Literature summary for 5.4.99.16 extracted from

Caner, S.; Nguyen, N.; Aguda, A.; Zhang, R.; Pan, Y.T.; Withers, S.G.; Brayer, G.D.
The structure of the Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding mode (2013), Glycobiology, 23, 1075-1083.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Inhibitors	Comment	Organism	Structure
acarbose	competitively inhibited by the potent alpha-glucosidase inhibitor acarbose, acarbose-binding site structure, overview	Mycolicibacterium smegmatis

Metals/Ions

Metals/Ions	Comment	Organism
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
Cl-	enzyme binding structure of 4 Cl- ions, overview	Mycolicibacterium smegmatis
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]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
68000	-	2 * 68000, SDS-PAGE	Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
maltose	Mycolicibacterium smegmatis	-	alpha,alpha-trehalose	-	r
maltose	Mycolicibacterium smegmatis ATCC 700084	-	alpha,alpha-trehalose	-	r

Organism

Organism	UniProt	Comment	Textmining
Mycolicibacterium smegmatis	A0R6E0	-	-
Mycolicibacterium smegmatis ATCC 700084	A0R6E0	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
maltose	-	Mycolicibacterium smegmatis	alpha,alpha-trehalose	-	r
maltose	two-step, double-displacement mechanism	Mycolicibacterium smegmatis	alpha,alpha-trehalose	-	r
maltose	-	Mycolicibacterium smegmatis ATCC 700084	alpha,alpha-trehalose	-	r
maltose	two-step, double-displacement mechanism	Mycolicibacterium smegmatis ATCC 700084	alpha,alpha-trehalose	-	r
additional information	trehalose synthase from Mycobacterium smegmatis also possesses an amylase activity, albeit several orders of magnitude lower than its isomerase activity	Mycolicibacterium smegmatis	?	-	?
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

Subunits	Comment	Organism
dimer	2 * 68000, SDS-PAGE	Mycolicibacterium smegmatis
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

Synonyms	Comment	Organism
Trehalose synthase	-	Mycolicibacterium smegmatis
TreS	-	Mycolicibacterium smegmatis

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to glycoside hydrolase family GH13	Mycolicibacterium smegmatis
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
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
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