| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 2.4.1.30 | recombinant enzyme expression in Escherichia coli | Euglena gracilis |
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 2.4.1.30 | enzyme crystal structure in the absence of substrate (PDB ID 6HQ6) and in complex with laminarihexaose (PDB ID 6HQ8) | uncultured bacterium |
| 2.4.1.31 | enzyme crystal structure analysis, PDB ID 6GH2 | Paenibacillus sp. YM1 |
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.4.1.30 | [(1->3)-beta-D-glucosyl]n + phosphate | Euglena gracilis | - |
[(1->3)-beta-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | - |
r | |
| 2.4.1.30 | [(1->3)-beta-D-glucosyl]n + phosphate | Ochromonas sp. | - |
[(1->3)-beta-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | - |
r | |
| 2.4.1.30 | [(1->3)-beta-D-glucosyl]n + phosphate | Paenibacillus polymyxa | - |
[(1->3)-beta-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | - |
? | |
| 2.4.1.30 | [(1->3)-beta-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | Euglena gracilis | - |
[(1->3)-beta-D-glucosyl]n + phosphate | - |
r | |
| 2.4.1.30 | [(1->3)-beta-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | Ochromonas sp. | - |
[(1->3)-beta-D-glucosyl]n + phosphate | - |
r | |
| 2.4.1.31 | 3-beta-D-glucosyl-D-glucose + phosphate | Paenibacillus sp. YM1 | - |
D-glucose + alpha-D-glucose 1-phosphate | - |
r |
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.4.1.30 | Euglena gracilis | A0A8D4WWT7 | - |
- |
| 2.4.1.30 | Ochromonas sp. | - |
- |
- |
| 2.4.1.30 | Paenibacillus polymyxa | - |
- |
- |
| 2.4.1.30 | uncultured bacterium | - |
- |
- |
| 2.4.1.31 | Paenibacillus sp. YM1 | - |
- |
- |
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.4.1.30 | additional information | crystalline oligosaccharides (DP 30) are produced by a partially purified beta-1,3-D-glucan phosphorylase extract from the microalga Euglena gracilis | Euglena gracilis | ? | - |
- |
|
| 2.4.1.30 | additional information | recombinant enzyme PapP shows neither synthetic activity in the presence of D-Glc and alpha-D-Glc-1P, nor phosphorolysis activity towards Glc-Glc disaccharides with different linkages. Nonetheless, phosphorolysis assays with DP3 to DP6 reveal its preference for longer substrates. These results strongly suggest that PapP can only operate on beta-1,3 linear oligosaccharide acceptors with DP greater than 2, evidencing its different specificity from GH149 glucan phosphorylases | Paenibacillus polymyxa | ? | - |
- |
|
| 2.4.1.30 | [(1->3)-beta-D-glucosyl]n + phosphate | - |
Euglena gracilis | [(1->3)-beta-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | - |
r | |
| 2.4.1.30 | [(1->3)-beta-D-glucosyl]n + phosphate | - |
Ochromonas sp. | [(1->3)-beta-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | - |
r | |
| 2.4.1.30 | [(1->3)-beta-D-glucosyl]n + phosphate | - |
Paenibacillus polymyxa | [(1->3)-beta-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | - |
? | |
| 2.4.1.30 | [(1->3)-beta-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | - |
Euglena gracilis | [(1->3)-beta-D-glucosyl]n + phosphate | - |
r | |
| 2.4.1.30 | [(1->3)-beta-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | - |
Ochromonas sp. | [(1->3)-beta-D-glucosyl]n + phosphate | - |
r | |
| 2.4.1.31 | 3-beta-D-glucosyl-D-glucose + phosphate | - |
Paenibacillus sp. YM1 | D-glucose + alpha-D-glucose 1-phosphate | - |
r | |
| 2.4.1.31 | D-glucose + alpha-D-glucose 1-phosphate | - |
Paenibacillus sp. YM1 | 3-beta-D-glucosyl-D-glucose + phosphate | - |
r | |
| 2.4.1.31 | D-glucose + alpha-D-mannose 1-phosphate | very low activity | Paenibacillus sp. YM1 | beta-D-mannopyranosyl-1,3-D-glucose + phosphate | - |
? | |
| 2.4.1.31 | additional information | the enzyme shows a broader substrate specificty, with specificity for disaccharides. It also catalyses the synthesis of beta-D-mannopyranosyl-1,3-D-glucopyranose from D-Glc and alpha-D-Man-1P, albeit with highly reduced catalytic efficiency. The loss of an important hydrogen bond between the axial hydroxy group at C2 and a key residue in the active site, thus possibly contributing to the low reaction turnover | Paenibacillus sp. YM1 | ? | - |
- |
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 2.4.1.30 | algal beta-1,3-glucan phosphorylase | - |
Euglena gracilis |
| 2.4.1.30 | algal beta-1,3-glucan phosphorylase | - |
Ochromonas sp. |
| 2.4.1.30 | beta-1,3-D-glucan phosphorylase | - |
Euglena gracilis |
| 2.4.1.30 | beta-1,3-D-glucan phosphorylase | - |
Ochromonas sp. |
| 2.4.1.30 | beta-1,3-D-glucan phosphorylase | - |
Paenibacillus polymyxa |
| 2.4.1.30 | beta-1,3-D-glucan phosphorylase | - |
uncultured bacterium |
| 2.4.1.30 | EgP1 | - |
Euglena gracilis |
| 2.4.1.30 | OcP1 | - |
Ochromonas sp. |
| 2.4.1.30 | PapP | - |
Paenibacillus polymyxa |
| 2.4.1.30 | Pro_7066 | - |
uncultured bacterium |
| 2.4.1.31 | PsLBP | - |
Paenibacillus sp. YM1 |
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 2.4.1.30 | evolution | the enzyme belongs to glycoside family 149, GH149 | Euglena gracilis |
| 2.4.1.30 | evolution | the enzyme belongs to glycoside family 161, GH161 | Ochromonas sp. |
| 2.4.1.30 | evolution | the enzyme belongs to glycoside family 161, GH161 | Paenibacillus polymyxa |
| 2.4.1.30 | evolution | the enzyme belongs to glycoside family 149, GH149. Although the overall domain organisation is similar to GH94, Pro_7066 enzyme contains two additional distinct domains flanking its catalytic region and a surface oligosaccharide binding site where laminarihexaose is accommodated, which is distant from the catalytic site and may be involved in the recognition of longer substrates | uncultured bacterium |
| 2.4.1.31 | evolution | enzyme LBP belongs to the glycoside family 94, GH94 | Paenibacillus sp. YM1 |