EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.4.1.2 | Co2+ | - |
Gluconobacter oxydans | |
2.4.1.2 | Cu2+ | strong inhibition | Gluconobacter oxydans | |
2.4.1.2 | Fe2+ | strong inhibition | Gluconobacter oxydans | |
2.4.1.2 | Ni2+ | - |
Gluconobacter oxydans | |
2.4.1.2 | Zn2+ | strong inhibition | Gluconobacter oxydans |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.4.1.2 | Ba2+ | slight activation | Gluconobacter oxydans | |
2.4.1.2 | Ca2+ | slight activation | Gluconobacter oxydans | |
2.4.1.2 | Mg2+ | slight activation | Gluconobacter oxydans | |
2.4.1.2 | Mn2+ | slight activation | Gluconobacter oxydans | |
2.4.1.2 | additional information | no effect by Fe3+ | Gluconobacter oxydans |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.4.1.2 | 62000 | - |
gel filtration | Gluconobacter oxydans |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.2 | additional information | Gluconobacter oxydans | DDase from strain DSM-2003 converts maltodextrins to dextran. The enzyme catalyzes the transfer of an alpha(1,4)-linked glucosyl unit from a donor to an acceptor molecule, forming an alpha(1,6) linkage: consecutive glucosyl transfers result in the formation of high molecular weight dextran from maltodextrin. DDase can use widely occurring in nature maltodextrin to produce dextran by transglucosylation | ? | - |
? | |
2.4.1.2 | additional information | Gluconobacter oxydans DSM 2003 | DDase from strain DSM-2003 converts maltodextrins to dextran. The enzyme catalyzes the transfer of an alpha(1,4)-linked glucosyl unit from a donor to an acceptor molecule, forming an alpha(1,6) linkage: consecutive glucosyl transfers result in the formation of high molecular weight dextran from maltodextrin. DDase can use widely occurring in nature maltodextrin to produce dextran by transglucosylation | ? | - |
? | |
2.4.1.2 | [(1->4)-alpha-D-glucosyl]n + [(1->6)-alpha-D-glucosyl]m | Gluconobacter oxydans | - |
[(1->4)-alpha-D-glucosyl]n-1 + [(1->6)-alpha-D-glucosyl]m+1 | dextran synthesized by DDase from strain DSM-2003 is composed of alpha(1,6)-linked chains containing alpha(1,4) branching points | ? | |
2.4.1.2 | [(1->4)-alpha-D-glucosyl]n + [(1->6)-alpha-D-glucosyl]m | Gluconobacter oxydans DSM 2003 | - |
[(1->4)-alpha-D-glucosyl]n-1 + [(1->6)-alpha-D-glucosyl]m+1 | dextran synthesized by DDase from strain DSM-2003 is composed of alpha(1,6)-linked chains containing alpha(1,4) branching points | ? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.1.2 | Gluconobacter oxydans | - |
- |
- |
2.4.1.2 | Gluconobacter oxydans DSM 2003 | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.4.1.2 | native DDase 187.5fold to homogeneity by anion exchange chromatography and gel filtration | Gluconobacter oxydans |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.4.1.2 | 112.5 | - |
purified enzyme, pH 6.5, 30°C | Gluconobacter oxydans |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.2 | 4-nitrophenyl-alpha-D-glucopyranoside + H2O | artificial substrate | Gluconobacter oxydans | 4-nitrophenol + alpha-D-glucopyranose | - |
? | |
2.4.1.2 | 4-nitrophenyl-alpha-D-glucopyranoside + H2O | artificial substrate | Gluconobacter oxydans DSM 2003 | 4-nitrophenol + alpha-D-glucopyranose | - |
? | |
2.4.1.2 | additional information | DDase from strain DSM-2003 converts maltodextrins to dextran. The enzyme catalyzes the transfer of an alpha(1,4)-linked glucosyl unit from a donor to an acceptor molecule, forming an alpha(1,6) linkage: consecutive glucosyl transfers result in the formation of high molecular weight dextran from maltodextrin. DDase can use widely occurring in nature maltodextrin to produce dextran by transglucosylation | Gluconobacter oxydans | ? | - |
? | |
2.4.1.2 | additional information | DDase from strain DSM-2003 converts maltodextrins to dextran. The enzyme catalyzes the transfer of an alpha(1,4)-linked glucosyl unit from a donor to an acceptor molecule, forming an alpha(1,6) linkage: consecutive glucosyl transfers result in the formation of high molecular weight dextran from maltodextrin. DDase can use widely occurring in nature maltodextrin to produce dextran by transglucosylation | Gluconobacter oxydans DSM 2003 | ? | - |
? | |
2.4.1.2 | [(1->4)-alpha-D-glucosyl]n + [(1->6)-alpha-D-glucosyl]m | - |
Gluconobacter oxydans | [(1->4)-alpha-D-glucosyl]n-1 + [(1->6)-alpha-D-glucosyl]m+1 | - |
? | |
2.4.1.2 | [(1->4)-alpha-D-glucosyl]n + [(1->6)-alpha-D-glucosyl]m | - |
Gluconobacter oxydans | [(1->4)-alpha-D-glucosyl]n-1 + [(1->6)-alpha-D-glucosyl]m+1 | dextran synthesized by DDase from strain DSM-2003 is composed of alpha(1,6)-linked chains containing alpha(1,4) branching points | ? | |
2.4.1.2 | [(1->4)-alpha-D-glucosyl]n + [(1->6)-alpha-D-glucosyl]m | - |
Gluconobacter oxydans DSM 2003 | [(1->4)-alpha-D-glucosyl]n-1 + [(1->6)-alpha-D-glucosyl]m+1 | - |
? | |
2.4.1.2 | [(1->4)-alpha-D-glucosyl]n + [(1->6)-alpha-D-glucosyl]m | - |
Gluconobacter oxydans DSM 2003 | [(1->4)-alpha-D-glucosyl]n-1 + [(1->6)-alpha-D-glucosyl]m+1 | dextran synthesized by DDase from strain DSM-2003 is composed of alpha(1,6)-linked chains containing alpha(1,4) branching points | ? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.4.1.2 | monomer | 1 * 62000, SDS-PAGE | Gluconobacter oxydans |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.1.2 | DDase | - |
Gluconobacter oxydans |
2.4.1.2 | dextran dextrinase | - |
Gluconobacter oxydans |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.4.1.2 | 30 | - |
- |
Gluconobacter oxydans |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.4.1.2 | 11 | 35 | sharp decrease at temperatures higher than 35 °C | Gluconobacter oxydans |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.4.1.2 | 30 | - |
stable below 30°C for 3 h | Gluconobacter oxydans |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.4.1.2 | 6.3 | - |
- |
Gluconobacter oxydans |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
2.4.1.2 | 5 | 9 | stable within this range for 3 h | Gluconobacter oxydans |