 47.5
-
beta-D-glucose pH 9.0, 25°C Priestia megaterium

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.47 30000
-
4 * 30000, SDS-PAGE Priestia megaterium
1.1.1.47 116000
-
gel filtration Priestia megaterium

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.47 Priestia megaterium
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.47 hydroxyapatite, QAE-Sephadex Priestia megaterium

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.47 550
-
-
Priestia megaterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.47 2-amino-2-deoxy-D-glucose + NAD+ 14% of the activity with D-glucose Priestia megaterium 2-amino-2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
?
1.1.1.47 2-deoxy-D-glucose + NAD+ 114% of the activity with D-glucose Priestia megaterium 2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
?
1.1.1.47 beta-D-glucose + NAD+ the enzyme is highly specific for beta-D-glucose Priestia megaterium D-glucono-1,5-lactone + NADH + H+
-
?
1.1.1.47 beta-D-glucose + NADP+ the enzyme is highly specific for beta-D-glucose Priestia megaterium D-glucono-1,5-lactone + NADPH + H+
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.47 tetramer 4 * 30000, SDS-PAGE Priestia megaterium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.47 8
-
sharp decrease above, Tris-HCl buffer Priestia megaterium
1.1.1.47 9
-
acetate/borate buffer Priestia megaterium

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.47 NAD+
-
Priestia megaterium
1.1.1.47 NADP+
-
Priestia megaterium

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.1.1.47 Priestia megaterium isoelectric focusing, two protein bands: the major one is located at pH 6.0 and a very weak one is located at pH 4.7. After preincubation in 8 M urea, only the major band at pH 6.0 can be observed 4.8 4.7
1.1.1.47 Priestia megaterium isoelectric focusing, two protein bands: the major one is located at pH 6.0 and a very weak one is located at pH 4.7. After preincubation in 8 M urea, only the major band at pH 6.0 can be observed
-
6