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Literature summary for 2.4.1.7 extracted from

  • Schwarz, A.; Nidetzky, B.
    Asp-196-->Ala mutant of Leuconostoc mesenteroides sucrose phosphorylase exhibits altered stereochemical course and kinetic mechanism of glucosyl transfer to and from phosphate (2006), FEBS Lett., 580, 3905-3910.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
D196A inactive mutant enzyme. External azide partly complements the catalytic defect in D196A while formate, acetate and halides can not restore activity. The mutant utilizes azide to convert alpha-D-glucose 1-phosphate into beta-D-glucose 1-azide, reflecting a change in stereochemical course of glucosyl transfer from alpha-retaining in wild-type to inverting in D196A. Phosphorolysis of beta-D-glucose 1-azide by D196A occurrs through a ternary complex kinetic mechanism, in contrast to the wild-type whose reactions feature a common glucosyl enzyme intermediate and ping-pong kinetics Leuconostoc mesenteroides

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1
-
 sucrose 30°C, pH 6.0, wild-type enzyme Leuconostoc mesenteroides
4.4
-
 phosphate 30°C, pH 6.0, wild-type enzyme Leuconostoc mesenteroides
8.6
-
 phosphate 30°C, pH 6.0, mutant enzyme D196A Leuconostoc mesenteroides

Organism

Organism UniProt Comment Textmining
Leuconostoc mesenteroides
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Leuconostoc mesenteroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + phosphate
-
 Leuconostoc mesenteroides D-fructose + alpha-D-glucose 1-phosphate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00026
-
 sucrose 30°C, pH 6.0, mutant enzyme D196A Leuconostoc mesenteroides
105
-
 sucrose 30°C, pH 6.0, wild-type enzyme Leuconostoc mesenteroides