Information on EC 3.2.1.84 - glucan 1,3-alpha-glucosidase

for references in articles please use BRENDA:EC3.2.1.84
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
3.2.1.84
-
RECOMMENDED NAME
GeneOntology No.
glucan 1,3-alpha-glucosidase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
hydrolysis of O-glycosyl bond
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
N-Glycan biosynthesis
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
3-alpha-D-glucan 3-glucohydrolase
Does not act on nigeran.
CAS REGISTRY NUMBER
COMMENTARY hide
9073-99-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
E16590
GenBank
Manually annotated by BRENDA team
sequence was found to be identical to previously published data
-
-
Manually annotated by BRENDA team
rich in alpha-(1-3)-glucans
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
mung bean
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-1,3-glucan + H2O
alpha-D-glucose
show the reaction diagram
alpha-1,3-glucans + H2O
alpha-D-glucose
show the reaction diagram
-
exo-wise hydrolysis from non-reducing ends
-
-
?
alpha-1,3-mutan + H2O
alpha-D-glucose
show the reaction diagram
beta-glucan:chitin + H2O
?
show the reaction diagram
mutan
glucan
show the reaction diagram
nigerose + H2O
alpha-D-glucose
show the reaction diagram
pseudonigeran + H2O
alpha-D-glucose
show the reaction diagram
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-1,3-mutan + H2O
alpha-D-glucose
show the reaction diagram
Q96VT3
involved in cell wall synthesis and sexual development
-
-
?
mutan
glucan
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
activates slightly
Na+
-
activates slightly
additional information
-
no or poor effects by Ba2+, K+, and Fe2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-epicastanospermine
-
poor inhibitor
Ca2+
-
moderate inhibition at 1 mM
Co2+
-
moderate inhibition at 1 mM
Cu2+
-
moderate inhibition at 1 mM
Mn2+
-
moderate inhibition at 1 mM
Sn2+
-
moderate inhibition at 1 mM
Zn2+
-
moderate inhibition at 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-1,3-glucan
-
streptococcal mutan, induction
cell wall material from fruiting bodies of Laetiporus sulphureus
-
induction
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.1 - 13
pseudonigeran
-
additional information
additional information
-
Km is 0.73 mg/ml with lyophilized Laetiporus sulphureus cell walls, pH 5.5, 45°C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.178
-
after incubation for 1 h at 45°C, medium supplementation with 2.0% cell wall preparation of Laetiporus sulphureus
1.72
-
after incubation for 1 h at 45°C, medium supplementation with 0.4% cell wall preparation of Laetiporus sulphureus
5.6
E16590
incubation at 35°C for 10 min, stop reaction by adding 0.4 ml of dinitrosalicylic acid solution, N-terminal domain with mutan-binding activity, C-terminal domain with mutanase activity and only low mutan-binding activity
115.6
-
purified enzyme with lyophilized Laetiporus sulphureus cell walls, pH 5.5, 45°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
E16590
80% of residual activity in comparison to the activity at ph 4.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
calculated from amino acid sequence
5.9
calculated from sequence
7.1
-
isoelectric focusing
7.5
-
basic chromatofocusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
-
gel filtration
47000
-
gel filtration
48000
calculated from amino acid sequence
63800
-
calculated from amino acid sequence
73000
12 * 73000, calculated from sequence
88000
-
gel filtration, SDS-PAGE
135000
E16590
by MALDI-TOF mass spectrometry
914000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 7
-
at 4°C
136906
3.5 - 6
-
at 30°C
136907
3.5 - 7
-
at 4°C
136907
4 - 7
-
at 30°C
136906
4.5 - 6
-
purified enzyme, 45°C, 1 h, stable at
731044
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
-
at pH 7.0
43
-
up to at pH 3.5
47
-
up to at pH 4.5
50
-
up to
60
E16590
above unstable, stable for 10 min
95
half-life: 33.8 h
100
half-life: 10.6 h
105
half-life: 1.8 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
alpha-1,3-glucan stabilizes the enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 100 mM acetate buffer, pH 5.5
-
4°C, stored for at least 6 months without any loss of activity
below 60°C, 10 min
E16590
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-fold purification and 98% residual enzyme activity after precipitation with propanol, around 2-fold purification and 77% enzyme recovery after salting out with ammonium sulfate at 50% saturation, 10-fold concentrated preparation of the enzyme with a yield of 98% after ultrafiltration, mutanase recovery of 97% after lyophilization and concentration of the culture broth in a vacuum evaporator
-
by chromatographic procedures
E16590
native extracellular enzyme 18.4fold by ultrafiltration, anion exchange and hydrophobic interaction chromatography, and chromatofocusing to homogeneity
-
yield of 56.3% of alkali-soluble and water-insoluble D-glucan
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
construction of a cDNA library
expressed in Sulfolobus acidocaldarius. Attempts to obtain soluble enzyme from Escherichia coli strains are unsuccessful
recombinant proteins in E. coli strains NV522 an B221
E16590
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium
the water-insoluble fraction of Laetiporus sulphureus fruiting bodies from 0.15 to 0.2% (w/v) induces mutanase activity in Paenibacillus sp. strain MP-1
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
medicine