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Literature summary for 3.2.1.20 extracted from

  • Dimitrijevic, A.; Velickovic, D.; Milosavic, N.; Bezbradica, D.
    Specificity of maltase to maltose in three different directions of reaction: hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis (2012), Biotechnol. Prog., 28, 1450-1456.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.27
-
4-nitrophenyl alpha-D-glucopyranoside pH 6.6, 37°C Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
63000
-
x * 63000, SDS-PAGE Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P53341
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
100
-
pH 6.6, 37°C Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl alpha-D-glucopyranoside + H2O
-
Saccharomyces cerevisiae 4-nitrophenol + D-glucose
-
?
additional information enzyme additionally catalyses transglucosylation of vanillyl alcohol, EC 2.4.1. The reaction is very efficient with selectivity factor 149 and occurs by a ping-pong mechanism with inhibition by glucose acceptor. At low concentration of vanillyl alcohol, one additional transglucosylation product, alpha-isomaltoside of vanillyl alcohol, is detected, indicating that vanillyl alcohol glucoside is a product of the first transglucosylation reaction and a substrate for second. The rate of isomaltoside synthesis is two orders of magnitude smaller than glucoside synthesis Saccharomyces cerevisiae ?
-
?
additional information no substrate: isomaltose Saccharomyces cerevisiae ?
-
?

Subunits

Subunits Comment Organism
? x * 63000, SDS-PAGE Saccharomyces cerevisiae