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Literature summary for 2.4.1.25 extracted from

  • Park, J.; Park, H.; Kang, H.; Hong, J.; Cha, H.; Woo, E.; Kim, J.; Kim, M.; Boos, W.; Lee, S.; Park, K.
    Oligomeric and functional properties of a debranching enzyme (TreX) from the archaeon Sulfolobus solfataricus P2 (2008), Biocatal. Biotransform., 26, 76-85.
No PubMed abstract available
Search for more literature for 2.4.1.25

Activating Compound

Activating Compound Comment Organism Structure
DMSO increases the enzyme's hydrolytic activity Saccharolobus solfataricus

Cloned(Commentary)

Cloned (Comment) Organism
gene treX, cloning from the trehalose biosynthesis gene cluster, expression of the His-tagged enzyme in Escherichia coli Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharolobus solfataricus the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain ?
-
 ?
additional information Saccharolobus solfataricus P2 the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain ?
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
 gene treX
-
Saccharolobus solfataricus P2
-
 gene treX
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain Saccharolobus solfataricus ?
-
 ?
additional information the enzyme exhibits hydrolyzing activity toward alpha-1,6-glycosidic linkages of amylopectin, glycogen, pullulan, and other branched substrates, glycogen is the preferred substrate, TreX shows high specificity for hydrolysis of maltohexaosyl alpha-1,6-beta-cyclodextrin, and high activity in 4-alpha-sulfoxide-glucantransferase activity transferring alpha-1,4-glucan oligosaccharides from one chain to another. The enzyme tetramer shows a 4fold higher catalytic activity than the dimer. The enzyme catalyzes intramolecular transglycosylation of maltooligosacchrides, i.e. disproportionation to produce linear alpha-1,4-glucans, as well as intramolecular transglycosylation of glycogen Saccharolobus solfataricus ?
-
 ?
additional information the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain Saccharolobus solfataricus P2 ?
-
 ?
additional information the enzyme exhibits hydrolyzing activity toward alpha-1,6-glycosidic linkages of amylopectin, glycogen, pullulan, and other branched substrates, glycogen is the preferred substrate, TreX shows high specificity for hydrolysis of maltohexaosyl alpha-1,6-beta-cyclodextrin, and high activity in 4-alpha-sulfoxide-glucantransferase activity transferring alpha-1,4-glucan oligosaccharides from one chain to another. The enzyme tetramer shows a 4fold higher catalytic activity than the dimer. The enzyme catalyzes intramolecular transglycosylation of maltooligosacchrides, i.e. disproportionation to produce linear alpha-1,4-glucans, as well as intramolecular transglycosylation of glycogen Saccharolobus solfataricus P2 ?
-
 ?

Subunits

Subunits Comment Organism
dimer at pH 7.0, gel filtration and analytical sedimentation ultracentrifugation Saccharolobus solfataricus
dimer or tetramer at pH 5.5, gel filtration and analytical sedimentation ultracentrifugation Saccharolobus solfataricus
More the tetramer shows a 4fold higher catalytic activity than the dimer Saccharolobus solfataricus
tetramer at pH 5.5-6.5 in presence of DMSO, gel filtration and analytical sedimentation ultracentrifugation Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
debranching enzyme
-
 Saccharolobus solfataricus
TreX
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
75
-
-
 Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
-
 Saccharolobus solfataricus