Cloned (Comment) | Organism |
---|---|
expression in Bacillus subtilis | Rhodothermus marinus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Km-value for amylose is 0.7 mg/ml, 30°C, pH 7.0 | Rhodothermus marinus | |
additional information | - |
additional information | enzyme reaction kinetics with different branched or unbranched alpha-glucans of controlled structure | Rhodothermus marinus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Rhodothermus marinus | the enzyme catalyzes starch branching by the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position, but the enzyme also shows an additional alpha-4-glucanotransferase activity not described so far for a member of the GH13 family. The enzyme is able to transfer alpha(1->4)-linked-glucan in C4 position (instead of C6 position for the branching activity) of a glucan to create new alpha(1->4) linkages yielding to the elongation of linear chains subsequently used for further branching, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodothermus marinus | Q93HU3 | - |
- |
Rhodothermus marinus | Q93HU3 | gene glgB | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
108 | - |
30°C, pH 7.0 | Rhodothermus marinus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
amylose | potato type III amylose | Rhodothermus marinus | amylose containing alpha-1,6-glucosidic linkages | - |
? | |
additional information | a minimal chain length of ten glucosyl units is required for the donor substrate to be recognized by Rhodothermus marinus branching enzyme that essentially produces branches with a degree of polymerization of 3-8. The enzyme preferentially creates new branches by intermolecular mechanism. Branched glucans define better substrates for the enzyme leading to the formation of hyper-branched particles of 30-70 nm in diameter, dextrins. The enzyme catalyzes an additional alpha-4-glucanotransferase activity | Rhodothermus marinus | ? | - |
? | |
additional information | the enzyme catalyzes starch branching by the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position, but the enzyme also shows an additional alpha-4-glucanotransferase activity not described so far for a member of the GH13 family. The enzyme is able to transfer alpha(1->4)-linked-glucan in C4 position (instead of C6 position for the branching activity) of a glucan to create new alpha(1->4) linkages yielding to the elongation of linear chains subsequently used for further branching, overview | Rhodothermus marinus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
RoBE | - |
Rhodothermus marinus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Rhodothermus marinus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Rhodothermus marinus |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the glycoside hydrolase family GH13 | Rhodothermus marinus |
metabolism | glycogen and starch branching enzymes catalyze the formation of alpha(1->6) linkages in storage polysaccharides by rearrangement of preexisting alpha-glucans. This reaction occurs through the cleavage of alpha(1->4) linkage and transfer in alpha(1->6) of the fragment in non-reducing position. These enzymes define major elements that control the structure of both glycogen and starch | Rhodothermus marinus |