Literature summary for 1.1.1.47 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.

General Stability

General Stability	Organism
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

Organism

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]

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

Molecular Weight [Da]

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

Organism

Organism	UniProt	Comment	Textmining
Priestia megaterium	-	-	-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

pH Optimum

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

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Priestia megaterium
NADP+	-	Priestia megaterium

pI Value

Organism	Comment	pI Value Maximum	pI Value
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
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