Crystallization (Comment) | Organism |
---|---|
crystal structures of the enzyme and its complex with maltose are determined at 2.4 A and 2.1 A resolution. Crystals belong to space group P4(1)22 with unit-cell dimensions a = b = 148.7 A, c = 106.7 A | Thermotoga maritima |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermotoga maritima | O33838 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme catalyzes the transfer of maltosyl units from alpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, malto-oligosaccharides or glucose. Analysis of maltose binding in the active site reveals that the transfer of dextrinyl residues longer than a maltosyl unit is prevented by termination of the active-site cleft after the -2 subsite by the side-chain of Lys151 and the stretch of residues 314-317, providing an explanation for the strict transfer specificity of MTase | Thermotoga maritima | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | each subunit consists of four domains | Thermotoga maritima |
Synonyms | Comment | Organism |
---|---|---|
maltosyltransferase | - |
Thermotoga maritima |