| Application | Comment | Organism |
|---|---|---|
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Thermus thermophilus |
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Pyrobaculum aerophilum |
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Pyrobaculum calidifontis |
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Thermoproteus uzoniensis |
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Deinococcus geothermalis |
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Acidothermus cellulolyticus |
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Thermus aquaticus |
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Thermus brockianus |
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Thermus filiformis |
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Thermus scotoductus |
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Streptococcus agalactiae |
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Escherichia coli |
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Aquifex aeolicus |
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Corynebacterium glutamicum |
| additional information | potential industrial application of amylomaltases from extremophilic Bacteria and Archaea, overview | Haloquadratum walsbyi |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Thermus thermophilus |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Pyrobaculum aerophilum |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Pyrobaculum calidifontis |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Thermoproteus uzoniensis |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Deinococcus geothermalis |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Acidothermus cellulolyticus |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Thermus aquaticus |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Thermus brockianus |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Thermus filiformis |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Thermus scotoductus |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Streptococcus agalactiae |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Escherichia coli |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Aquifex aeolicus |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Corynebacterium glutamicum |
| synthesis | starch modifications and synthesis of cycloamyloses (CAs) for applicative purposes, detailed overview | Haloquadratum walsbyi |
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure analysis (PDB ID 1ESW), structure comparisons, detailed overview | Thermus aquaticus |
| crystal structure analysis (PDB ID 1FP8), structure comparisons, detailed overview | Thermus thermophilus |
| crystal structure analysis (PDB ID 1TZ7), structure comparisons, detailed overview | Aquifex aeolicus |
| crystal structure analysis (PDB ID 2X1I), structure comparisons, detailed overview | Thermus brockianus |
| crystal structure analysis (PDB ID 4S3P), structure comparisons, detailed overview | Escherichia coli |
| crystal structure analysis (PDB ID 5B68), structure comparisons, detailed overview | Corynebacterium glutamicum |
| crystal structure analysis (PDB ID 6M6T), structure comparisons, detailed overview | Streptococcus agalactiae |
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acidothermus cellulolyticus | A0LVB3 | - |
- |
| Acidothermus cellulolyticus 11B | A0LVB3 | - |
- |
| Acidothermus cellulolyticus ATCC 43068 | A0LVB3 | - |
- |
| Acidothermus cellulolyticus DSM 8971 | A0LVB3 | - |
- |
| Aquifex aeolicus | O66937 | - |
- |
| 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 | - |
- |
| Deinococcus geothermalis | Q1J0L5 | - |
- |
| Deinococcus geothermalis AG-3a | Q1J0L5 | - |
- |
| Deinococcus geothermalis CIP 105573 | Q1J0L5 | - |
- |
| Deinococcus geothermalis DSM 11300 | Q1J0L5 | - |
- |
| Escherichia coli | P15977 | - |
- |
| Escherichia coli K12 | P15977 | - |
- |
| Haloquadratum walsbyi | - |
- |
- |
| 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 | - |
- |
| Streptococcus agalactiae | A0A0E1EIJ0 | - |
- |
| Thermoproteus uzoniensis | F2L2Q5 | - |
- |
| Thermoproteus uzoniensis 768-20 | F2L2Q5 | - |
- |
| Thermus aquaticus | Q6JHX9 | - |
- |
| Thermus brockianus | Q2VJA0 | - |
- |
| Thermus filiformis | A0A0K0Q020 | - |
- |
| Thermus scotoductus | A0A430UEB1 | - |
- |
| Thermus thermophilus | O87172 | - |
- |
| Thermus thermophilus | Q5SIV3 | - |
- |
| Thermus thermophilus AT-62 | O87172 | - |
- |
| Thermus thermophilus ATCC 27634 | Q5SIV3 | - |
- |
| Thermus thermophilus DSM 579 | Q5SIV3 | - |
- |
| 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview | Thermus thermophilus | |
| 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview | Pyrobaculum aerophilum | |
| 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview | Pyrobaculum calidifontis | |
| 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview | Thermoproteus uzoniensis | |
| 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview | Deinococcus geothermalis | |
| 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview | Acidothermus cellulolyticus | |
| 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview | Thermus brockianus | |
| 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview | Thermus filiformis | |
| 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview | Thermus scotoductus | |
| 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview | Streptococcus agalactiae | |
| 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview | Escherichia coli | |
| 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview | Aquifex aeolicus | |
| 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview | Corynebacterium glutamicum | |
| 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 | reactions catalyzed by 4alpha-GTases: disproportionation, transglycosylation, and cyclization, overview | Haloquadratum walsbyi |
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Maltotetraose and maltopentaose are the most effective substrates for the Thermus thermophilus enzyme | Thermus thermophilus | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Kinetic values indicate the maximum efficiency (kcat/Km) for maltotriose, with decreasing values for the other substrates as their length increase | Pyrobaculum aerophilum | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Pyrobaculum calidifontis | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Thermoproteus uzoniensis | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Synthesis of cycloamyloses (CAs) of small dimensions (DP of 5 and 7) is described for amylomaltase from the thermophilic bacterium Deinococcus geothermalis using as substrate the debranched products of amylomaize, instead of the usually used potato amylose or rice amylose | Deinococcus geothermalis | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Acidothermus cellulolyticus | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Products have a degree of polymerization between 19 and 35. Cyclization is favored by raising the temperature to 70°C and lowering the pH to 5. Synthesis of cycloamyloses (CAs) of small dimensions (DP of 5 and 7) is also described for amylomaltase from the thermophilic bacterium Thermus aquaticus using as substrate the debranched products of amylomaize, instead of the usually used potato amylose or rice amylose | Thermus aquaticus | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Enzyme specific activity of amylomaltase from Thermus brockianus decreases from maltotriose to maltoheptaose | Thermus brockianus | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Maltotriose is the most effective substrate for the Thermus filiformis enzyme, products have a degree of polymerization between 22 and 29 | Thermus filiformis | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Synthesis of cycloamyloses (CAs) of small dimensions (DP of 5 and 7) is described for amylomaltase from the thermophilic bacterium Thermus scotoductus using as substrate the debranched products of amylomaize, instead of the usually used potato amylose or rice amylose | Thermus scotoductus | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Streptococcus agalactiae | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Escherichia coli | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Highest catalytic efficiency is found for maltopentaose, with decreasing values for all the other substrates, products have a degree of polymerization between 16 and 50 | Aquifex aeolicus | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Corynebacterium glutamicum | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Haloquadratum walsbyi | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Corynebacterium glutamicum ATCC 13032 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Kinetic values indicate the maximum efficiency (kcat/Km) for maltotriose, with decreasing values for the other substrates as their length increase | Pyrobaculum aerophilum IM2 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Pyrobaculum calidifontis VA1 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Maltotetraose and maltopentaose are the most effective substrates for the Thermus thermophilus enzyme | Thermus thermophilus AT-62 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Synthesis of cycloamyloses (CAs) of small dimensions (DP of 5 and 7) is described for amylomaltase from the thermophilic bacterium Deinococcus geothermalis using as substrate the debranched products of amylomaize, instead of the usually used potato amylose or rice amylose | Deinococcus geothermalis DSM 11300 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Acidothermus cellulolyticus 11B | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Corynebacterium glutamicum DSM 20300 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Kinetic values indicate the maximum efficiency (kcat/Km) for maltotriose, with decreasing values for the other substrates as their length increase | Pyrobaculum aerophilum DSM 7523 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Pyrobaculum calidifontis JCM 11548 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Maltotetraose and maltopentaose are the most effective substrates for the Thermus thermophilus enzyme | Thermus thermophilus DSM 579 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Acidothermus cellulolyticus ATCC 43068 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Thermoproteus uzoniensis 768-20 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Escherichia coli K12 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Corynebacterium glutamicum JCM 1318 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Corynebacterium glutamicum LMG 3730 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Corynebacterium glutamicum NCIMB 10025 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Kinetic values indicate the maximum efficiency (kcat/Km) for maltotriose, with decreasing values for the other substrates as their length increase | Pyrobaculum aerophilum ATCC 51768 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Maltotetraose and maltopentaose are the most effective substrates for the Thermus thermophilus enzyme | Thermus thermophilus ATCC 27634 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Kinetic values indicate the maximum efficiency (kcat/Km) for maltotriose, with decreasing values for the other substrates as their length increase | Pyrobaculum aerophilum JCM 9630 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Kinetic values indicate the maximum efficiency (kcat/Km) for maltotriose, with decreasing values for the other substrates as their length increase | Pyrobaculum aerophilum NBRC 100827 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Corynebacterium glutamicum BCRC 11384 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Synthesis of cycloamyloses (CAs) of small dimensions (DP of 5 and 7) is described for amylomaltase from the thermophilic bacterium Deinococcus geothermalis using as substrate the debranched products of amylomaize, instead of the usually used potato amylose or rice amylose | Deinococcus geothermalis AG-3a | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Pyrobaculum calidifontis DSM 21063 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Acidothermus cellulolyticus DSM 8971 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Corynebacterium glutamicum CCUG 27702 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Corynebacterium glutamicum NBRC 12168 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Corynebacterium glutamicum NRRL B-2784 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Corynebacterium glutamicum 534 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Kinetic values indicate the maximum efficiency (kcat/Km) for maltotriose, with decreasing values for the other substrates as their length increase | Pyrobaculum aerophilum CIP 104966 | ? | - |
- |
|
| additional information | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Synthesis of cycloamyloses (CAs) of small dimensions (DP of 5 and 7) is described for amylomaltase from the thermophilic bacterium Deinococcus geothermalis using as substrate the debranched products of amylomaize, instead of the usually used potato amylose or rice amylose | Deinococcus geothermalis CIP 105573 | ? | - |
- |
| Synonyms | Comment | Organism |
|---|---|---|
| 4alpha-GTase | - |
Thermus thermophilus |
| 4alpha-GTase | - |
Pyrobaculum aerophilum |
| 4alpha-GTase | - |
Pyrobaculum calidifontis |
| 4alpha-GTase | - |
Thermoproteus uzoniensis |
| 4alpha-GTase | - |
Deinococcus geothermalis |
| 4alpha-GTase | - |
Acidothermus cellulolyticus |
| 4alpha-GTase | - |
Thermus aquaticus |
| 4alpha-GTase | - |
Thermus brockianus |
| 4alpha-GTase | - |
Thermus filiformis |
| 4alpha-GTase | - |
Thermus scotoductus |
| 4alpha-GTase | - |
Streptococcus agalactiae |
| 4alpha-GTase | - |
Escherichia coli |
| 4alpha-GTase | - |
Aquifex aeolicus |
| 4alpha-GTase | - |
Corynebacterium glutamicum |
| 4alpha-GTase | - |
Haloquadratum walsbyi |
| amylomaltase | - |
Thermus thermophilus |
| amylomaltase | - |
Pyrobaculum aerophilum |
| amylomaltase | - |
Pyrobaculum calidifontis |
| amylomaltase | - |
Thermoproteus uzoniensis |
| amylomaltase | - |
Deinococcus geothermalis |
| amylomaltase | - |
Acidothermus cellulolyticus |
| amylomaltase | - |
Thermus aquaticus |
| amylomaltase | - |
Thermus brockianus |
| amylomaltase | - |
Thermus filiformis |
| amylomaltase | - |
Thermus scotoductus |
| amylomaltase | - |
Streptococcus agalactiae |
| amylomaltase | - |
Escherichia coli |
| amylomaltase | - |
Aquifex aeolicus |
| amylomaltase | - |
Corynebacterium glutamicum |
| amylomaltase | - |
Haloquadratum walsbyi |
| MalQ | - |
Thermus thermophilus |
| MalQ | - |
Pyrobaculum aerophilum |
| MalQ | - |
Pyrobaculum calidifontis |
| MalQ | - |
Thermoproteus uzoniensis |
| MalQ | - |
Deinococcus geothermalis |
| MalQ | - |
Acidothermus cellulolyticus |
| MalQ | - |
Thermus aquaticus |
| MalQ | - |
Thermus brockianus |
| MalQ | - |
Thermus filiformis |
| MalQ | - |
Thermus scotoductus |
| MalQ | - |
Streptococcus agalactiae |
| MalQ | - |
Escherichia coli |
| MalQ | - |
Aquifex aeolicus |
| MalQ | - |
Corynebacterium glutamicum |
| MalQ | - |
Haloquadratum walsbyi |
| prokaryotic 4-alpha-glucanotransferase | - |
Thermus thermophilus |
| prokaryotic 4-alpha-glucanotransferase | - |
Pyrobaculum aerophilum |
| prokaryotic 4-alpha-glucanotransferase | - |
Pyrobaculum calidifontis |
| prokaryotic 4-alpha-glucanotransferase | - |
Thermoproteus uzoniensis |
| prokaryotic 4-alpha-glucanotransferase | - |
Deinococcus geothermalis |
| prokaryotic 4-alpha-glucanotransferase | - |
Acidothermus cellulolyticus |
| prokaryotic 4-alpha-glucanotransferase | - |
Thermus aquaticus |
| prokaryotic 4-alpha-glucanotransferase | - |
Thermus brockianus |
| prokaryotic 4-alpha-glucanotransferase | - |
Thermus filiformis |
| prokaryotic 4-alpha-glucanotransferase | - |
Thermus scotoductus |
| prokaryotic 4-alpha-glucanotransferase | - |
Streptococcus agalactiae |
| prokaryotic 4-alpha-glucanotransferase | - |
Escherichia coli |
| prokaryotic 4-alpha-glucanotransferase | - |
Aquifex aeolicus |
| prokaryotic 4-alpha-glucanotransferase | - |
Corynebacterium glutamicum |
| prokaryotic 4-alpha-glucanotransferase | - |
Haloquadratum walsbyi |
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
- |
Thermus filiformis |
| 70 | - |
- |
Thermus aquaticus |
| 70 | 75 | - |
Thermus brockianus |
| 70 | 75 | - |
Thermus thermophilus |
| 90 | - |
- |
Aquifex aeolicus |
| 95 | - |
- |
Pyrobaculum aerophilum |
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
about 90% activity remaining | Thermus thermophilus |
| 80 | - |
about 90% activity remaining | Thermus aquaticus |
| 80 | - |
about 90% activity remaining | Aquifex aeolicus |
| 95 | - |
70% activity remaining after 55 min | Pyrobaculum aerophilum |
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
- |
Thermus aquaticus |
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Thermus thermophilus |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Pyrobaculum aerophilum |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Pyrobaculum calidifontis |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Thermoproteus uzoniensis |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Deinococcus geothermalis |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Acidothermus cellulolyticus |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Thermus aquaticus |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Thermus brockianus |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Thermus filiformis |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Thermus scotoductus |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Streptococcus agalactiae |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Escherichia coli |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Aquifex aeolicus |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Corynebacterium glutamicum |
| evolution | the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview | Haloquadratum walsbyi |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism | Thermus thermophilus |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism | Pyrobaculum aerophilum |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism | Pyrobaculum calidifontis |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism | Thermoproteus uzoniensis |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism | Deinococcus geothermalis |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism | Acidothermus cellulolyticus |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism | Thermus aquaticus |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism | Thermus brockianus |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism | Thermus filiformis |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism | Thermus scotoductus |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism | Streptococcus agalactiae |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism, involvement of amylomaltase in the degradation of glycogen in Escherichia coli | Escherichia coli |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. In Aquifex aeolicus, the enzyme might be involved in the metabolism of glycogen, since its gene is located in the glycogen operon and the bacterium lacks the gene for the maltose transport proteins | Aquifex aeolicus |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. Amylomaltase may be involved in the synthesis of trehalose | Corynebacterium glutamicum |
| metabolism | amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism | Haloquadratum walsbyi |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Presence of glucoamylase-resistant glucans among the products of the reaction of the Thermus thermophilus enzyme on amylose | Thermus thermophilus |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Pyrobaculum aerophilum |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Pyrobaculum calidifontis |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Thermoproteus uzoniensis |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Deinococcus geothermalis |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Acidothermus cellulolyticus |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Thermus aquaticus |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Thermus brockianus |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Thermus filiformis |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Thermus scotoductus |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Streptococcus agalactiae |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Escherichia coli |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Aquifex aeolicus |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan. Amylomaltase may be involved in the synthesis of trehalose in Corynebacterium glutamicum. The sugar is required by the bacterium to counteract osmotic stress and for the production of mycolic acids, important components of the cell envelope in Corynebacteriaceae | Corynebacterium glutamicum |
| physiological function | amylomaltases (4-alpha-glucanotransferases) are enzymes which can perform a double-step catalytic process, resulting in a transglycosylation reaction. They hydrolyse glucosidic bonds of alpha-1,4'-D-glucans and transfer the glucan portion with the newly available anomeric carbon to the 4'-position of an alpha-1,4'-D-glucan acceptor. The intramolecular reaction produces a cyclic alpha-1,4'-glucan | Haloquadratum walsbyi |