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Literature summary for 2.4.1.8 extracted from

  • Huewel, S.; Haalck, L.; Conrath, N.; Spener, F.
    Production and stabilization of pure maltose phosphorylase from Lactobacillus brevis for sensing inorganic phosphate (1996), Ann. N. Y. Acad. Sci., 799, 701-706.
    View publication on PubMed

Application

Application Comment Organism
biotechnology enzyme based biosensor for phosphate Levilactobacillus brevis

General Stability

General Stability Organism
carbohydrates, polyhydroxy alcohols, polymers stabilize during freeze-drying 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
-20°C, several months without loss of activity 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