EC Number   |
General Information |
Reference |
|---|
    2.4.1.25 | 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 |
-, 778609 |
| 2.4.1.25 | evolution |
the enzyme belongs to the glycoside hydrolase family 77, GH77 |
-, 777638 |
| 2.4.1.25 | evolution |
the enzyme belongs to the glycoside hydrolase family 77, GH77, which contains specific 4-alpha-glucanotransferases identified only in plants and algae (known as disproportionating or D-enzymes) and in prokaryotes (amylomaltases). Most of the GH77 enzymes reported in CAZy are of bacterial origin, while only few are from Archaea, plants, and algae. The gene encoding the amylomaltase in halophilic archaeon Haloquadratum walsbyi is not part of any operon involved in the metabolism of maltooligosaccharides or glycogen, as it has been found in bacteria. The gene has specific insertions yet unknown in homologous genes in prokaryotes, and present only in amylomaltase genes identified in the genomes of other Haloquadratum walsbyi strains. Amylomaltases can be classified in at least four distinct groups, structural features, overview |
778398 |
| 2.4.1.25 | evolution |
the enzyme belongs to the glycoside hydrolase family 77, GH77. Comparisons of enzyme sequences, structure-function relationships, and different structure type groups, overview |
-, 776728 |
| 2.4.1.25 | evolution |
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups, sequence comparisons, overview |
-, 776247 |
| 2.4.1.25 | evolution |
the enzyme belongs to the glycoside hydrolase family 77, GH77. The N-terminal domains of G77 members may represent a distinct type of starch-binding domain and define a distinct CBM family, which is supported by studying docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree, preliminary evolutionary distribution of all 100 GH77 amylomaltases into four groups. sequence comparisons, overview |
-, 776247 |
| 2.4.1.25 | metabolism |
a distinct macroscopic debranching pathway is proposed: via 4-alpha-glucanotransferase, the G3-residue of the donor branch is transferred to a long (n >/= 5) linear Gn-residue linked to a different branching G residue |
771779 |
| 2.4.1.25 | metabolism |
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism |
-, 776728 |
| 2.4.1.25 | metabolism |
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism, involvement of amylomaltase in the degradation of glycogen in Escherichia coli |
-, 776728 |
| 2.4.1.25 | metabolism |
amylomaltases in prokaryotes are involved in glycogen degradation and maltose metabolism. Amylomaltase may be involved in the synthesis of trehalose |
-, 776728 |
