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Literature summary extracted from
- The structure of the Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding mode (2013), Glycobiology, 23, 1075-1083.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.4.99.16 | free enzyme and enzyme in complex with inhibitor acarbose, hanging drop vapor diffusion technique, mixing of 0.002 ml of 20 mg/ml protein in 40 mM sodium phosphate buffer, pH 6.0, with 0.002 ml of reservoir solution containing 0.1 M sodium cacodylate, pH 6.5, 0.2 M MgCl2, and 10-14% PEG 1000, 20°C, 1 day to 1 week, X-ray diffraction structure determination and analysis at 1.84 A resolution, molecular replacement | Mycolicibacterium smegmatis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.99.16 | acarbose | competitively inhibited by the potent alpha-glucosidase inhibitor acarbose, acarbose-binding site structure, overview | Mycolicibacterium smegmatis |  |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.99.16 | Ca2+ | hepta-coordinated calcium-ion-binding site located about 13 A from the active site at the interface between domain A and domain B, enzyme binding structure, overview | Mycolicibacterium smegmatis | |
| 5.4.99.16 | Cl- | enzyme binding structure of 4 Cl- ions, overview | Mycolicibacterium smegmatis | |
| 5.4.99.16 | Mg2+ | hexa-coordinated magnesium ion located in the solvent-accessible loop L1, residues 50-60, of domain A, about 25 A from the catalytic center, enzyme binding structure, overview. Interactions with this magnesium ion come from Asp51, Asn53, Asp55, Ile57, Asp59 and one water molecule | Mycolicibacterium smegmatis | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 68000 | - |
2 * 68000, SDS-PAGE | Mycolicibacterium smegmatis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.16 | maltose | Mycolicibacterium smegmatis | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Mycolicibacterium smegmatis ATCC 700084 | - |
alpha,alpha-trehalose | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.4.99.16 | Mycolicibacterium smegmatis | A0R6E0 | - |
- |
| 5.4.99.16 | Mycolicibacterium smegmatis ATCC 700084 | A0R6E0 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.16 | maltose | - |
Mycolicibacterium smegmatis | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | two-step, double-displacement mechanism | Mycolicibacterium smegmatis | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Mycolicibacterium smegmatis ATCC 700084 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | two-step, double-displacement mechanism | Mycolicibacterium smegmatis ATCC 700084 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | additional information | trehalose synthase from Mycobacterium smegmatis also possesses an amylase activity, albeit several orders of magnitude lower than its isomerase activity | Mycolicibacterium smegmatis | ? | - |
? | |
| 5.4.99.16 | additional information | trehalose synthase from Mycobacterium smegmatis also possesses an amylase activity, albeit several orders of magnitude lower than its isomerase activity | Mycolicibacterium smegmatis ATCC 700084 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | dimer | 2 * 68000, SDS-PAGE | Mycolicibacterium smegmatis |
| 5.4.99.16 | More | determination and analysis of the structure of the free enzyme and of the enzyme in complex with acarbose, overview. TreS asymmetric unit dimer is tightly held together with numerous hydrogen bonds and van der Waals contacts. The enzyme is thermodynamically stable in both the dimeric and tetrameric states, pointing out there may be a dynamic equilibrium between these two structural forms | Mycolicibacterium smegmatis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | Trehalose synthase | - |
Mycolicibacterium smegmatis |
| 5.4.99.16 | TreS | - |
Mycolicibacterium smegmatis |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | evolution | the enzyme belongs to glycoside hydrolase family GH13 | Mycolicibacterium smegmatis |
| 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 | Mycolicibacterium smegmatis |
| 5.4.99.16 | 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 | Mycolicibacterium smegmatis |
| 5.4.99.16 | physiological function | importance of trehalose to survival of mycobacteria, possible association of the enzyme with glycogen enhances its role in glycogen biosynthesis and degradation | Mycolicibacterium smegmatis |
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