Any feedback?
Information on EC 3.2.1.33 - amylo-alpha-1,6-glucosidase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q7LX99
for references in articles please use BRENDA:EC3.2.1.33Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.2.1.33 amylo-alpha-1,6-glucosidaseIUBMB Comments
This enzyme hydrolyses an unsubstituted glucose unit linked by an alpha(1->6) bond to an alpha(1->4) glucose chain. The enzyme activity found in mammals and yeast is in a polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25 (4-alpha-glucanotransferase), which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can then hydrolyse. Together, these two activities constitute the glycogen debranching system.
Specify your search results
Word Map
- 3.2.1.33
- glycogenosis
- myopathy
- hepatomegaly
- maltase
-
gsd-iii
-
maltotetraosyl
- maltooligosaccharide
-
maltotriosyl
- medicine
- synthesis
- nutrition
- analysis
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
amylo-1,6-glucosidase, debrancher enzyme, amylo-alpha-1,6-glucosidase, debrancher protein, amylo-alpha-1,6-glucosidase activity, amylo-1,6-glucosidase/4-alpha-glucanotransferase, dextrin 6-glucohydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-glucan-4-glucosyltransferase/amylo-1,6-glucosidase
-
-
-
-
4-alpha-glucano-transferase amylo-1,6-glucosidase
-
-
-
-
alpha-(1,6)-glucosidase
-
-
-
-
amylo-1,6-glucosidase
-
-
-
-
amylo-1,6-glucosidase-oligo-1,4-1,4-transferase
-
-
-
-
amylo-1,6-glucosidase/1,4-alpha-glucan 4-alpha-glucan 4-alpha-glycosyltransferase
-
-
-
-
amylo-1,6-glucosidase/1,4-alpha-glucan:1,4-alpha-glucan 4-alpha-glycosyltransferase
-
-
-
-
amylo-1,6-glucosidase/4-alpha-glucanotransferase
-
-
-
-
amylo-1,6-glucosidase/oligo-1,4-1,4-glucantransferase
-
-
-
-
amylopectin 1,6-glucosidase
-
-
-
-
debrancher enzyme
-
-
-
-
debrancher protein
-
-
-
-
dextrin 6-alpha-D-glucosidase
-
-
-
-
dextrin 6-alpha-glucosidase
-
-
-
-
dextrin 6-glucanohydrolase
-
-
-
-
dextrin 6-glucohydrolase
-
-
-
-
dextrin-1,6-glucosidase
-
-
-
-
dextrin:6-glucohydrolase
-
-
-
-
glucosidase, amylo-1,6-
-
-
-
-
glucosidase/transferase
-
-
-
-
glycogen debranching enzyme
-
-
-
-
glycogen phosphorylase limit dextrin debranching system
-
-
-
-
indirect debranching enzyme
-
-
-
-
oligo-alpha-1,4-glucan:alpha-1,4-glucan-4-glycosyltransferase-amylo-1,6-glucosidase
-
-
-
-
transferase-glucosidase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
glycogen phosphorylase-limit dextrin 6-alpha-glucohydrolase
This enzyme hydrolyses an unsubstituted glucose unit linked by an alpha(1->6) bond to an alpha(1->4) glucose chain. The enzyme activity found in mammals and yeast is in a polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25 (4-alpha-glucanotransferase), which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can then hydrolyse. Together, these two activities constitute the glycogen debranching system.
CAS REGISTRY NUMBER
COMMENTARY
9012-47-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-O-alpha-maltotetraosyl-beta-cyclodextrin + H2O
?
the enzyme catalyzes both hydrolysis of alpha-1,6-glycosidic linkages and transglycosylation at relatively high (above 0.5 mM) substrate concentrations
-
-
?
branched cyclodextrin + H2O
?
the TreX protein has a specificity for hydrolysis of chains consisting of 6 glucose residues or longer
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DMSO
catalytic activity is promoted in the presence of DMSO. DMSO affects the oligomerization state, causing the enzyme dimers to associate into tetramers
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.206
6-O-alpha-maltotetraosyl-beta-cyclodextrin
pH 5.5, 75°C
additional information
amylopectin
Km-values: 31.1 mg/ml at pH 5.5, 75°C, in absence of DMSO. 88.0 mg/ml at pH 5.5, 75°C, in presence of DMSO. 92.3 mg/ml at pH 6.5, 75°C, in absence of DMSO. 345 mg/ml at pH 5.5, 75°C, in presence of DMSO
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2570
6-O-alpha-maltotetraosyl-beta-cyclodextrin
pH 5.5, 75°C
0.48
amylopectin
pH 6.5, 75°C, calculated as microMol maltose released from the substrate, in absence of DMSO
0.923
amylopectin
pH 5.5, 75°C, calculated as microMol maltose released from the substrate, in absence of DMSO
7.57
amylopectin
pH 5.5, 75°C, calculated as microMol maltose released from the substrate, in presence of DMSO
17.35
amylopectin
pH 5.5, 75°C, calculated as microMol maltose released from the substrate, in presence of DMSO
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
catalytic efficiency (the kcat/Km ratio) increases as the degree of polymerization of branch chains rises
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6.5
pH 5.0: about 20% of maximal activity, pH 6.5: about 85% of maximal activity, pH 7.0: about 15% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65 - 80
65°C: about 45% of maximal activity, 80°C: about 80% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme may be involved in glycogen metabolism in debranching and rearranging the side chain of the glycogen by both alpha-1,6-hydrolase and alpha-1,6-transferase activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
355000
tetrameric enzyme form, analytical ultracentrfugation
83000
93091
83000
2 * 83000, the enzyme is mainly dimeric at pH 7.0, SDS-PAGE
83000
4 * 83000, the enzyme is mainly dimeric at pH 5.5-6.5, SDS-PAGE
93091
2 * 93091, the enzyme is mainly dimeric at pH 7.0, calculated from sequence
93091
4 * 93091, the enzyme is mainly dimeric at pH 5.5-6.5, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
dimer
2 * 83000, the enzyme is mainly dimeric at pH 7.0, SDS-PAGE
dimer
2 * 93091, the enzyme is mainly dimeric at pH 7.0, calculated from sequence
tetramer
4 * 83000, the enzyme is mainly dimeric at pH 5.5-6.5, SDS-PAGE
tetramer
4 * 93091, the enzyme is mainly dimeric at pH 5.5-6.5, calculated from sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Biocatal. Biotransform.
26
76-85
2008
Saccharolobus solfataricus (Q7LX99), Saccharolobus solfataricus P2 (Q7LX99)
-
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
J. Biol. Chem.
283
28641-28648
2008
Saccharolobus solfataricus (P95868)
Nguyen, D.H.; Park, J.T.; Shim, J.H.; Tran, P.L.; Oktavina, E.F.; Nguyen, T.L.; Lee, S.J.; Park, C.S.; Li, D.; Park, S.H.; Stapleton, D.; Lee, J.S.; Park, K.H.
The reaction kinetics and the effect of substrate transglycosylation catalyzed by TreX of Sulfolobus solfataricus on glycogen breakdown
J. Bacteriol.
196
1941-1949
2014
Saccharolobus solfataricus (Q7LX99), Saccharolobus solfataricus P2 (Q7LX99)
EXTERNAL LINKS (specific for EC-Number 3.2.1.33)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
