| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Limosilactobacillus fermentum |
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Al3+ | - |
Limosilactobacillus fermentum | |
| Co2+ | - |
Limosilactobacillus fermentum | |
| Cu2+ | - |
Limosilactobacillus fermentum | |
| Fe2+ | - |
Limosilactobacillus fermentum | |
| Pb2+ | - |
Limosilactobacillus fermentum |
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | 1 mM, stimulates activity by 2.22fold | Limosilactobacillus fermentum |
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 100000 | - |
SDS-PAGE | Limosilactobacillus fermentum |
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Limosilactobacillus fermentum | A0A1D7ZV76 | cf. EC 2.4.1.5; cf. EC 2.4.1.5 | - |
| Purification (Comment) | Organism |
|---|---|
- |
Limosilactobacillus fermentum |
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| high-amylose maize starch | - |
Limosilactobacillus fermentum | ? | - |
? | |
| maize starch | - |
Limosilactobacillus fermentum | ? | - |
? | |
| additional information | 4,3-alpha-GTase has a stronger affinity for linear starch chains than for branched glucan chains. The affinity of 4,3-alpha-GTase for alpha-1,4 linked glucan chains is positively correlated with the degree of polymerization of the substrate. Oligosaccharides are the receptor molecules of 4,3-alpha-GTase. Therefore the hydrolytic activity of the enzyme is preferentially presented when the enzyme was incubated with long-chain alpha-1,4 glucans. Longchain alpha-1,4 linked glucan chains are the preferred donor molecules for the enzymatic transglycosylation reaction, and the higher degree of polymerization value results in higher efficiency of the transglycosylation reaction | Limosilactobacillus fermentum | ? | - |
- |
|
| waxy maize starch | - |
Limosilactobacillus fermentum | ? | - |
? |
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 100000, SDS-PAGE | Limosilactobacillus fermentum |
| Synonyms | Comment | Organism |
|---|---|---|
| 4,3-alpha-GTase | - |
Limosilactobacillus fermentum |
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
- |
Limosilactobacillus fermentum |
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 50 | more than 90% activity between 30°C-50°C | Limosilactobacillus fermentum |
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
6 h, approximately 90% residual activity is retained | Limosilactobacillus fermentum |
| 45 | - |
6 h, more than 60% residual activity is retained | Limosilactobacillus fermentum |
| 50 | - |
6 h, more than 40% residual activity is retained | Limosilactobacillus fermentum |
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
- |
Limosilactobacillus fermentum |
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 6.5 | more than 90% activity between pH 5.0-6.5 | Limosilactobacillus fermentum |