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	
2.4.1.25	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	776728	
2.4.1.25	metabolism	key enzymes in the pathway for maltose catabolism. Glucose derived from the action of 4-alpha-glucanotransferase is subsequently metabolized via an Embden-Meyerhof pathway	748071	
2.4.1.25	additional information	analysis of the functional amino acid positions of Corynebacterium glutamicum amylomaltase (CgAM) involved in LR-CD synthesis, overview. Molecular interactions analysis using the three-dimensional crystal structure of enzyme CgAM (PDB ID 5B68), computational analysis	-, 777118	
2.4.1.25	additional information	MQ-01 fails to exhibit mutagenic activity and does not display clastogenic properties in Chinese hamster lung fibroblast cells. In a 13-week subchronic toxicity study in rats, oral administration of MQ-01 at doses of up to 15 ml/kg body weight/day do not produce compound-related clinical signs or toxicity, changes in body weight gain, food consumption, hematology, clinical chemistry, urinalysis, organ weights, or in any gross and microscopic findings, overview	706686	
2.4.1.25	additional information	the amylomaltase from Corynebacterium glutamicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview	-, 776247	
2.4.1.25	additional information	the amylomaltase from Escherichia coli, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Residue Tyr108 may be involved in alpha-glucan binding. Molecular docking, overview	-, 776247	
2.4.1.25	additional information	the amylomaltase from Kushneria marisflavi, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview	776247	
2.4.1.25	additional information	the amylomaltase from Pelotomaculum thermopropionicum, a bacterial GH77 member, possesses an N-terminal extension, that forms a distinct immunoglobulin-like fold domain, with unknown function. Molecular docking, overview	-, 776247	
2.4.1.25	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	-, 778609	
2.4.1.25	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	-, 778609	
2.4.1.25	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	-, 776728	
2.4.1.25	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	-, 776728	
2.4.1.25	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	-, 776728	
2.4.1.25	physiological function	enzyme amylomaltase (AMM) from Thermus thermophilus is a thermo-active 4-alpha-glucanotransferase. It catalyzes the transfer of linear glucan segments from the donor amylose (AM) to the acceptor non-reducing end of the amylopectin (AP) chains via a disproportionation reaction. In a model starch system, AMM can in situ change starch fine molecular structure by elongating the AP chains at the expense of the length of AM chains resulting in significantly lower extent and rate of starch digestion	777344	
2.4.1.25	physiological function	enzyme amylomaltase has the ability to synthesize cyclic glucans, or large ring cyclodextrins (LR-CDs), with a degree of polymerization (DP) of more than eight through intramolecular transglycosylation reaction. The LR-CDs are highly soluble in water and relatively have a larger hydrophobic cavity compared to the small ring cyclodextrin	-, 777118	
2.4.1.25	physiological function	glycogen debranching enzyme (GDE) is bifunctional in that it exhibits both 4-alpha-glucanotransferase (EC 2.4.1.25) and amylo-alpha-1,6-glucosidase activity at two distinct catalytic sites. GDE converts the phosphorylase-limit biantennary branch into a linear maltooligosyl residue, which is then subjected to phosphorylase, and glycogen degradation continues	771779	
2.4.1.25	physiological function	in general, GH77 4-alpha-glucanotransferases catalyse transfer of a glucan chain from one alpha-1,4-glucan to extend another alpha-1,4-glucan or produce a cyclic alpha-1,4-glucan from a single linear alpha-1,4-glucan chain. The enzyme is also known as amylomaltase in prokaryotes and as disproportionating enzyme in plants	-, 776247