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Information on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase and Organism(s) Aspergillus sulphureus and UniProt Accession Q2LE69

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Aspergillus sulphureus
UNIPROT: Q2LE69 not found.
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The taxonomic range for the selected organisms is: Aspergillus sulphureus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
beta-mannanase, endo-beta-mannanase, man5a, endo-mannanase, manb-1601, man26a, endo-beta-1,4-mannanase, man26b, man5c, endo-1,4-beta-mannanase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-beta-D-mannan mannanohydrolase
-
-
-
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beta-1,4-mannan 4-mannanohydrolase
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-
-
-
beta-D-mannanase
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-
-
-
Beta-mannanase
beta-mannanase B
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-
-
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endo-1,4-beta-mannanase
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-
-
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endo-1,4-mannanase
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-
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endo-beta-1,4-mannase
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-
-
-
endo-beta-mannanase
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-
-
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mannanase, endo-1,4-beta-
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
4-beta-D-mannan mannanohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
37288-54-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
locust bean gum + H2O
?
show the reaction diagram
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-
-
?
konjac glucomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
show the reaction diagram
-
-
-
-
?
locust bean gum galactomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 7
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more than 80% of enzyme activity is retained in the pH range 2.0-7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
-
more than 50% activity between 30 and 70°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q2LE69_9EURO
383
0
41452
TrEMBL
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
41389
x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
48000
x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
treatment with Endo H leads to 30% loss of enzymic activity and a reduction in molecular weight by about 9 kDa
glycoprotein
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the enzyme has three N-glycosylation sites (N173, N242, N313) and two O-glycosylation sites (S5, S334)
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
half-life 50 min
40 - 60
-
the enzyme remains stable for 12 h at 40°C and exhibits about 30% activity after 2 h at 50°C. The enzyme shows no activity at 60°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is stable at room temperature for at least 2 days
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris
expressed in Saccharomyces cerevisiae strain BY4741
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, X.; Cao, Y.; Ding, Y.; Lu, W.; Li, D.
Cloning, functional expression and characterization of Aspergillus sulphureus beta-mannanase in Pichia pastoris
J. Biotechnol.
128
452-461
2007
Aspergillus sulphureus (Q2LE69), Aspergillus sulphureus
Manually annotated by BRENDA team
Liu, J.; Basit, A.; Miao, T.; Zheng, F.; Yu, H.; Wang, Y.; Jiang, W.; Cao, Y.
Secretory expression of beta-mannanase in Saccharomyces cerevisiae and its high efficiency for hydrolysis of mannans to mannooligosaccharides
Appl. Microbiol. Biotechnol.
102
10027-10041
2018
Aspergillus sulphureus, Aspergillus sulphureus CGMCC0608
Manually annotated by BRENDA team