Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Deinococcus radiodurans |
Crystallization (Comment) | Organism |
---|---|
purified recombinant enzyme mutant N253F, hanging drop vapour diffusion method, mixing of 0.002 ml of 30 mg/ml protein in 20 mM HEPES, pH 7.5, 100 mM NaCl, 3.3% glycerol, and 1 mM DTT, with 0.0.02 ml of reservoir solution containing 0.3 M Tris-HCl pH 7.0, 7% PEG 4000, and 0.2 M sodium acetate trihydrate, and equilibration against 0.5 ml of reservoir solution, 15°C, 2-3 weeks, X-ray diffraction structure determination and analysis | Deinococcus radiodurans |
Protein Variants | Comment | Organism |
---|---|---|
N253F | site-directed mutagenesis, the apo structure of the DrTS N253F mutant displays a new open conformation with an empty active site. The structure of the N253F mutant is drastically altered compared with that of the wild-type DrTS-Tris complex | Deinococcus radiodurans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
maltose | Deinococcus radiodurans | - |
alpha,alpha-trehalose | - |
r | |
maltose | Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 | - |
alpha,alpha-trehalose | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Deinococcus radiodurans | I3NX86 | - |
- |
Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 | I3NX86 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Deinococcus radiodurans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
maltose | - |
Deinococcus radiodurans | alpha,alpha-trehalose | - |
r | |
maltose | - |
Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 | alpha,alpha-trehalose | - |
r | |
additional information | trehalose synthase catalyzes the reversible conversion of maltose to trehalose. The opening and closing of the active site is probably a rate-limiting protein conformational change | Deinococcus radiodurans | ? | - |
? | |
additional information | trehalose synthase catalyzes the reversible conversion of maltose to trehalose. The opening and closing of the active site is probably a rate-limiting protein conformational change | Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | each N253F mutant protomer consists of the three common GH13 domains [catalytic (beta/alpha)8-barrel, subdomain B and domain C] and two loop-rich modules, S7 and S8, that are unique to trehalose synthase | Deinococcus radiodurans |
Synonyms | Comment | Organism |
---|---|---|
DrTS | - |
Deinococcus radiodurans |
Trehalose synthase | - |
Deinococcus radiodurans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Deinococcus radiodurans |
General Information | Comment | Organism |
---|---|---|
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 | Deinococcus radiodurans |