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Literature summary for 2.4.1.8 extracted from

  • Huwel, S.; Haalck, L.; Conrath, N.; Spener, F.
    Maltose phosphorylase from Lactobacillus brevis: purification, characterization, and application in a biosensor for ortho-phosphate (1997), Enzyme Microb. Technol., 21, 413-420.
    View publication on PubMed
Search for more literature for 2.4.1.8

Application

Application Comment Organism
biotechnology enzyme based biosensor for phosphate Levilactobacillus brevis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.9
-
 maltose
-
 Levilactobacillus brevis
21.8
-
 phosphate
-
 Levilactobacillus brevis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
196000
-
 gel filtration Levilactobacillus brevis

Organism

Organism UniProt Comment Textmining
Levilactobacillus brevis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Levilactobacillus brevis

Storage Stability

Storage Stability Organism
4°C, 10 mM phosphate, pH 6.5, up to 6 months with minimal losses Levilactobacillus brevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
maltose + phosphate
-
 Levilactobacillus brevis beta-D-glucose 1-phosphate + D-glucose
-
 ?

Subunits

Subunits Comment Organism
dimer 2 x 86000, SDS-PAGE Levilactobacillus brevis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
36
-
-
 Levilactobacillus brevis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
 Levilactobacillus brevis

Cofactor

Cofactor Comment Organism Structure
additional information no pyridoxal 5'-phosphate required Levilactobacillus brevis