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Literature summary extracted from

  • Tsumuraya, Y.; Brewer, C.F.; Hehre, E.J.
    Substrate-induced activation of maltose phosphorylase: interaction with the anomeric hydroxyl group of alpha-maltose and alpha-D-glucose controls the enzymes glucosyltransferase activity (1990), Arch. Biochem. Biophys., 281, 58-65.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.8 additional information
-
 additional information kinetic studies Levilactobacillus brevis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.8 maltose + phosphate Levilactobacillus brevis catalyzes narrowly defined set of glycosyl transfer reactions with little hydrolysis beta-D-glucose 1-phosphate + D-glucose
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.8 Levilactobacillus brevis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.8 partial Levilactobacillus brevis

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.1.8 maltose + phosphate = D-glucose + beta-D-glucose 1-phosphate mechanism Levilactobacillus brevis
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.8 14.9
-
-
 Levilactobacillus brevis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.8 beta-D-glucose 1-phosphate + D-glucose
-
 Levilactobacillus brevis maltose + phosphate
-
 r
2.4.1.8 beta-D-glucosylfluoride + alpha-D-glucose no acceptors are methyl-alpha-D-glucoside, D-glucal, beta-D-glucose, salicin and alpha/beta-D-glucosylfluoride Levilactobacillus brevis alpha-maltose + HF
-
 ?
2.4.1.8 maltose + arsenate no substrate: alpha/beta-maltosyl fluoride, methyl-alpha-maltoside, maltal Levilactobacillus brevis D-glucose + D-glucose + arsenate
-
 ?
2.4.1.8 maltose + phosphate
-
 Levilactobacillus brevis beta-D-glucose 1-phosphate + D-glucose
-
 r
2.4.1.8 maltose + phosphate catalyzes narrowly defined set of glycosyl transfer reactions with little hydrolysis Levilactobacillus brevis beta-D-glucose 1-phosphate + D-glucose
-
 ?
2.4.1.8 additional information no substrate: beta-maltose, alpha-maltosylfluoride Levilactobacillus brevis ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.8 30
-
 assay at Levilactobacillus brevis