Literature summary for 3.2.1.141 extracted from

Okazaki, N.; Tamada, T.; Feese, M.D.; Kato, M.; Miura, Y.; Komeda, T.; Kobayashi, K.; Kondo, K.; Blaber, M.; Kuroki, R.
Substrate recognition mechanism of a glycosyltrehalose trehalohydrolase from Sulfolobus solfataricus KM1 (2012), Protein Sci., 21, 539-552.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method at 4°C. The crystal structure of the E283Q mutant enzyme in complex with the substrate, maltotriosyltrehalose is determined to 2.6 A resolution. The structure with maltotriosyltrehalose indicates that the enzyme has at least five substrate binding subsites and that Glu283 is the catalytic acid, and Asp252 is the nucleophile that attacks the C1 carbon in the glycosidic linkage of maltotriosyltrehalose	Saccharolobus solfataricus

Crystallization (Comment)

Organism

hanging drop vapor diffusion method at 4°C. The crystal structure of the E283Q mutant enzyme in complex with the substrate, maltotriosyltrehalose is determined to 2.6 A resolution. The structure with maltotriosyltrehalose indicates that the enzyme has at least five substrate binding subsites and that Glu283 is the catalytic acid, and Asp252 is the nucleophile that attacks the C1 carbon in the glycosidic linkage of maltotriosyltrehalose

Saccharolobus solfataricus

Protein Variants

Protein Variants	Comment	Organism
D252E	mutant shows 0.03% of enzymatic activity compared to the wild-type	Saccharolobus solfataricus
D252S	mutant shows 0.6% of enzymatic activity compared to the wild-type	Saccharolobus solfataricus
E283Q	mutant shows 0.04% of enzymatic activity compared to the wild-type	Saccharolobus solfataricus

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	Q55088	-	-
Saccharolobus solfataricus KM1	Q55088	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the crystal structure reveals a scheme for substrate recognition that involves two unique interactions: stacking of Tyr325 with the terminal glucose ring of the trehalose moiety and perpendicularly placement of Trp215 to the pyranose rings at the subsites -1 and +1 glucose	Saccharolobus solfataricus	?	-	?
additional information	the crystal structure reveals a scheme for substrate recognition that involves two unique interactions: stacking of Tyr325 with the terminal glucose ring of the trehalose moiety and perpendicularly placement of Trp215 to the pyranose rings at the subsites -1 and +1 glucose	Saccharolobus solfataricus KM1	?	-	?

Synonyms

Synonyms	Comment	Organism
glycosyltrehalose trehalohydrolase	-	Saccharolobus solfataricus
GTHase	-	Saccharolobus solfataricus