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Literature summary for 2.4.1.25 extracted from
- Production of large-ring cyclodextrins by amylomaltases (2022), Molecules, 27, 1446.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| chloroplast | - |
Arabidopsis thaliana | 9507 | - |
| chloroplast | - |
Solanum tuberosum | 9507 | - |
| chloroplast | - |
Oryza sativa Japonica Group | 9507 | - |
| cytosol | - |
Arabidopsis thaliana | 5829 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acidothermus cellulolyticus | A0LVB3 | - |
- |
| Acidothermus cellulolyticus 11B | A0LVB3 | - |
- |
| Acidothermus cellulolyticus ATCC 43068 | A0LVB3 | - |
- |
| Acidothermus cellulolyticus DSM 8971 | A0LVB3 | - |
- |
| Aquifex aeolicus | O66937 | - |
- |
| Arabidopsis thaliana | Q9LV91 | - |
- |
| Arabidopsis thaliana | Q8RXD9 | - |
- |
| Borreliella burgdorferi | A6YM39 | - |
- |
| Corynebacterium glutamicum | Q8NNA7 | - |
- |
| Corynebacterium glutamicum 534 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum ATCC 13032 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum BCRC 11384 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum CCUG 27702 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum DSM 20300 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum JCM 1318 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum LMG 3730 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum NBRC 12168 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum NCIMB 10025 | Q8NNA7 | - |
- |
| Corynebacterium glutamicum NRRL B-2784 | Q8NNA7 | - |
- |
| Escherichia coli | P15977 | - |
- |
| Escherichia coli K12 | P15977 | - |
- |
| Manihot esculenta | A0A2C9VJ68 | cv. AM560-2, Jatropha manihot | - |
| Manihot esculenta Crantz | A0A2C9VJ68 | cv. AM560-2, Jatropha manihot | - |
| Oryza sativa Japonica Group | Q8LI30 | - |
- |
| Oryza sativa Japonica Group | Q69Q02 | - |
- |
| Pyrobaculum aerophilum | Q8ZXM0 | - |
- |
| Pyrobaculum aerophilum ATCC 51768 | Q8ZXM0 | - |
- |
| Pyrobaculum aerophilum CIP 104966 | Q8ZXM0 | - |
- |
| Pyrobaculum aerophilum DSM 7523 | Q8ZXM0 | - |
- |
| Pyrobaculum aerophilum IM2 | Q8ZXM0 | - |
- |
| Pyrobaculum aerophilum JCM 9630 | Q8ZXM0 | - |
- |
| Pyrobaculum aerophilum NBRC 100827 | Q8ZXM0 | - |
- |
| Pyrobaculum calidifontis | A3MU77 | - |
- |
| Pyrobaculum calidifontis DSM 21063 | A3MU77 | - |
- |
| Pyrobaculum calidifontis JCM 11548 | A3MU77 | - |
- |
| Pyrobaculum calidifontis VA1 | A3MU77 | - |
- |
| Saccharophagus degradans | Q21M31 | - |
- |
| Saccharophagus degradans ATCC 43961 | Q21M31 | - |
- |
| Saccharophagus degradans DSM 17024 | Q21M31 | - |
- |
| Solanum tuberosum | Q06801 | - |
- |
| Streptococcus agalactiae | A0A0E1EIJ0 | - |
- |
| Streptococcus agalactiae YZ1605 | A0A0E1EIJ0 | - |
- |
| Synechocystis sp. PCC 6803 | P72785 | - |
- |
| Thermus aquaticus | Q6JHX9 | - |
- |
| Thermus aquaticus ATCC 33923 | Q6JHX9 | - |
- |
| Thermus brockianus | Q2VJA0 | - |
- |
| Thermus filiformis | A0A0K0Q020 | - |
- |
| Thermus scotoductus | A0A430UEB1 | - |
- |
| Thermus thermophilus | O87172 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan | cyclization mechanism of amylomaltase, and large-ring cyclodextrin production by amylomaltase overview | Thermus aquaticus | |
| Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan | cyclization mechanism of amylomaltase AtDPE1, overview | Arabidopsis thaliana |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 2.9 | - |
pH 5.5-6.0, 75°C, disproportionation activity | Thermus aquaticus |
| 5.84 | - |
pH 7.0, 45°C, disproportionation activity | Synechocystis sp. PCC 6803 |
| 21.8 | 44.3 | pH 6.0, 30-45°C, disproportionation activity | Corynebacterium glutamicum |
| 44.2 | - |
pH 6.6, 90°C, disproportionation activity | Aquifex aeolicus |
| 47.5 | - |
pH 6.7, 45°C, disproportionation activity | Solanum tuberosum |
| 54 | - |
pH 6.0, 40°C, disproportionation activity | Streptococcus agalactiae |
| 159 | - |
pH 6.5, 60°C, disproportionation activity | Thermus filiformis |
| 400 | - |
pH 5.5-6.3, 72-75°C, disproportionation activity | Thermus thermophilus |
| 450 | - |
pH 6.7, 95°C, disproportionation activity | Pyrobaculum aerophilum |
| 690 | - |
pH 6.9, 80°C, disproportionation activity | Pyrobaculum calidifontis |
| 9400 | - |
pH 6.9, 28°C, disproportionation activity | Escherichia coli |
| 17734 | - |
pH 6.0, 70°C, disproportionation activity | Thermus brockianus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP16-DP50 from amylose | Aquifex aeolicus | ? | - |
- |
 |
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch | Corynebacterium glutamicum | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22-DP50 from pea starch | Streptococcus agalactiae | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22 to over DP60 from synthetic amylose | Thermus aquaticus | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22-DP60 from pea starch | Thermus filiformis | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP24-DP284 from sucrose and of DP12-DP36 from corn starch | Synechocystis sp. PCC 6803 | ? | - |
- |
|
| additional information | the enzyme AtDPE1 produces oligosaccharides with degree of polymerization (DP) of DP16-DP50 from potato amylose | Arabidopsis thaliana | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22 to over DP60 from potato amylose | Manihot esculenta | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP17 to over DP100 from synthetic amylose | Solanum tuberosum | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch | Corynebacterium glutamicum ATCC 13032 | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch | Corynebacterium glutamicum DSM 20300 | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch | Corynebacterium glutamicum JCM 1318 | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch | Corynebacterium glutamicum LMG 3730 | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch | Corynebacterium glutamicum NCIMB 10025 | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch | Corynebacterium glutamicum BCRC 11384 | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22 to over DP60 from potato amylose | Manihot esculenta Crantz | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch | Corynebacterium glutamicum CCUG 27702 | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch | Corynebacterium glutamicum NBRC 12168 | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch | Corynebacterium glutamicum NRRL B-2784 | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP19-DP50 from pea starch and of DP22-DP54 from tapioka starch | Corynebacterium glutamicum 534 | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22-DP50 from pea starch | Streptococcus agalactiae YZ1605 | ? | - |
- |
|
| additional information | the enzyme produces oligosaccharides with degree of polymerization (DP) of DP22 to over DP60 from synthetic amylose | Thermus aquaticus ATCC 33923 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | the D-enzyme from Arabidopsis thaliana (AtDPE1) is present in a dimeric form | Arabidopsis thaliana |
| additional information | the three-dimensional structure of TaAM can be divided into two main domains, namely domain A and B. The subdomains B1, B2, and B3 are generated from insertion loops of (alpha,beta)8 barrel structure of domain A. Co-crystallization of TaAM with 34mer CA presents it as an asymmetric dimer. Domain structure, overview | Thermus aquaticus |
| additional information | the monomeric AtDPE1 possesses a long N-terminal part as a dimerization arm for engagement | Arabidopsis thaliana |
| additional information | isoform AtDPE2 specially contains two putative carbohydrate-binding modules (CBM20) at the N-terminus. In addition, the catalytic domain sequence is also divided into two parts as there is an insertion of 173 amino acid residues between the area of nucleophilic and acid/base-catalytic residues | Arabidopsis thaliana |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic | - |
Arabidopsis thaliana |
| 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic | - |
Oryza sativa Japonica Group |
| 4-alpha-glucanotransferase DPE2 | - |
Arabidopsis thaliana |
| 4-alpha-glucanotransferase DPE2 | - |
Oryza sativa Japonica Group |
| 4-alpha-glucanotransferase, chloroplastic/amyloplastic | - |
Solanum tuberosum |
| 4alphaGTase | - |
Pyrobaculum aerophilum |
| 4alphaGTase | - |
Pyrobaculum calidifontis |
| 4alphaGTase | - |
Aquifex aeolicus |
| 4alphaGTase | - |
Corynebacterium glutamicum |
| 4alphaGTase | - |
Streptococcus agalactiae |
| 4alphaGTase | - |
Thermus aquaticus |
| 4alphaGTase | - |
Thermus filiformis |
| 4alphaGTase | - |
Thermus brockianus |
| 4alphaGTase | - |
Thermus thermophilus |
| 4alphaGTase | - |
Acidothermus cellulolyticus |
| 4alphaGTase | - |
Borreliella burgdorferi |
| 4alphaGTase | - |
Escherichia coli |
| 4alphaGTase | - |
Saccharophagus degradans |
| 4alphaGTase | - |
Synechocystis sp. PCC 6803 |
| 4alphaGTase | - |
Thermus scotoductus |
| 4alphaGTase | - |
Arabidopsis thaliana |
| 4alphaGTase | - |
Manihot esculenta |
| 4alphaGTase | - |
Solanum tuberosum |
| 4alphaGTase | - |
Oryza sativa Japonica Group |
| amylomaltase | - |
Pyrobaculum aerophilum |
| amylomaltase | - |
Pyrobaculum calidifontis |
| amylomaltase | - |
Aquifex aeolicus |
| amylomaltase | - |
Corynebacterium glutamicum |
| amylomaltase | - |
Streptococcus agalactiae |
| amylomaltase | - |
Thermus aquaticus |
| amylomaltase | - |
Thermus filiformis |
| amylomaltase | - |
Thermus brockianus |
| amylomaltase | - |
Thermus thermophilus |
| amylomaltase | - |
Acidothermus cellulolyticus |
| amylomaltase | - |
Borreliella burgdorferi |
| amylomaltase | - |
Escherichia coli |
| amylomaltase | - |
Saccharophagus degradans |
| amylomaltase | - |
Synechocystis sp. PCC 6803 |
| amylomaltase | - |
Thermus scotoductus |
| amylomaltase | - |
Arabidopsis thaliana |
| amylomaltase | - |
Manihot esculenta |
| amylomaltase | - |
Solanum tuberosum |
| amylomaltase | - |
Oryza sativa Japonica Group |
| AtDPE1 | - |
Arabidopsis thaliana |
| AtDPE2 | - |
Arabidopsis thaliana |
| CgAM | - |
Corynebacterium glutamicum |
| DPE1 | - |
Arabidopsis thaliana |
| DPE1 | - |
Oryza sativa Japonica Group |
| DPE2 | - |
Arabidopsis thaliana |
| DPE2 | - |
Oryza sativa Japonica Group |
| DPEP | - |
Solanum tuberosum |
| MalQ | - |
Pyrobaculum aerophilum |
| MalQ | - |
Pyrobaculum calidifontis |
| MalQ | - |
Aquifex aeolicus |
| MalQ | - |
Corynebacterium glutamicum |
| MalQ | - |
Streptococcus agalactiae |
| MalQ | - |
Thermus aquaticus |
| MalQ | - |
Thermus filiformis |
| MalQ | - |
Thermus brockianus |
| MalQ | - |
Thermus thermophilus |
| MalQ | - |
Acidothermus cellulolyticus |
| MalQ | - |
Borreliella burgdorferi |
| MalQ | - |
Escherichia coli |
| MalQ | - |
Saccharophagus degradans |
| MalQ | - |
Synechocystis sp. PCC 6803 |
| MalQ | - |
Thermus scotoductus |
| MalQ | - |
Arabidopsis thaliana |
| MalQ | - |
Manihot esculenta |
| MalQ | - |
Solanum tuberosum |
| MalQ | - |
Oryza sativa Japonica Group |
| MeDPE1 | - |
Manihot esculenta |
| OsDPE1 | - |
Oryza sativa Japonica Group |
| OsDPE2 | - |
Oryza sativa Japonica Group |
| prokaryotic 4-alpha-glucanotransferase | - |
Pyrobaculum aerophilum |
| prokaryotic 4-alpha-glucanotransferase | - |
Pyrobaculum calidifontis |
| prokaryotic 4-alpha-glucanotransferase | - |
Aquifex aeolicus |
| prokaryotic 4-alpha-glucanotransferase | - |
Corynebacterium glutamicum |
| prokaryotic 4-alpha-glucanotransferase | - |
Streptococcus agalactiae |
| prokaryotic 4-alpha-glucanotransferase | - |
Thermus aquaticus |
| prokaryotic 4-alpha-glucanotransferase | - |
Thermus filiformis |
| prokaryotic 4-alpha-glucanotransferase | - |
Thermus brockianus |
| prokaryotic 4-alpha-glucanotransferase | - |
Thermus thermophilus |
| prokaryotic 4-alpha-glucanotransferase | - |
Acidothermus cellulolyticus |
| prokaryotic 4-alpha-glucanotransferase | - |
Borreliella burgdorferi |
| prokaryotic 4-alpha-glucanotransferase | - |
Escherichia coli |
| prokaryotic 4-alpha-glucanotransferase | - |
Saccharophagus degradans |
| prokaryotic 4-alpha-glucanotransferase | - |
Synechocystis sp. PCC 6803 |
| prokaryotic 4-alpha-glucanotransferase | - |
Thermus scotoductus |
| Sde_0986 | - |
Saccharophagus degradans |
| TaAM | - |
Thermus aquaticus |
| TBGT | - |
Thermus brockianus |
| TfAM | - |
Thermus filiformis |
| TtAM | - |
Thermus thermophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 28 | - |
disproportionation activity | Escherichia coli |
| 30 | 45 | disproportionation and cyclization activity | Corynebacterium glutamicum |
| 30 | 39 | disproportionation activity | Oryza sativa Japonica Group |
| 30 | - |
cyclization activity | Streptococcus agalactiae |
| 35 | - |
disproportionation activity | Saccharophagus degradans |
| 37 | - |
disproportionation activity | Arabidopsis thaliana |
| 37 | - |
disproportionation activity | Borreliella burgdorferi |
| 37 | - |
disproportionation activity | Manihot esculenta |
| 40 | - |
disproportionation activity | Streptococcus agalactiae |
| 42 | - |
disproportionation activity | Arabidopsis thaliana |
| 45 | - |
disproportionation activity | Solanum tuberosum |
| 45 | - |
disproportionation activity | Synechocystis sp. PCC 6803 |
| 60 | - |
disproportionation activity | Thermus filiformis |
| 70 | - |
disproportionation activity | Thermus brockianus |
| 70 | - |
cyclization activity | Thermus filiformis |
| 72 | 75 | disproportionation activity | Thermus thermophilus |
| 75 | - |
disproportionation activity | Acidothermus cellulolyticus |
| 75 | - |
disproportionation activity | Thermus aquaticus |
| 75 | - |
disproportionation activity | Thermus scotoductus |
| 80 | - |
disproportionation activity | Pyrobaculum calidifontis |
| 90 | - |
disproportionation activity | Aquifex aeolicus |
| 95 | - |
disproportionation activity | Pyrobaculum aerophilum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
cyclization activity | Thermus filiformis |
| 5.5 | 6 | disproportionation activity | Thermus aquaticus |
| 5.5 | 6.3 | disproportionation activity | Thermus thermophilus |
| 5.5 | - |
disproportionation activity | Borreliella burgdorferi |
| 6 | - |
disproportionation and cyclization activity | Corynebacterium glutamicum |
| 6 | - |
disproportionation and cyclization activities | Streptococcus agalactiae |
| 6 | - |
disproportionation activity | Thermus brockianus |
| 6 | 8 | disproportionation activity | Arabidopsis thaliana |
| 6 | 8 | disproportionation activity | Manihot esculenta |
| 6 | 7 | disproportionation activity | Oryza sativa Japonica Group |
| 6.5 | - |
disproportionation activity | Thermus filiformis |
| 6.6 | - |
disproportionation activity | Aquifex aeolicus |
| 6.7 | - |
disproportionation activity | Pyrobaculum aerophilum |
| 6.7 | - |
disproportionation activity | Solanum tuberosum |
| 6.9 | - |
disproportionation activity | Pyrobaculum calidifontis |
| 6.9 | - |
disproportionation activity | Escherichia coli |
| 7 | - |
disproportionation activity | Synechocystis sp. PCC 6803 |
| 7 | - |
disproportionation activity | Arabidopsis thaliana |
| 7.5 | - |
disproportionation activity | Acidothermus cellulolyticus |
| 7.5 | - |
disproportionation activity | Thermus scotoductus |
| 8.5 | - |
disproportionation activity | Saccharophagus degradans |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Pyrobaculum aerophilum |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Pyrobaculum calidifontis |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Aquifex aeolicus |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Corynebacterium glutamicum |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Streptococcus agalactiae |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Thermus aquaticus |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Thermus filiformis |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Thermus brockianus |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Thermus thermophilus |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Acidothermus cellulolyticus |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Borreliella burgdorferi |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Escherichia coli |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Saccharophagus degradans |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Synechocystis sp. PCC 6803 |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Thermus scotoductus |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Arabidopsis thaliana |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Manihot esculenta |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Solanum tuberosum |
| evolution | members of 4alphaGTases include amylomaltases from microorganisms and disproportionation enzymes (D-enzymes) from plants and algae, as well as the bacterial cyclodextrin glucanotransferases (CGTases, EC 2.4.1.19). 4alphaGTases belong to the glycoside hydrolase GH13, GH57, and GH77 families as classified by the CAZy database. Pyrobaculum aerophilum amylomaltase belongs to GH77 | Oryza sativa Japonica Group |
| additional information | the catalytic triad residues of TaAM consist of D293, E340, and D395 as a nucleophile, acid-base catalyst, and transition state-stabilizer, respectively. Structure-function analysis, overview | Thermus aquaticus |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Pyrobaculum aerophilum |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Pyrobaculum calidifontis |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Aquifex aeolicus |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Corynebacterium glutamicum |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Streptococcus agalactiae |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Thermus aquaticus |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Thermus filiformis |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Thermus brockianus |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Thermus thermophilus |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Acidothermus cellulolyticus |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Borreliella burgdorferi |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Escherichia coli |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Saccharophagus degradans |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Synechocystis sp. PCC 6803 |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Thermus scotoductus |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Arabidopsis thaliana |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Manihot esculenta |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Solanum tuberosum |
| physiological function | 4-alpha-glucanotransferases (4alphaGTases) catalyze a hydrolysis of an alpha-1,4-linkage and a transfer of a (1,4)-alpha-D-glucan to an acceptor. The intermolecular transglycosylation or disproportionation reaction results in longer chain linear oligosaccharides, while the intramolecular transglycosylation or cyclization reaction produces large-ring cyclodextrins (LR-CDs) or cycloamyloses (CAs), which is a dominant feature in this group. Large-ring cyclodextrin (LR-CD) or cycloamylose (CA) are cyclic (1,4)-alpha-D-glucan polymers consisting of nine or more glucose units, a higher degree of polymerization (DP) than well-known cyclodextrins (alpha-, beta-, and gamma-cyclodextrins (CDs) or CD6, CD7, and CD8). LR-CDs can be produced from starch or linear amylose by an enzymatic reaction of 4alphaGTases, especially the amylomaltases and D-enzymes | Oryza sativa Japonica Group |
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