Literature summary for 3.2.1.33 extracted from

Woo, E.J.; Lee, S.; Cha, H.; Park, J.T.; Yoon, S.M.; Song, H.N.; Park, K.H.
Structural Insight into the Bifunctional Mechanism of the Glycogen-debranching Enzyme TreX from the Archaeon Sulfolobus solfataricus (2008), J. Biol. Chem., 283, 28641-28648.

Crystallization (Commentary)

Crystallization (Comment)	Organism
native dimer, native tetramer and the tetramer in complex with acarbose ligand covalently bound to residue D363, occupying subsites -1 to -3. Protein exhibits two different active-site configurations depending on its oligomeric state. The N-terminus of one subunit is located at the active site of the other molecule, resulting in a reshaping of the active site in the tetramer. This is accompanied by a large shift in the flexible loop of amino acids 399-416, creating connected holes inside the tetramer	Saccharolobus solfataricus

Crystallization (Comment)

Organism

native dimer, native tetramer and the tetramer in complex with acarbose ligand covalently bound to residue D363, occupying subsites -1 to -3. Protein exhibits two different active-site configurations depending on its oligomeric state. The N-terminus of one subunit is located at the active site of the other molecule, resulting in a reshaping of the active site in the tetramer. This is accompanied by a large shift in the flexible loop of amino acids 399-416, creating connected holes inside the tetramer

Saccharolobus solfataricus

Protein Variants

Protein Variants	Comment	Organism
D318A	sharp increasein alpha-1,4-transferase activity	Saccharolobus solfataricus
E94A	minor change in the amylo-1,6-glucosidase activity	Saccharolobus solfataricus

Organism

Organism	UniProt	Comment	Textmining
Saccharolobus solfataricus	P95868	bifunctional amylo-1,6-glucosidase and 4-alpha-glucanotransferase	-

Synonyms

Synonyms	Comment	Organism
TreX	-	Saccharolobus solfataricus

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Release 2023.1 (January 2023)