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Literature summary for 2.4.1.5 extracted from

  • Wang, C.; Zhang, H.B.; Li, M.Q.; Hu, X.Q.; Li, Y.
    Functional analysis of truncated and site-directed mutagenesis dextransucrases to produce different type dextrans (2017), Enzyme Microb. Technol., 102, 26-34 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
the recombinant wild-type enzyme and mutant proteins are expressed from Escherichia coli BL21 star (DE3) Leuconostoc mesenteroides

Protein Variants

Protein Variants Comment Organism
A670V the mutation increases the percentage of alpha(1->3) linkages (9% at most) and decreases the percentage of alpha(1->6) linkages in the product Leuconostoc mesenteroides
D590A the mutation introduces a decrease the percentage of alpha(1->3) linkage in the product Leuconostoc mesenteroides
E664K the mutation introduces additional alpha(1->3) glycosidic linkages and also some additional alpha(1->2) glycosidic linkages, the mutation decreases the percentage of alpha(1->6) linkages in the product Leuconostoc mesenteroides
additional information DSR-S1-DELTAV (residues 1-1425) and DSR-S2-DELTA(V) (residues 1-1279) are constructed by deleting partial YG repeats of domain V. DSR-S3-DELTA(V) (residues 1-1160), DSR-S-DELTA IV (residues 1-1124), and DSR-S-DELTA(B) (residues 1-1110) are constructed by deleting the relevant fragments from C-terminal ends. The truncation mutant DSR-S1-DELTA(A) (residues 1-1029) is constructed by deleting partial domain A while containing complete conserved Motif regions I. DSR-S2-DELTA(A) (residues 1-1022) is constructed by deleting partial domain A including conserved Motif regions I. DSRS3-DELTA(A) (residues 1-1000) is constructed by deleting more domain A fragment, allowing further investigation of the functions of C-terminal end domain. 102 amino acids of C-terminal end has no effect on dextran synthesis, but it will improve enzyme protein expression by deleting these amino acids. After further deletion, polysaccharidesynthesizing capability of dextransucrase will be inhibited. With the addition of maltose as postreceptors, truncated enzymes undergoes glycosylation reaction and transferred glucosyl from sucrose to acceptor effectively. By deleting the 417 amino acid fragment, its oligosaccharide synthesizing capability significantly increases. This is an effective way to make use of dextransucrase for prebiotic synthesis Leuconostoc mesenteroides
N555Y the mutation increases the percentage of alpha(1->3) linkages (9% at most) and decreases the percentage of alpha(1->6) linkages in the product Leuconostoc mesenteroides
Q1029K the mutation has no significant effect on the linkage specificity Leuconostoc mesenteroides
Q666R the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreases the percentage of alpha(1->6) linkages in the product Leuconostoc mesenteroides
S663N the mutation increases the percentage of alpha(1->3) linkages (9% at most) and decreases the percentage of alpha(1->6) linkages in the product Leuconostoc mesenteroides
V553A the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreased the production of alpha(1->3) linkage polysaccharides Leuconostoc mesenteroides
V556I the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreased the production of alpha(1->3) linkage polysaccharides Leuconostoc mesenteroides
V665A the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreases the percentage of alpha(1->6) linkages in the product Leuconostoc mesenteroides
W591G the mutation introduces a decrease the percentage of alpha(1->3) linkage in the product Leuconostoc mesenteroides

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics analysis of continuously truncated enzymes with sucrose and maltose as the substrate Leuconostoc mesenteroides

Organism

Organism UniProt Comment Textmining
Leuconostoc mesenteroides Q2I2N5
-
-
Leuconostoc mesenteroides 0326 Q2I2N5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Leuconostoc mesenteroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + maltose
-
Leuconostoc mesenteroides D-fructose + ?
-
?
sucrose + maltose
-
Leuconostoc mesenteroides 0326 D-fructose + ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
-
Leuconostoc mesenteroides

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information kinetics analysis of continuously truncated enzymes with sucrose and maltose as the substrate Leuconostoc mesenteroides

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4
-
-
Leuconostoc mesenteroides