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Literature summary extracted from

  • Chow, S.Y.; Wang, Y.L.; Hsieh, Y.C.; Lee, G.C.; Liaw, S.H.
    The N253F mutant structure of trehalose synthase from Deinococcus radiodurans reveals an open active-site topology (2017), Acta Crystallogr. Sect. F, 73, 588-594 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.16 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Deinococcus radiodurans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.99.16 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

EC Number Protein Variants Comment Organism
5.4.99.16 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/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.99.16 maltose Deinococcus radiodurans
-
 alpha,alpha-trehalose
-
 r
5.4.99.16 maltose Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422
-
 alpha,alpha-trehalose
-
 r

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.16 Deinococcus radiodurans I3NX86
-
-
5.4.99.16 Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 I3NX86
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.99.16 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Deinococcus radiodurans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.16 maltose
-
 Deinococcus radiodurans alpha,alpha-trehalose
-
 r
5.4.99.16 maltose
-
 Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 alpha,alpha-trehalose
-
 r
5.4.99.16 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 ?
-
 ?
5.4.99.16 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

EC Number Subunits Comment Organism
5.4.99.16 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

EC Number Synonyms Comment Organism
5.4.99.16 DrTS
-
 Deinococcus radiodurans
5.4.99.16 Trehalose synthase
-
 Deinococcus radiodurans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4.99.16 7.4
-
 assay at Deinococcus radiodurans

General Information

EC Number General Information Comment Organism
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 Deinococcus radiodurans