EC Number   |
General Information |
Reference |
|---|
    5.4.99.16 | evolution |
enzyme TtTS belongs to the glycoside hydrolase family 13 and exhibits the typical three domain structure |
-, 748015 |
| 5.4.99.16 | evolution |
phylogenetic tree |
-, 746863 |
| 5.4.99.16 | evolution |
the enzyme belongs to glycoside hydrolase family GH13 |
-, 727598 |
| 5.4.99.16 | evolution |
the enzyme belongs to the glycosyl hydrolase family 13 |
728630 |
| 5.4.99.16 | evolution |
the enzyme is a retaining alpha-transglycosidase in the alpha-amylase family (GH13) |
727887 |
| 5.4.99.16 | evolution |
trehalose synthase belongs to glycoside hydrolase family 13 (GH13), which includes a diverse range of carbohydrate-metabolizing enzymes. The GH13 enzymes share a catalytic (beta/alpha)8-barrel and a C-terminal beta-sandwich (domain C) as their structurally conserved core. Substrate-induced rotation of subdomain B has been maintained during evolution |
-, 746668 |
| 5.4.99.16 | malfunction |
disruption of the interaction networks through the replacement of Arg148 and Asn253 with alanine results in a decrease in isomerase activity by 8-9fold and an increased hydrolase activity by 1.5-1.8fold. The N253A structure shows a small pore created for water entry. Active site structure and substrate-induced conformational changes, enzyme structure comparisons, detailed overview |
746621 |
| 5.4.99.16 | malfunction |
the C-terminal domain of the three-domain-comprising trehalose synthase from Thermus thermophilus is truncated in order to study the effect on the enzyme's activity and substrate specificity. Two truncated enzymes (DM1 and DM2) show lower maltose- and trehalose-converting activities and a different transglycosylation reaction mechanism compared to the wild-type enzyme. In the mutants, the glucose moiety cleaved from the maltose substrate is released from the enzyme and intercepted by external glucose oxidase, preventing the production of trehalose. Mutant DM1 synthesizes much higher amounts of mannose-containing disaccharide trehalose analogue (Man-TA) than does the wild-type or mutant DM2. The mutant enzymes could be used to produce Man-TA, a postulatedinhibitor of gut disaccharidases |
-, 747681 |
| 5.4.99.16 | metabolism |
trehalose synthase catalyzes the reversible conversion of maltose into trehalose in mycobacteria as one of three biosynthetic pathways to this nonreducing disaccharide |
-, 727598 |
| 5.4.99.16 | more |
determination and analysis of the structure of the enzyme and of the enzyme in complex with acarbose, oligosaccharide-binding site within the C-terminal domain, catalytic site structure, overview. Structure-function analysis |
-, 727598 |
