Any feedback?
Literature summary extracted from
- Identification of Bacillus selenitireducens MLS10 maltose phosphorylase possessing synthetic ability for branched alpha-D-glucosyl trisaccharides (2012), Carbohydr. Res., 360, 25-30.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 2.4.1.8 | expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Salisediminibacterium selenitireducens |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 2.4.1.8 | 0.6 | - |
maltose | pH 6.5, 30°C, phosphorolysis | Salisediminibacterium selenitireducens |  |
| 2.4.1.8 | 4.6 | - |
sophorose | pH 6.5, 30°C, reverse phosphorolysis | Salisediminibacterium selenitireducens | |
| 2.4.1.8 | 24 | - |
kojibiose | pH 6.5, 30°C, reverse phosphorolysis | Salisediminibacterium selenitireducens | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.8 | 90000 | - |
x * 90660, sequence calculation, x * 90000, recombinant His6-tagged Bsel2056, SDS-PAGE | Salisediminibacterium selenitireducens |
| 2.4.1.8 | 90660 | - |
x * 90660, sequence calculation, x * 90000, recombinant His6-tagged Bsel2056, SDS-PAGE | Salisediminibacterium selenitireducens |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.4.1.8 | maltose + phosphate | Salisediminibacterium selenitireducens | - |
D-glucose + beta-D-glucose 1-phosphate | - |
r | |
| 2.4.1.8 | maltose + phosphate | Salisediminibacterium selenitireducens MLS10 | - |
D-glucose + beta-D-glucose 1-phosphate | - |
r | |
| 2.4.1.8 | additional information | Salisediminibacterium selenitireducens | the enzyme possesses synthetic ability for alpha-D-glucosyl disaccharides and trisaccharides through the reverse phosphorolysis with beta-D-glucose 1-phosphate as the donor | ? | - |
? | |
| 2.4.1.8 | additional information | Salisediminibacterium selenitireducens MLS10 | the enzyme possesses synthetic ability for alpha-D-glucosyl disaccharides and trisaccharides through the reverse phosphorolysis with beta-D-glucose 1-phosphate as the donor | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.4.1.8 | Salisediminibacterium selenitireducens | D6XUS4 | gene bsel2056 | - |
| 2.4.1.8 | Salisediminibacterium selenitireducens MLS10 | D6XUS4 | gene bsel2056 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 2.4.1.8 | recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography | Salisediminibacterium selenitireducens |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 2.4.1.8 | maltose + phosphate = D-glucose + beta-D-glucose 1-phosphate | sequential Bi Bi mechanism | Salisediminibacterium selenitireducens |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 2.4.1.8 | 4°C, purified recombinant His-tagged enzyme, 24 h, stable | Salisediminibacterium selenitireducens |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.4.1.8 | 2-acetamido-2-deoxy-D-glucose + beta-D-glucose 1-phosphate | - |
Salisediminibacterium selenitireducens | ? + phosphate | - |
? | |
| 2.4.1.8 | 2-acetamido-2-deoxy-D-glucose + beta-D-glucose 1-phosphate | - |
Salisediminibacterium selenitireducens MLS10 | ? + phosphate | - |
? | |
| 2.4.1.8 | 2-amino-2-deoxy-D-glucose + beta-D-glucose 1-phosphate | - |
Salisediminibacterium selenitireducens | ? + phosphate | - |
? | |
| 2.4.1.8 | 2-amino-2-deoxy-D-glucose + beta-D-glucose 1-phosphate | - |
Salisediminibacterium selenitireducens MLS10 | ? + phosphate | - |
? | |
| 2.4.1.8 | 2-deoxy-D-arabino-hexose + beta-D-glucose 1-phosphate | - |
Salisediminibacterium selenitireducens | ? + phosphate | - |
? | |
| 2.4.1.8 | D-mannose + beta-D-glucose 1-phosphate | - |
Salisediminibacterium selenitireducens | ? + phosphate | - |
? | |
| 2.4.1.8 | kojibiose + beta-D-glucose 1-phosphate | - |
Salisediminibacterium selenitireducens | 1,4-alpha-D-glucopyranosyl-[1,2-alpha-D-glucopyranosyl]-D-glucose + phosphate | - |
? | |
| 2.4.1.8 | maltose + phosphate | - |
Salisediminibacterium selenitireducens | D-glucose + beta-D-glucose 1-phosphate | - |
r | |
| 2.4.1.8 | maltose + phosphate | - |
Salisediminibacterium selenitireducens MLS10 | D-glucose + beta-D-glucose 1-phosphate | - |
r | |
| 2.4.1.8 | additional information | the enzyme possesses synthetic ability for alpha-D-glucosyl disaccharides and trisaccharides through the reverse phosphorolysis with beta-D-glucose 1-phosphate as the donor | Salisediminibacterium selenitireducens | ? | - |
? | |
| 2.4.1.8 | additional information | Bsel2056 phosphorolyzes only maltose with inversion of the anomeric configuration releasing beta-D-glucose 1-phosphate and D-glucose. Bsel2056 does not cleave the maltose in the absence of inorganic phosphate. In addition, maltooligosaccharides of degree of polymerization 3-6 are not substrate for Bsel2056. But Bsel2056 shows the flexibility for monosaccharide acceptors with alternative C2 substituent, e.g. 2-amino-2-deoxy-D-glucose, 2-deoxy-D-arabino-hexose, 2-acetamido-2-deoxy-D-glucose, and D-mannose, in the reverse reaction resulting in production of 1,4-alpha-D-glucosyl disaccharides with strict regioselectivity. Bsel2056 possesses a binding space to accommodate the bulky C2 substituent of D-glucose. Substrate specificity and product analysis using NMR, overview | Salisediminibacterium selenitireducens | ? | - |
? | |
| 2.4.1.8 | additional information | the enzyme possesses synthetic ability for alpha-D-glucosyl disaccharides and trisaccharides through the reverse phosphorolysis with beta-D-glucose 1-phosphate as the donor | Salisediminibacterium selenitireducens MLS10 | ? | - |
? | |
| 2.4.1.8 | additional information | Bsel2056 phosphorolyzes only maltose with inversion of the anomeric configuration releasing beta-D-glucose 1-phosphate and D-glucose. Bsel2056 does not cleave the maltose in the absence of inorganic phosphate. In addition, maltooligosaccharides of degree of polymerization 3-6 are not substrate for Bsel2056. But Bsel2056 shows the flexibility for monosaccharide acceptors with alternative C2 substituent, e.g. 2-amino-2-deoxy-D-glucose, 2-deoxy-D-arabino-hexose, 2-acetamido-2-deoxy-D-glucose, and D-mannose, in the reverse reaction resulting in production of 1,4-alpha-D-glucosyl disaccharides with strict regioselectivity. Bsel2056 possesses a binding space to accommodate the bulky C2 substituent of D-glucose. Substrate specificity and product analysis using NMR, overview | Salisediminibacterium selenitireducens MLS10 | ? | - |
? | |
| 2.4.1.8 | sophorose + beta-D-glucose 1-phosphate | - |
Salisediminibacterium selenitireducens | 1,4-alpha-D-glucopyranosyl-[1,2-beta-D-glucopyranosyl]-D-glucose + phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 2.4.1.8 | ? | x * 90660, sequence calculation, x * 90000, recombinant His6-tagged Bsel2056, SDS-PAGE | Salisediminibacterium selenitireducens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 2.4.1.8 | Bsel2056 | - |
Salisediminibacterium selenitireducens |
| 2.4.1.8 | inverting maltose phosphorylase | - |
Salisediminibacterium selenitireducens |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.8 | 55 | - |
- |
Salisediminibacterium selenitireducens |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.8 | 50 | - |
purified recombinant His-tagged enzyme, 15 min, stable | Salisediminibacterium selenitireducens |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 2.4.1.8 | 6.6 | - |
sophorose | pH 6.5, 30°C, reverse phosphorolysis | Salisediminibacterium selenitireducens | |
| 2.4.1.8 | 12.3 | - |
maltose | pH 6.5, 30°C | Salisediminibacterium selenitireducens | |
| 2.4.1.8 | 40 | - |
kojibiose | pH 6.5, 30°C, reverse phosphorolysis | Salisediminibacterium selenitireducens | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.8 | 5.5 | - |
reverse reaction | Salisediminibacterium selenitireducens |
| 2.4.1.8 | 6.5 | - |
phosphorolysis | Salisediminibacterium selenitireducens |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.8 | 5.5 | 10.5 | purified recombinant His-tagged enzyme, 4°C, 24 h, stable | Salisediminibacterium selenitireducens |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 2.4.1.8 | evolution | the inverting maltose phosphorylase belongs to the glycoside hydrolase family 65, GH65 | Salisediminibacterium selenitireducens |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 2.4.1.8 | 1.4 | - |
sophorose | pH 6.5, 30°C, reverse phosphorolysis | Salisediminibacterium selenitireducens | |
| 2.4.1.8 | 1.7 | - |
kojibiose | pH 6.5, 30°C, reverse phosphorolysis | Salisediminibacterium selenitireducens | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
