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Literature summary for 2.4.1.390 extracted from

  • Chen, Y.; Dong, J.; Li, X.; Jin, Z.; Svensson, B.; Bai, Y.
    Acceptor subsite mutants of Limosilactobacillus fermentum NCC 2970 GtfB 4,3-alpha-glucanotransferase regulate the ratio of (alpha1->3)/(alpha1->6) linkages in biosynthesized alpha-glucans (2024), J. Agric. Food Chem., 72, 19994-20004.
    View publication on PubMed
Search for more literature for 2.4.1.390

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 (DE3) Limosilactobacillus fermentum

Protein Variants

Protein Variants Comment Organism
A1398Y the mutant shows decreased total activity and slightly increased hydrolytic activity, leading to low transglucosylase efficiency Limosilactobacillus fermentum
D991H the mutant has relatively higher total activity but is more hydrolytic than the wild-type enzyme. The mutant enzyme has increased temperature optimum of 45°C Limosilactobacillus fermentum
D991N besides native (alpha1->4) and (alpha1->3) linkages,the mutant shows 10% (alpha1->6) linkage increases compared to 1% for wild-type in products. The orientation of acceptor binding in the mutant is favorable for (alpha1->6) linkage synthesis Limosilactobacillus fermentum
E1405D the mutant displays lower total activity and lower hydrolytic activity and slightly decreased transglucosylase efficiency Limosilactobacillus fermentum
G1028R besides native (alpha1->4) and (alpha1->3) linkages,the mutant shows 8% (alpha1->6) linkage increases compared to 1% for wild-type in products. The orientation of acceptor binding in the mutant is favorable for (alpha1->6) linkage synthesis Limosilactobacillus fermentum
G1028R the mutant shows decreased total activity and slightly increased hydrolytic activity, leading to low transglucosylase efficiency. The mutant enzyme has increased temperature optimum of 45°C Limosilactobacillus fermentum
T1400E the mutant has relatively higher total activity but is more hydrolytic than the wild-type enzyme Limosilactobacillus fermentum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 amylose Km: 0.61 mg/ml, pH 5.0, 40°C, wild-type enzyme Limosilactobacillus fermentum
additional information
-
 amylose Km: 0.53 mg/ml, pH 5.0, 40°C, mutant enzyme A1398Y Limosilactobacillus fermentum
additional information
-
 amylose Km: 3.96 mg/ml, pH 5.0, 40°C, mutant enzyme G1028R Limosilactobacillus fermentum
additional information
-
 amylose Km: 0.39 mg/ml, pH 5.0, 40°C, mutant enzyme E1405D Limosilactobacillus fermentum
additional information
-
 amylose Km: 0.61 mg/ml, pH 5.0, 40°C, mutant enzyme D991H Limosilactobacillus fermentum
additional information
-
 amylose Km: 0.35 mg/ml, pH 5.0, 40°C, mutant enzyme T1400E Limosilactobacillus fermentum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
110000
-
 SDS-PAGE Limosilactobacillus fermentum

Organism

Organism UniProt Comment Textmining
Limosilactobacillus fermentum A0A1D7ZV76 cf. EC 2.4.1.5; cf. EC 2.4.1.5
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Limosilactobacillus fermentum NCC 2970 A0A1D7ZV76 cf. EC 2.4.1.5; cf. EC 2.4.1.5
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA affinity chromatography Limosilactobacillus fermentum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amylose besides native (alpha1->4) and (alpha1->3) linkages, the mutant enzymes G1028R and D991N show 8 and 10% (alpha1->6) linkage increases compared to 1% for wild-type in products Limosilactobacillus fermentum ?
-
 ?
amylose besides native (alpha1->4) and (alpha1->3) linkages, the mutant enzymes G1028R and D991N show 8 and 10% (alpha1->6) linkage increases compared to 1% for wild-type in products Limosilactobacillus fermentum NCC 2970 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 110000, SDS-PAGE Limosilactobacillus fermentum

Synonyms

Synonyms Comment Organism
4,3-alpha-GTase
-
 Limosilactobacillus fermentum
GtfB
-
 Limosilactobacillus fermentum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.1615
-
 amylose pH 5.0, 40°C, mutant enzyme E1405D Limosilactobacillus fermentum
0.269
-
 amylose pH 5.0, 40°C, mutant enzyme A1398Y Limosilactobacillus fermentum
0.4295
-
 amylose pH 5.0, 40°C, wild-type enzyme Limosilactobacillus fermentum
0.629
-
 amylose pH 5.0, 40°C, mutant enzyme G1028R Limosilactobacillus fermentum
0.64
-
 amylose pH 5.0, 40°C, mutant enzyme D991H Limosilactobacillus fermentum
0.8
-
 amylose pH 5.0, 40°C, mutant enzyme T1400E Limosilactobacillus fermentum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Limosilactobacillus fermentum