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evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
phylogenetic tree
evolution
the enzyme belongs to glycoside hydrolase family GH13
evolution
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the enzyme belongs to the glycosyl hydrolase family 13
evolution
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the enzyme is a retaining alpha-transglycosidase in the alpha-amylase family (GH13)
evolution
enzyme TtTS belongs to the glycoside hydrolase family 13 and exhibits the typical three domain structure
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
evolution
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phylogenetic tree
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evolution
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phylogenetic tree
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evolution
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enzyme TtTS belongs to the glycoside hydrolase family 13 and exhibits the typical three domain structure
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evolution
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phylogenetic tree
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evolution
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phylogenetic tree
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evolution
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phylogenetic tree
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evolution
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the enzyme belongs to glycoside hydrolase family GH13
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evolution
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phylogenetic tree
-
evolution
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phylogenetic tree
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evolution
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phylogenetic tree
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evolution
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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
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evolution
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phylogenetic tree
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evolution
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phylogenetic tree
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evolution
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phylogenetic tree
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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
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
malfunction
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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
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metabolism
trehalose synthase catalyzes the reversible conversion of maltose into trehalose in mycobacteria as one of three biosynthetic pathways to this nonreducing disaccharide
metabolism
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trehalose synthase catalyzes the reversible conversion of maltose into trehalose in mycobacteria as one of three biosynthetic pathways to this nonreducing disaccharide
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physiological function
importance of trehalose to survival of mycobacteria, possible association of the enzyme with glycogen enhances its role in glycogen biosynthesis and degradation
physiological function
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the enzyme functions primarily in the mobilization of trehalose as a glycogen precursor
physiological function
the thermostable enzyme trehalose synthase from Thermobaculum terrenum (TtTS) catalyzes the reversible interconversion of maltose and trehalose
physiological function
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the thermostable enzyme trehalose synthase from Thermobaculum terrenum (TtTS) catalyzes the reversible interconversion of maltose and trehalose
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physiological function
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importance of trehalose to survival of mycobacteria, possible association of the enzyme with glycogen enhances its role in glycogen biosynthesis and degradation
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additional information
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
additional information
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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
additional information
enzyme structure analysis and molecular modeling, overview
additional information
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enzyme structure analysis and molecular modeling, overview
additional information
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the highly conserved Asp294 residue is critical for catalytic activity, homology modeling and flexible docking studies of the enzyme-substrate system, overview
additional information
residues Tyr213, Glu320 and Glu324 are essential within the +1 subsite for the enzyme activity. The interaction networks between subdomains B and S7 seal the active-site entrance
additional information
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residues Tyr213, Glu320 and Glu324 are essential within the +1 subsite for the enzyme activity. The interaction networks between subdomains B and S7 seal the active-site entrance
additional information
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the C-terminal domain from TtTS plays a key role in maintaining the thermostability, reducing the byproduct glucose formation, and increasing enzyme activity
additional information
the C-terminal domain from TtTS plays a key role in maintaining the thermostability, reducing the byproduct glucose formation, and increasing enzyme activity
additional information
the C-terminal domain in the wild-type enzyme is important for retaining the glucose moiety of the substrate within the active site
additional information
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the C-terminal domain in the wild-type enzyme is important for retaining the glucose moiety of the substrate within the active site
additional information
the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS
additional information
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the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS
additional information
the enzyme's catalytic cleft consists of Asp202-Glu244-Asp310 and various conserved substrate-binding residues, three-dimensional structure enzyme structure and active site structure
additional information
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the enzyme's catalytic cleft consists of Asp202-Glu244-Asp310 and various conserved substrate-binding residues, three-dimensional structure enzyme structure and active site structure
additional information
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the C-terminal domain from TtTS plays a key role in maintaining the thermostability, reducing the byproduct glucose formation, and increasing enzyme activity
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additional information
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the C-terminal domain in the wild-type enzyme is important for retaining the glucose moiety of the substrate within the active site
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additional information
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enzyme structure analysis and molecular modeling, overview
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additional information
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the enzyme's catalytic cleft consists of Asp202-Glu244-Asp310 and various conserved substrate-binding residues, three-dimensional structure enzyme structure and active site structure
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additional information
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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
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additional information
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the highly conserved Asp294 residue is critical for catalytic activity, homology modeling and flexible docking studies of the enzyme-substrate system, overview
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