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Information on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase
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EC Tree
3.2.1.78 mannan endo-1,4-beta-mannosidaseSpecify your search results
Word Map
- 3.2.1.78
- mannans
- galactomannans
- locust
- glucomannans
- guar
- konjac
- mannobiose
- alpha-galactosidase
- reesei
- manno-oligosaccharides
- carob
- radicle
-
micropylar
-
mannan-degrading
-
ivory
-
kraft
- mannotetraose
- beta-mannans
- mannopentaose
-
hemicellulase
-
softwood
-
endohydrolases
- cellulosome
- cellvibrio
- endo-1,4-beta-glucanase
-
copra
-
thermomonospora
-
mannan-binding
- food industry
- agriculture
- synthesis
- pharmacology
- degradation
- biotechnology
- paper production
- nutrition
- medicine
- industry
- drug development
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-beta-D-mannan mannanohydrolase
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-
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1,4-beta-mannanase
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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CelB
CsMan5
CtManf
Dtur_0671
endo-1,4-beta-D-mannanase
endo-1,4-beta-mannanase
endo-1,4-mannanase
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-
-
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endo-beta-(1,4)-mannanase
endo-beta-(1->4)-mannanase
endo-beta-1,4 mannanase
endo-beta-1,4-mannanase
endo-beta-1,4-mannase
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-
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endo-beta-D-1,4-mannanase
endo-beta-D-mannanase
endo-beta-mannanase
endo-mannanase
GH5-CBM27
KMAN-3
LeMAN4a
Man
MAN-P
Man26A
Man26b
Man5
Man5A
Man5C
Man5P1
Man5XZ3
Man5_8
ManA
ManB
ManC
ManF
ManH
ManIII
mannan endo-1,4-beta-mannanase
mannan endo-1,4-beta-mannosidase
mannan endo-1.4-beta-D-mannosidase
mannanase, endo-1,4-beta-
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PoMan5A
TpMan
Beta-mannanase
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endo-1,4-beta-mannanase
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endo-beta-mannanase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O = Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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SYSTEMATIC NAME
IUBMB Comments
4-beta-D-mannan mannanohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
37288-54-3
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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
2,4-dinitrophenyl-beta-mannobioside + H2O
2,4-dinitrophenol + beta-mannobiose
-
-
-
-
?
4-methylumbelliferyl mannotrioside + H2O
4-methylumbelliferone + mannotriose
-
-
-
?
beta-1,4-D-mannan + H2O
?
166% of the activity with locust bean gum
main products are manno-oligosaccharides of 2-6 residues and mannose
-
?
beta-1,4-mannan + H2O
beta-1,4-mannotriose + beta-1,4-mannotetraose
-
-
-
-
?
beta-1,4-mannan + H2O
mannose + mannobiose + mannotriose
87% activity compared to konjac glucomannan
-
-
?
beta-galactomannan + H2O
mannobiose + mannotriose + mannotetraose
-
the catalytic efficiency of the enzyme is 6.8fold higher toward galactomannan from locust bean gum, than toward galactomannan from guar gum, but similar toward galactomannan from locust bean gum and glucomannan from konjac flour
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-
?
beta-glucomannan + H2O
mannobiose + mannotriose + mannotetraose
-
the catalytic efficiency of the enzyme is 6.8fold higher toward galactomannan from locust bean gum, than toward galactomannan from guar gum, but similar toward galactomannan from locust bean gum and glucomannan from konjac flour
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-
?
ceratonia siliqua gum + H2O
?
-
46.6% activity compared to locust bean gum
-
-
?
galactoglucomannan + oligosaccharide
[3H]-labelled polysaccharide
-
transglucosylation
-
-
?
galactomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose
-
different contents of glucose and mannose, overview
product ratio overview
-
?
glucomannan + H2O
mannobiose + mannotriose
high activity
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-
?
guar gum + H2O
mannobiose + mannotriose
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-
mannobiose, mannotriose, and a mixture of various mannose-linked oligosaccharides
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?
guar gum + H2O
mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose
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-
product ratio overview
-
?
ivory nut mannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
Paenibacillus sp. HY-8
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-
-
-
?
konjac glucomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
konjac powder + H2O
?
33.5% activity compared to locust bean gum
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-
?
konjac powder + H2O
mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose + mannoheptaose
-
85.1% activity compared to locust bean gum
-
-
?
locust bean gum + H2O
mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose
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-
product ratio overview
-
?
locust bean gum + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
Paenibacillus sp. HY-8
-
-
-
-
?
locust bean gum + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose + mannoheptaose
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100% activity
-
-
?
locust bean gum galactomannan + H2O
?
highest activity
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-
?
locust bean gum galactomannan + H2O
mannobiose + glucosyl-mannosyl oligosaccharides
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main product, with low amounts of mannotriose and higher manno-oligosaccharides
-
?
locust bean gum galactomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
low-viscosity locust bean galactomannan + H2O
?
-
-
-
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
Man-beta-1,4-Man-beta-1,4-Man + Man-beta-1,4-Man
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
Man-beta-1,4-Man + Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + mannose
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-
-
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?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + mannose + Manbeta(1-4)Man
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-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
mannose + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Man
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-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man
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-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + mannose
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + mannose
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-
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?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man-ol + H2O
D-mannitol + Manbeta(1-4)Man-ol + D-mannose + Manbeta(1-4)Manbeta(1-4)Man-ol + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man-ol + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man-ol + Manbeta(1-4)Manbeta(1-4)Man
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-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man-ol + H2O
Manbeta(1-4)Man-ol + Manbeta(1-4)Manbeta(1-4)Man + mannose + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man-ol + Manbeta(1-4)Man
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + mannose
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man
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-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Man + mannose + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
-
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man-ol + H2O
mannose + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man-ol + Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man-ol + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
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-
-
?
mannan + H2O
mannosyl oligosaccharides
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products show a degree of polymerization of 2-6
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?
mannobiose + H2O
mannose + mannobiose
Paenibacillus sp. HY-8
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degradation of mannobiose yields a mixture of mannose (16.6 %) and mannobiose (83.4 %)
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-
?
mannohexaose + H2O
mannotriose + mannotetraose + mannopentaose + mannobiose
-
-
-
?
mannopentaose + H2O
mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose
Paenibacillus sp. HY-8
-
degradation of mannopentaose yields a mixture of mannose (3.1 %), mannobiose (11.2 %), mannotriose (41.1%), mannotetraose (21.7%), and mannopentaose (22.9%)
-
-
?
mannopentaose + H2O
mannotriose + mannobiose + mannotetraose
-
-
-
?
mannotetraose + H2O
mannobiose + mannotriose + mannopentaose
-
-
-
?
mannotetraose + H2O
mannose + mannobiose + mannotriose + mannotetraose
Paenibacillus sp. HY-8
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degradation of mannotetraose yields a mixture of mannose (2.4 %), mannobiose (9.5 %) and mannotriose (62.3%) and mannotetraose (25.8%)
-
-
?
mannotriose + H2O
mannose + mannobiose + mannotriose
Paenibacillus sp. HY-8
-
degradation of mannotriose yields a mixture of mannose (2.8 %), mannobiose (11.8 %) and mannotriose (85.4%)
-
-
?
sesbania gum + H2O
?
-
26% activity compared to konjac glucomannan
-
-
?
xanthan gum + H2O
mannose + mannobiose
-
345.6% activity compared to locust bean gum
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
-
-
-
?
birch wood xylan + H2O
?
9.1% of the activity with locust bean gum
-
-
?
birch wood xylan + H2O
?
9.1% of the activity with locust bean gum
-
-
?
carob galactomannan + H2O
?
56% activity compared to konjac glucomannan
-
-
?
carob glucomannan + H2O
?
13% of the activity with konjac glucomannan
-
-
?
carob glucomannan + H2O
?
13% of the activity with konjac glucomannan
-
-
?
copra meal defatted with n-hexane + H2O
?
-
better substrate than locust bean gum and guar gum
-
-
?
copra meal defatted with n-hexane + H2O
?
-
better substrate than locust bean gum and guar gum
-
-
?
galactomannan + H2O
?
-
the enzyme exhibits higher activity on galactomannan branched with (1->6)-linked alpha-D-galactose than glucomannan
-
-
?
galactomannan + H2O
?
Bacillus subtilis YH12
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the enzyme exhibits higher activity on galactomannan branched with (1->6)-linked alpha-D-galactose than glucomannan
-
-
?
galactomannan + H2O
galactosyl-mannosyl oligosaccharides
-
source of substrate locust bean gum
-
-
?
galactomannan + H2O
galactosyl-mannosyl oligosaccharides
-
products show a degree of polymerization of 2-6
-
?
galactomannan + H2O
galactosyl-mannosyl oligosaccharides
-
enzyme prefers galactomannans with lower degree of galactosylation e.g. from carob gum
-
-
?
glucomannan + H2O
?
219% of the activity with locust bean gum
-
-
?
glucomannan + H2O
?
-
from konjac flour
products are a large amount of oligosaccharides with a degree of polymerizytion of 2-6 and a very small amount of monosaccharide
-
?
glucomannan + H2O
?
-
from konjac flour
products are a large amount of oligosaccharides with a degree of polymerizytion of 2-6 and a very small amount of monosaccharide
-
?
glucomannan + H2O
?
from konjac flour
70% of the activity with locust bean gum
-
?
glucomannan + H2O
glucosyl-mannosyl oligosaccharides
-
source of substrate konjac
-
-
?
glucomannan + H2O
glucosyl-mannosyl oligosaccharides
-
products show a degree of polymerization of 2-6
-
?
guar galactomannan + H2O
?
1.4% of the activity with konjac glucomannan
-
-
?
guar galactomannan + H2O
?
1.4% of the activity with konjac glucomannan
-
-
?
guar gum + H2O
?
highest activity with a mannose to galactose ratio of 79:21
-
-
?
guar gum + H2O
?
-
18.1% activity compared to konjac glucomannan
-
-
?
guar gum + H2O
?
-
18.1% activity compared to konjac glucomannan
-
-
?
guar gum + H2O
?
18% of the activity with locust bean gum
-
-
?
guar gum + H2O
mannobiose + mannotriose + mannose
-
-
-
?
guar gum + H2O
mannose + mannobiose + mannotriose
-
-
mannobiose + mannotriose + mannotetraose
?
insoluble mannan + H2O
mannotriose + mannotetraose + mannopentaose
-
-
-
-
?
insoluble mannan + H2O
mannotriose + mannotetraose + mannopentaose
-
-
-
-
?
ivory nut mannan + H2O
mannotriose + mannotetraose + mannopentaose + mannohexaose
-
main products, at 14%, 25%, 20%, and 13%, respectively
-
?
ivory nut mannan + H2O
mannotriose + mannotetraose + mannopentaose + mannohexaose
-
main products, at 14%, 25%, 20%, and 13%, respectively
-
?
konjac glucomannan + H2O
?
-
highest activity
-
-
?
konjac glucomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
-
-
-
-
?
konjac glucomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
Aspergillus sulphureus CGMCC0608
-
-
-
-
?
konjaku flour + H2O
mannobiose + mannotriose + mannose
-
-
-
?
locust bean galactomannan + H2O
mannotriose + mannotetraose + mannopentaose
-
-
-
-
?
locust bean galactomannan + H2O
mannotriose + mannotetraose + mannopentaose
-
-
-
-
?
locust bean gum + H2O
?
-
88.2% activity compared to konjac glucomannan
-
-
?
locust bean gum + H2O
?
-
88.2% activity compared to konjac glucomannan
-
-
?
locust bean gum + H2O
?
-
main products are manno-oligosaccharides of 2-6 residues and mannose
-
?
locust bean gum + H2O
?
-
products are various manno-oligosaccharides of M2-M6 size and mannose
-
?
locust bean gum + H2O
?
-
enzyme is highly specific for substrate
-
-
?
locust bean gum + H2O
?
-
hydrolysis products are mainly oligosaccharides plus one monosaccharide
-
?
locust bean gum + H2O
?
Niallia circulans CGMCC 1416
-
hydrolysis products are mainly oligosaccharides plus one monosaccharide
-
?
locust bean gum + H2O
mannobiose + mannotriose
-
52.7% mannobiose, 18.1% mannotriose and 29.2% other unidentifiable oligosaccharides
-
?
locust bean gum + H2O
mannobiose + mannotriose
-
52.7% mannobiose, 18.1% mannotriose and 29.2% other unidentifiable oligosaccharides
-
?
locust bean gum + H2O
mannobiose + mannotriose
-
best substrate
mannobiose, mannotriose, and a mixture of various mannose-linked oligosaccharides
-
?
locust bean gum + H2O
mannobiose + mannotriose + mannotetraose
-
best substrate
hydrolysis products are 17.2% mannobiose, 37.4% mannotriose, 9.9% mannotetraose, and 35.5% other unidentified oligosaccharides
-
?
locust bean gum + H2O
mannobiose + mannotriose + mannotetraose
-
best substrate
hydrolysis products are 17.2% mannobiose, 37.4% mannotriose, 9.9% mannotetraose, and 35.5% other unidentified oligosaccharides
-
?
locust bean gum + H2O
mannobiose + mannotriose + mannotetraose
-
-
-
?
locust bean gum + H2O
mannopentaose
-
44%, main product
-
?
locust bean gum galactomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
-
-
-
-
?
locust bean gum galactomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose
Aspergillus sulphureus CGMCC0608
-
-
-
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
2 Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4 mannooligosaccharides with the degree of polymerisation from 4 to 6
64% of product
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
2 Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4-mannooligosaccharides with the degree of polymerisation from 4 to 6
68% of product
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
2 Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4-mannooligosaccharides with the degree of polymerisation from 4 to 6
68% of product
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
2 Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4 mannooligosaccharides with the degree of polymerisation from 4 to 6
64% of product
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
Man-beta-1,4-Man-beta-1,4-Man + Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4 mannooligosaccharides with the degree of polymerisation from 4 to 6
sole products
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
Man-beta-1,4-Man-beta-1,4-Man + Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4-mannooligosaccharides with the degree of polymerisation from 4 to 6
sole products
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
Man-beta-1,4-Man + Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4 mannooligosaccharides with the degree of polymerisation from 4 to 6
88% of products
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
Man-beta-1,4-Man + Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
increasing catalytic efficiency towards beta-1,4-mannooligosaccharides with the degree of polymerisation from 4 to 6
88% of products
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + mannose
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + mannose
-
-
-
?
mannan + H2O
?
the amino-terminal catalytic domain has beta-mannanase activity, and the carboxy-terminal domain acts as an endoglucanase
-
-
?
mannan + H2O
mannotetraose + mannobiose + mannotriose
-
source of substrate: copra
-
-
?
mannan + H2O
mannotetraose + mannobiose + mannotriose
-
source of substrate: copra
-
-
?
mannan + H2O
oligosaccharides
-
-
dimers, trimers and other
?
mannan + H2O
oligosaccharides
-
-
dimers, trimers and other
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
-
-
-
?
mannotetraose + H2O
?
the wild-type enzyme produces mannobiose as dominant product from mannotetraose. The R171K mutant enzyme produces mannotriose and mannose
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
small amounts of mannose and mannotriose
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
small amounts of mannose and mannotriose
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
small amounts of mannose and mannotriose
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
-
-
-
-
?
additional information
?
-
-
production of mannooligosaccharides from pretreated and defatted copra meal hydrolysis by the enzyme
-
-
?
additional information
?
-
-
production of mannooligosaccharides from pretreated and defatted copra meal hydrolysis by the enzyme
-
-
?
additional information
?
-
no activity with mannotriose, barley beta-glucan, birchwood xylan, and carboxymethyl cellulose
-
-
?
additional information
?
-
-
the enzyme shows no activity towards carboxymethyl cellulose, xylan, glucan, pectin, chitin, soluble starch, or alpha-1,6-linked yeast mannan. Also, the enzyme shows no activity on 4-nitrophenyl beta- and alpha-mannosides, beta- and alpha-galactosides, and beta- and alpha-glucosides
-
-
?
additional information
?
-
-
the enzyme shows no activity towards carboxymethyl cellulose, xylan, glucan, pectin, chitin, soluble starch, or alpha-1,6-linked yeast mannan. Also, the enzyme shows no activity on 4-nitrophenyl beta- and alpha-mannosides, beta- and alpha-galactosides, and beta- and alpha-glucosides
-
-
?
additional information
?
-
-
preferably degrades a linear beta-1,4-mannan from green algae Codium fragile producing tri- and disaccharides. no substrate: carboxymethyl cellulose, agarose, dextran and xylan
-
-
?
additional information
?
-
-
the enzyme is involved in release of mannooligosaccharides from spent coffee ground cleaving the backbone at random locations in galactomannan, glucomannan, galactoglucomannan and mannan
-
-
?
additional information
?
-
-
the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides
-
-
?
additional information
?
-
-
the enzyme has no exo-activity and is a typical endo-acting beta-mannanase, substrate specificity, overview. No activity with mannobiose, beechwood xylan, barley beta-glucan, 4-nitrophenyl beta-D-mannoside, and carboxymethyl cellulose
-
-
?
additional information
?
-
-
the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides
-
-
?
additional information
?
-
-
the enzyme has no exo-activity and is a typical endo-acting beta-mannanase, substrate specificity, overview. No activity with mannobiose, beechwood xylan, barley beta-glucan, 4-nitrophenyl beta-D-mannoside, and carboxymethyl cellulose
-
-
?
additional information
?
-
enzyme displays good transgycosylation activity using mannotriose, melezitose and isomaltotriose as acceptors
-
-
?
additional information
?
-
enzyme displays good transgycosylation activity using mannotriose, melezitose and isomaltotriose as acceptors
-
-
?
additional information
?
-
enzyme displays transglycosylation activity using only mannotriose as acceptor
-
-
?
additional information
?
-
enzyme displays transglycosylation activity using only mannotriose as acceptor
-
-
?
additional information
?
-
-
no activity with beechwood xylan, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-mannoside, and carboxymethyl cellulose
-
-
?
additional information
?
-
enzyme displays good transgycosylation activity using mannotriose, melezitose and isomaltotriose as acceptors
-
-
?
additional information
?
-
enzyme displays good transgycosylation activity using mannotriose, melezitose and isomaltotriose as acceptors
-
-
?
additional information
?
-
enzyme displays transglycosylation activity using only mannotriose as acceptor
-
-
?
additional information
?
-
enzyme displays transglycosylation activity using only mannotriose as acceptor
-
-
?
additional information
?
-
-
no activity with beechwood xylan, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-mannoside, and carboxymethyl cellulose
-
-
?
additional information
?
-
negligible activity with starch, carboxymethyl cellulose, and alpha-cellulose
-
-
?
additional information
?
-
-
negligible activity with starch, carboxymethyl cellulose, and alpha-cellulose
-
-
?
additional information
?
-
negligible activity with starch, carboxymethyl cellulose, and alpha-cellulose
-
-
?
additional information
?
-
-
negligible activity with starch, carboxymethyl cellulose, and alpha-cellulose
-
-
?
additional information
?
-
-
no activity with mannobiose, mannotriose, and mannotetraose
-
-
?
additional information
?
-
-
no activity with cellulose, casein and pectin
-
-
?
additional information
?
-
the enzyme does not show activity toward guar galactomannan, 4-nitrophenyl beta-D-mannopyranoside, mannobiose, birchwood xylan, or carboxymethyl cellulose
-
-
?
additional information
?
-
no substrates: mannobiose, mannotriose, mannotetraose, mannohexaose
-
-
?
additional information
?
-
-
no substrates: mannobiose, mannotriose, mannotetraose, mannohexaose
-
-
?
additional information
?
-
-
no substrate: carboxymethyl cellulose
-
-
?
additional information
?
-
-
the enzyme displays no activity towards mannotriose, Avicel and guar gum
-
-
?
additional information
?
-
-
the enzyme displays no activity towards mannotriose, Avicel and guar gum
-
-
?
additional information
?
-
no substrate: mannobiose, or 4-nitrophenyl sugar derivatives
-
-
?
additional information
?
-
no substrate: mannobiose, or 4-nitrophenyl sugar derivatives
-
-
?
additional information
?
-
-
no substrate: mannotriose, mannobiose, enzyme requires a minimum of four sugar units in substrates
-
-
?
additional information
?
-
enzyme shows high endo-beta-1,4-mannanase activity versus various mannans, but low endo-beta-1,4 glucanase activity towards carboxymethylcellulose, andd negligible activity towards glucomannans
-
-
?
additional information
?
-
-
enzyme shows high endo-beta-1,4-mannanase activity versus various mannans, but low endo-beta-1,4 glucanase activity towards carboxymethylcellulose, andd negligible activity towards glucomannans
-
-
?
additional information
?
-
enzyme shows high endo-beta-1,4-mannanase activity versus various mannans, but low endo-beta-1,4 glucanase activity towards carboxymethylcellulose, andd negligible activity towards glucomannans
-
-
?
additional information
?
-
no activity with mannotriose, mannobiose, starch, carboxy methylcellulose, and birchwood xylan
-
-
?
additional information
?
-
-
enzyme is active in hydrolyzing the beta-mannan-rich cell wall of soybean seeds
-
-
?
additional information
?
-
-
enzyme degrades either beta-1,4-mannan or beta-1,4-mannooligosaccharides to mannotriose and mannotetraose. Enzyme disperses the fronds of the red alga Porphyra yezoensis into cell masses consisting of 10-20 cells that are available for cell engineering
-
-
?
additional information
?
-
during hydrolysis of 1,4-beta-manno-oligosaccharides, transglycosylation reactions occur
-
-
?
additional information
?
-
-
during hydrolysis of 1,4-beta-manno-oligosaccharides, transglycosylation reactions occur
-
-
?
additional information
?
-
-
the enzyme hydrolyzes high-molecular weight polysaccharides with beta-1,4-glycosidic bonds
-
-
?
additional information
?
-
-
main by products of the hydrolysis of both guar and locust bean gum are mannose and manno-oligosaccharides of different sizes (mannobiose, mannotriose and mannotetraose). Enzyme mode of action involving a transglycosylation reaction in the mechanism that allows the enzyme to hydrolyze this manno-oligosaccharide. No activity with mannobiose and mannotriose
-
-
?
additional information
?
-
no activity with 4-nitrophenyl beta-D-mannopyranoside
-
-
?
additional information
?
-
-
no activity with carboxymethyl cellulose
-
-
?
additional information
?
-
Klebsiella oxytoca KUB-CW2-3
-
no activity with carboxymethyl cellulose
-
-
?
additional information
?
-
-
no substrate: xylan, caroxymethyl cellulose, cellulose, mannan
-
-
?
additional information
?
-
the native wild-type enzyme shows bifunctional activity as both an endo-glucanase and an endo-mannanase, substrate specificity, overview
-
-
?
additional information
?
-
-
the native wild-type enzyme shows bifunctional activity as both an endo-glucanase and an endo-mannanase, substrate specificity, overview
-
-
?
additional information
?
-
the enzyme also show transglycosylation activity
-
-
?
additional information
?
-
-
the enzyme also show transglycosylation activity
-
-
?
additional information
?
-
the native wild-type enzyme shows bifunctional activity as both an endo-glucanase and an endo-mannanase, substrate specificity, overview
-
-
?
additional information
?
-
the enzyme also show transglycosylation activity
-
-
?
additional information
?
-
no substrate: soluble starch, methylcellulose
-
-
?
additional information
?
-
-
no substrate: soluble starch, methylcellulose
-
-
?
additional information
?
-
Niallia circulans CGMCC 1416
no substrate: soluble starch, methylcellulose
-
-
?
additional information
?
-
Paenibacillus sp. HY-8
-
no activity with carboxymethyl cellulose, soluble starch, birchwood xylan, and pectin
-
-
?
additional information
?
-
-
the enzyme catalyzes the random hydrolysis of beta-1,4-mannosidic linkages in the main chain of mannans, glucomannans and galactomannans, main products are mannobiose, mannotriose, and mannopentaose
-
-
?
additional information
?
-
-
the enzyme catalyzes the random hydrolysis of beta-1,4-mannosidic linkages in the main chain of mannans, glucomannans and galactomannans, main products are mannobiose, mannotriose, and mannopentaose
-
-
?
additional information
?
-
-
no substrate: carboxymethyl cellulose, oat spelt xylan, starch, pectin, 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
additional information
?
-
-
no substrate: carboxymethyl cellulose, oat spelt xylan, starch, pectin, 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
additional information
?
-
enzyme exhibits substantial transglycosylase activity
-
-
?
additional information
?
-
Reinekea sp. KIT-YO10
-
no activity with tamarind xyloglucan, sodium arginate, carboxymethylcellulose, low-melting point agarose, gellan gum, xylan, carrageenan, and laminaran
-
-
?
additional information
?
-
-
the enzyme shows requirement of four mannose residues for hydrolysis, and is also capable of catalyzing transglycosylation reactions
-
-
?
additional information
?
-
requires at least five sugar moieties for effective catalytic activity, no substrate: yeast mannan
-
-
?
additional information
?
-
no activity against barley beta-glucan, birchwood xylan, and low viscosity carboxymethyl cellulose
-
-
?
additional information
?
-
-
no activity against barley beta-glucan, birchwood xylan, and low viscosity carboxymethyl cellulose
-
-
?
additional information
?
-
the enzyme catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides, such as glucomannans and galactomannans. Protein-ligand interactions from crystal structure analysis, circular dichroism spectroscopy, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides, such as glucomannans and galactomannans. Protein-ligand interactions from crystal structure analysis, circular dichroism spectroscopy, overview
-
-
?
additional information
?
-
the enzyme catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides, such as glucomannans and galactomannans. Protein-ligand interactions from crystal structure analysis, circular dichroism spectroscopy, overview
-
-
?
additional information
?
-
the wild-type enzyme can perform transglycosylation on to saccharide acceptors while the R171K mutant cannot Wild-type and mutant enzyme show the ability to perform alcoholysis reactions with methanol and butanol, forming new beta-linked glycoconjugates. It appears that the wild-type enzyme produces mainly mannobiose conjugates using mannotetetraoses substrate, while in contrast the R171K mutant produces mainly mannotriose conjugates, due to the altered subsite binding
-
-
?
additional information
?
-
-
transglycosylation reaction, Streptomyces: transfer of one mannose unit from oligosaccharides, fenugreek: transfer of oligomannose residues
-
-
?
additional information
?
-
-
transglycosylation reaction, Streptomyces: transfer of one mannose unit from oligosaccharides, fenugreek: transfer of oligomannose residues
-
-
?
additional information
?
-
enzyme has the ability to bind soluble beta-mannans
-
-
?
additional information
?
-
-
enzyme has the ability to bind soluble beta-mannans
-
-
?
additional information
?
-
enzyme hydrolyzes homopolysaccharides such as codium mannan, Porphyra mannan, coffee mannan, and coconut mannan, to form mainly mannobiose and mannotriose in addition to minor sugars, such as mannose, mannotetraose, and mannopentaose
-
-
?
additional information
?
-
-
enzyme hydrolyzes homopolysaccharides such as codium mannan, Porphyra mannan, coffee mannan, and coconut mannan, to form mainly mannobiose and mannotriose in addition to minor sugars, such as mannose, mannotetraose, and mannopentaose
-
-
?
additional information
?
-
enzyme has the ability to bind soluble beta-mannans
-
-
?
additional information
?
-
enzyme hydrolyzes homopolysaccharides such as codium mannan, Porphyra mannan, coffee mannan, and coconut mannan, to form mainly mannobiose and mannotriose in addition to minor sugars, such as mannose, mannotetraose, and mannopentaose
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
beta-galactomannan + H2O
mannobiose + mannotriose + mannotetraose
-
the catalytic efficiency of the enzyme is 6.8fold higher toward galactomannan from locust bean gum, than toward galactomannan from guar gum, but similar toward galactomannan from locust bean gum and glucomannan from konjac flour
-
-
?
beta-glucomannan + H2O
mannobiose + mannotriose + mannotetraose
-
the catalytic efficiency of the enzyme is 6.8fold higher toward galactomannan from locust bean gum, than toward galactomannan from guar gum, but similar toward galactomannan from locust bean gum and glucomannan from konjac flour
-
-
?
guar gum + H2O
mannose + mannobiose + mannotriose
-
-
mannobiose + mannotriose + mannotetraose
?
additional information
?
-
-
the enzyme is involved in release of mannooligosaccharides from spent coffee ground cleaving the backbone at random locations in galactomannan, glucomannan, galactoglucomannan and mannan
-
-
?
additional information
?
-
-
the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides
-
-
?
additional information
?
-
-
the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides
-
-
?
additional information
?
-
-
enzyme is active in hydrolyzing the beta-mannan-rich cell wall of soybean seeds
-
-
?
additional information
?
-
-
the enzyme hydrolyzes high-molecular weight polysaccharides with beta-1,4-glycosidic bonds
-
-
?
additional information
?
-
the native wild-type enzyme shows bifunctional activity as both an endo-glucanase and an endo-mannanase, substrate specificity, overview
-
-
?
additional information
?
-
-
the native wild-type enzyme shows bifunctional activity as both an endo-glucanase and an endo-mannanase, substrate specificity, overview
-
-
?
additional information
?
-
the native wild-type enzyme shows bifunctional activity as both an endo-glucanase and an endo-mannanase, substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the random hydrolysis of beta-1,4-mannosidic linkages in the main chain of mannans, glucomannans and galactomannans, main products are mannobiose, mannotriose, and mannopentaose
-
-
?
additional information
?
-
-
the enzyme catalyzes the random hydrolysis of beta-1,4-mannosidic linkages in the main chain of mannans, glucomannans and galactomannans, main products are mannobiose, mannotriose, and mannopentaose
-
-
?
additional information
?
-
the enzyme catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides, such as glucomannans and galactomannans. Protein-ligand interactions from crystal structure analysis, circular dichroism spectroscopy, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides, such as glucomannans and galactomannans. Protein-ligand interactions from crystal structure analysis, circular dichroism spectroscopy, overview
-
-
?
additional information
?
-
the enzyme catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides, such as glucomannans and galactomannans. Protein-ligand interactions from crystal structure analysis, circular dichroism spectroscopy, overview
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Cu2+
Fe2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
additional information
-
Co2+, Ni2+, Ca2+, and Mg2+ do not affect the activity of the enzyme
additional information
Na+, Li+, NH4+, Ca2+, Mg2+ and Ba2+ have no effect on the recombinant mannanase activity
additional information
not affected by Mg2+, Ca2+, Ni2+, and Cd2+
additional information
Paenibacillus sp. HY-8
-
the stimulatory or inhibitory effect of divalent cations (each 1 mM) including Ni2+, Zn2+, and Sn2+ on the locust bean gum-degrading activity of the enzyme is negligible
additional information
poor effects by Na+, K+, Ag+, Li+, Ca2+, Ni2+ and EDTA at 1 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
abscisic acid
-
presence of exogenous abscisic acid provokes a delay in the cellular disassembly of the endosperm and disappearance of endo-beta-mannanase in the tissue, resulting in delayed galactomannan degradation
SDS
-
the enzyme shows about 45% activity in the presence of 10% (w/v) SDS
additional information
-
the purified recombinant enzyme has a strong resistance to SDS and Ag+ and proteases pepsin and trypsin
-
additional information
-
not inhibitory: EDTA, phenyl methyl sulfonyl fluoride, 1,10-phenanthroline
-
additional information
-
EDTA does not affect the activity of the enzyme
-
additional information
enzymatic activity is not significantly affected by ions such as Ca2+, Cr3+, Co2+, Zn2+, Na+, K+, and Mg2+
-
additional information
EDTA has no effect on enzyme activity
-
additional information
Reinekea sp. KIT-YO10
-
Ca2+, Mg2+, Mn2+, Fe2+, Ni2+, and Zn2+ have either no effect or a slightly inhibitory effect
-
additional information
-
not influenced by Triton X-100 and Tween-20 (10% (v/v)
-
additional information
presence of Ca2+, Na+, Mg2+, Mn2+, urea, and EDTA does not affect catalytic activity
-
additional information
-
presence of Ca2+, Na+, Mg2+, Mn2+, urea, and EDTA does not affect catalytic activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetone
-
activates the wild-type enzyme and mutant Man5DELTACBM at 40-60% v/v, no effect on mutant Man5DELTACL
additional information
-
an assembly of ManB with mini-CbpA, which contains a carbohydrate-binding module that provides proximity to insoluble substrates, increases the activity toward galactomannan from locust bean gum and guar gum 1.7- and 2.0fold over those without mini-CbpA
-
SDS
-
the wild-type enzyme slightly at 0.5-1.0% v/v, inhibits the mutant enzymes
Sodium azide
hydrolysis of locust bean gum is enhanced by approximately 1.45fold in poresence of sodium azide
Triton X-100
-
activates the wild-type enzyme slightly at 0.5% v/v, inhibits the mutant enzymes
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Enteritis
Beneficial effect of beta-mannanase feed enzyme on performance of chicks challenged with Eimerla sp. and Clostridium perfringens.
Plant Diseases
From structure to function: insights into the catalytic substrate specificity and thermostability displayed by Bacillus subtilis mannanase BCman.
Rhinitis, Allergic, Seasonal
Tomato endo beta-mannanase: A candidate of potential tomato allergen protein detected with human monoclonal antibody established from a patient suffered from Japanese cedar pollinosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.25
4-methylumbelliferyl mannotrioside
pH 40°C, pH 4.5, wild-type enzyme
0.46
4-methylumbelliferyl mannotrioside
pH 40°C, pH 4.5, mutant enzyme R171K
0.592
locust bean gum
-
pH and temperature not specified in the publication
-
1.6
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
1.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
wild-type, pH 5.5, 37°C
2.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
2.9
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
pH 5.5, 37°C
0.6
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
wild-type, pH 5.5, 37°C
1
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
1.3
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
1.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
pH 5.5, 37°C
additional information
carob galactomannan
Km value 2.22 mg/ml, pH 5.0, 60°C
-
additional information
carob galactomannan
-
Km value 2.22 mg/ml, pH 5.0, 60°C
-
additional information
konjac glucomannan
Km value 3.22 mg/ml, pH 5.0, 60°C
-
additional information
konjac glucomannan
-
Km value 3.22 mg/ml, pH 5.0, 60°C
-
additional information
konjac glucomannan
Km value 4.7 mg/ml, pH 5.4, 70°C
-
additional information
konjac glucomannan
-
Km value 4.7 mg/ml, pH 5.4, 70°C
-
additional information
additional information
-
copra beta-mannan: 2.0 mg/ml, locust bean beta-mannan: 3.8 mg/ml, konjak beta-mannan: 7.7 mg/ml, carob galactomannan: 0.9 mg/ml
-
additional information
additional information
apparent Km values of the mannanase for locust bean gum, glucomannan, glactomannan and mannan are 3, 2.3, 1.6 and 0.54 mg/ml, respectively
-
additional information
additional information
-
apparent Km values of the mannanase for locust bean gum, guar gum and konjac powder are 7.6, 10.5 and 27.4 mg/ml, respectively
-
additional information
additional information
Km value for locust bean gum at pH 2.4, 50°C is 0.93 mg/ml
-
additional information
additional information
-
Km value for locust bean gum at pH 2.4, 50°C is 0.93 mg/ml
-
additional information
additional information
Km value is 0.16 mg/ml for locust-bean galactomannan
-
additional information
additional information
-
Km value is 0.16 mg/ml for locust-bean galactomannan
-
additional information
additional information
-
Km value for konjac flour is 7.5 mg/ml, for locust bean gum 11.67 mg/ml
-
additional information
additional information
Km value for konjac glucomannan 0.6 mg/ml
-
additional information
additional information
-
Km value for konjac glucomannan 0.6 mg/ml
-
additional information
additional information
Km values are 14.9 mg/ml, 17.5 mg/ml, and 15.2 mg/ml for glucomannan, locust bean gum and beta-D-mannan, respectively
-
additional information
additional information
-
Km values are 14.9 mg/ml, 17.5 mg/ml, and 15.2 mg/ml for glucomannan, locust bean gum and beta-D-mannan, respectively
-
additional information
additional information
Km values for konjac glucomannan of low viscosity, locust bean gum galactomannan, carob galactomannan of low viscosity, and 1,4-beta-D-mannan from carob are 0.6 mg/ml, 2.0 mg/ml, 2.2 mg/ml and 1.5 mg/ml, respectively
-
additional information
additional information
-
Km values for konjac glucomannan of low viscosity, locust bean gum galactomannan, carob galactomannan of low viscosity, and 1,4-beta-D-mannan from carob are 0.6 mg/ml, 2.0 mg/ml, 2.2 mg/ml and 1.5 mg/ml, respectively
-
additional information
additional information
-
Km values for locust bean gum, guar gum, and copra mannan, are 0.11, 0.28, and 0.33 mg/ml, respectively
-
additional information
additional information
kinetics of recombinant chimeric enzymes, overview
-
additional information
additional information
-
Km is 2.074 mg/ml with guar gum for the recombinant enzyme at pH 5.5 and 30°C
-
additional information
additional information
Km of the recombinant enzyme is 7.8 mg/ml for locust bean gum, pH 4.5, 50°C
-
additional information
additional information
-
Km values of the recombinant enzyme are 3.78 mg/ml for locust bean gum, and 7.75 mg/ml for guar gum
-
additional information
additional information
-
Km values with ocust bean gum are 0.9 mg/ml for wild-type enzyme, 0.8 mg/ml for mutant Man5DELTACBM, and 1.1 mg/ml for mutant Man5DELTACL
-
additional information
additional information
-
Michaelis-Menten kinetics, Km values for locust bean gum, konjac mannan, and guar gum are 7.6 mg/ml, 2.1 mg/ml, and 2.3 mg/ml, respectively, pH 4.0, 80°C
-
additional information
additional information
-
recombinant enzyme, Km for locust bean gum is 0.83 ± 0.2 mg/ml, pH 4.0, 80°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1828
low-viscosity locust bean galactomannan
-
at pH 6.0 and 37°C
-
0.01
4-methylumbelliferyl mannotrioside
pH 40°C, pH 4.5, mutant enzyme R171K
0.03
4-methylumbelliferyl mannotrioside
pH 40°C, pH 4.5, wild-type enzyme
2.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
67
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
pH 5.5, 37°C
98
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
112
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
wild-type, pH 5.5, 37°C
117
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
134
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
wild-type, pH 5.5, 37°C
148
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
193
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
pH 5.5, 37°C
additional information
additional information
turnover numbers are 61.2 per s, substrate locust bean gum, wild-type, 75.1 per s, konjac flour, wild-type, 11 per s, ivory nut mannan, wild-type, 1.97 per s, locust bean gum, mutant E167A, 26.5 per s, locust bean gum, mutant H1A/H23A, respectively, at 37°C, pH 7.0
-
additional information
additional information
-
turnover numbers are 61.2 per s, substrate locust bean gum, wild-type, 75.1 per s, konjac flour, wild-type, 11 per s, ivory nut mannan, wild-type, 1.97 per s, locust bean gum, mutant E167A, 26.5 per s, locust bean gum, mutant H1A/H23A, respectively, at 37°C, pH 7.0
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
4-methylumbelliferyl mannotrioside
pH 40°C, pH 4.5, mutant enzyme R171K
0.12
4-methylumbelliferyl mannotrioside
pH 40°C, pH 4.5, wild-type enzyme
23
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
pH 5.5, 37°C
27
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
36
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
61
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
wild-type, pH 5.5, 37°C
109
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
pH 5.5, 37°C
115
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
118
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37°C
215
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
wild-type, pH 5.5, 37°C
additional information
carob galactomannan
kcat/Km value 8022 ml/mg/s, pH 5.0, 60°C
-
additional information
carob galactomannan
-
kcat/Km value 8022 ml/mg/s, pH 5.0, 60°C
-
additional information
konjac glucomannan
kcat/Km value 8855 ml/mg/s, pH 5.0, 60°C
-
additional information
konjac glucomannan
-
kcat/Km value 8855 ml/mg/s, pH 5.0, 60°C
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10760
-
purified recombinant enzyme, pH 7.0, 55°C, substrate locust bean gum
1703
-
purified recombinant enzyme, substrate locust bean gum, pH 4.0, 80°C
215
225.4
-
isozyme MAN II, after 49fold purification with Phenyl Sepharose chromatography
420.9
-
purified recombinant enzyme, locust bean gum as substrate, pH 4.0, 80°C
45.7
-
isozyme MAN I, after 9.9fold purification with DEAE Sepharose chromatography
471
-
isozyme MAN I, after 102.4fold purification with Phenyl Sepharose chromatography
56.7
-
isozyme MAN II, after 12.3fold purification with DEAE Sepharose chromatography
additional information
additional information
-
recombinant enzyme in Yarrowia lipolytica is produced with an activity of 183.5 U/ml and 0.23 mg protein/ml
additional information
-
1638 A550/min/mg optical path 1cm,isozyme MAN I, OBR-LBG
additional information
-
1763 A550/min/mg optical path 1cm, isozyme MAN II, OBR-LBG
additional information
-
no activity against 4-nitrophenyl-alpha and -beta-mannopyranosides
additional information
-
84.4 U/ml of recombinant enzyme in the culture supernatant of Pichia pastoris, pH 4.0, 80°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
4.8
5.2
5.4
5.5
6.5
6.9
7.1
7.5
7.6
9.5
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 7
2 - 9
-
recombinant enzyme, over 20% of maximal activity at pH 2.0 and pH 9.0
3 - 11
-
about 45% activity at pH 3.0, about 60% activity at pH 4.0, about 90% activity at pH 5.0, 100% activity at pH 6.0, about 85% activity at pH 7.0, about 70% activity at pH 8.0, about 65% activity at pH 9.0, about 55% activity at pH 10.0, about 45% activity at pH 11.0
3 - 8
3.5 - 8
-
the immobilized enzyme exhibits more than 50% activity between pH 3.5 and 8.0
4 - 6.5
4 - 8
-
95% activity at pH 5.0 and 75% activity at pH 4.0, pH 6.0 and pH 7.0, 50% at pH 7.5 and pH 8.0
4 - 9
4.8 - 9.1
recombinant enzyme, more than 80% of the maximum activity at pH 4.8-7.8, the enzyme activity drops rapidly when at below pH 4.8 or above pH 9.1
5 - 11
-
more than 50% activity is retained at pH range 5.0-10.0, while there are 32.5% and 34.1% of relative activity at pH 6.0 and 11.0, respectively
5 - 8
additional information
2 - 7
activity range, recombinant chimeric enzymes, profiles overview
2 - 7
-
more than 80% of enzyme activity is retained in the pH range 2.0-7.0
3 - 8
-
more than 60% activity between pH 3.0 and 8.0, no activity at pH 10.0
4 - 6.5
-
the free enzyme exhibits more than 50% activity between pH 4.0 and 6.5
4 - 9
-
activity range, wild-type enzyme, optimum at pH 5.0, 45% of maximal activity at pH 9.0
4 - 9
more than 77% of the maximal activity in the pH range of pH 4.0 to pH 7.0
5 - 8
-
about 30% activity at pH 4.0, about 90% activity at pH 5.0, 100% activity at pH 6.0, about 90% activity at pH 7.0, about 70% activity at pH 8.0, about 20% activity at pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
40
45
50
50 - 60
55
60
60 - 70
65
70
80
additional information
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 60
the enzyme shows 20-40% of its maximum activity at 0-4°C and has its optimum at 30°C, about 10% of maximal activity at 50-60°C, inactivation at 70°C, profile overview
10 - 50
-
approximately 70% between 10°C and 20°C, 60% activity at 40°C, 30% activity at 50°C
10 - 80
activity range, recombinant chimeric enzymes, profiles overview
30 - 70
30 - 80
30 - 90
40 - 60
40 - 70
40°C: about 45% of maximal activity, 70°C: about 55% of maximal activity
40 - 80
40 - 90
-
recombinant enzyme, over 20% of maximal activity within this range
45 - 60
additional information
30 - 70
-
the purified enzyme is highly active (more than 50% activity) between 30 and 70°C
30 - 80
-
30°C: about 25% of maximal activity, 80°C: about 30% of maximal activity
40 - 60
-
more than 80% activity between 40 and 60°C, less than 10% activity at 65°C
40 - 80
recombinant enzyme, over 80% of maximal activity within this range
40 - 80
about 40% activity at 40°C, about 65% activity at 50°C, 100% activity at 60°C, about 90% activity at 70°C, about 25% activity at 80°C
45 - 60
-
about 60% activity at 45°C, about 80% activity at 50°C, 100% activity at 55°C, about 80% activity at 60°C, about 20% activity at 65°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6
5.5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
member of glycosyl hydrolase family 5
UniProt
brenda
isolated from soil sample of Heilongjiang Liangshui National Nature Reserve
UniProt
brenda
induced by growth on konjac powder as carbon source at 50°C
-
-
brenda
bifunctional endo-1,4-beta-mannanase/endoglucanase, EC 3.2.1.78/EC 3.2.1.4, respectively
UniProt
brenda
bifunctional endo-1,4-beta-mannanase/endoglucanase, EC 3.2.1.78/EC 3.2.1.4, respectively
UniProt
brenda
enzyme belongs to glycosyl hydrolase family 26. Protein additionally contains a glycosyl hydroxylase family 44 catalytic domain, a fibronectin domain type 3, and a cellulose-binding module type 3
-
-
brenda
enzyme belongs to glycosyl hydrolase family 26. Protein additionally contains a glycosyl hydroxylase family 44 catalytic domain, a fibronectin domain type 3, and a cellulose-binding module type 3
-
-
brenda
sequence consists of a carbohydrate binding module belonging to family 6 and a family 26 catalytic domain
UniProt
brenda
sequence consists of a carbohydrate binding module belonging to family 6 and a family 26 catalytic domain
UniProt
brenda
strain IMI 385708, formerly Thermomyces lanuginosus strain IMI 158749
-
-
brenda
isolated from soil sample of Heilongjiang Liangshui National Nature Reserve
UniProt
brenda
closely related to Caldicellulosiruptor sp. Rt8B.4
UniProt
brenda
isolated from the Kubiki oil reservoir in Niigata (Japan)
UniProt
brenda
isolated from the Kubiki oil reservoir in Niigata (Japan)
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
isoform Man4a is expressed in the fruit cell wall at all ripening stages, but it is not active during the initial green stage. This is not due to the presence of inhibitors of its activity, nor due to changes in its mRNA sequence
brenda
-
high degree of enzyme expression during germination facilitates radicle protrusion through the surrounding endosperm by weakeing it in the region close to the radicle tip
brenda
additional information
solid state fermentation on medium containing microcrystalline cellulose
brenda
additional information
-
solid state fermentation on medium containing microcrystalline cellulose
brenda
additional information
-
solid state fermentation on medium containing microcrystalline cellulose
-
brenda
additional information
the temperature range for growth is 47-88°C with an optimum at 80°C
brenda
additional information
-
the temperature range for growth is 47-88°C with an optimum at 80°C
brenda
additional information
-
the temperature range for growth is 47-88°C with an optimum at 80°C
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
transient expression in onion epidermal cells of endo-beta-mannanase trancripts fused to green fluorescent protein results in the expressed enzyme being localized to the cell walls. This occurs initially during ripening in the skin and outer pericarp of the fruit, and later in the skin and throughout the pericarp
brenda
-
the enzyme contains a putative 19-residue signal peptide at the N-terminus
-
brenda
-
the enzyme contains a putative 19-residue signal peptide at the N-terminus
-
-
brenda
additional information
the enzyme contains a putative 18-residue signal peptide
-
brenda
additional information
-
the enzyme contains a putative 18-residue signal peptide
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
the enzyme belongs to the glycosyl hydrolae famiyl 5, GH5
evolution
the enzyme belongs to the glycosyl hydrolase family 5, GH5
evolution
the enzyme belongs to the glycosyl hydrolase family 5, GH5
evolution
the enzyme belongs to the glycosyl hydrolase family 5, GH5, structure comparisons, the overall fold of the enzyme is strongly conserved, overview. The enzyme displays the typical (beta/alpha)8-barrel fold and a unique structural arrangement of three surface loops that stretch over the active centre, promoting an altered topography of the binding cleft
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5, structure comparisons, the overall fold of the enzyme is strongly conserved, overview. The enzyme displays the typical (beta/alpha)8-barrel fold and a unique structural arrangement of three surface loops that stretch over the active centre, promoting an altered topography of the binding cleft
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
-
metabolism
key enzyme for hydrolyzing mannan, a major constituent of hemicellulose
metabolism
the enzyme is involved in the hydrolysis of plant cell wall mannans and heteromannans
metabolism
-
key enzyme for hydrolyzing mannan, a major constituent of hemicellulose
-
physiological function
when endo-beta-mannanase activity is much reduced by RNAi and antisense RNA strategies, their firmness is higher compared to those of control fruits at the turning and orange-color stages, but at the red-ripe stage firmness is similar between the two fruit-types
physiological function
enzyme strongly binds to ivory nut mannan, Avicel, chitosan, and chitin, but does not attach to curdlan, insoluble oat spelt xylan, lignin, or poly(3-hydroxybutyrate)
physiological function
germination time in T-DNA insertion mutant almost doubles compared to wild-type. Enzyme is important for the germination of Arabidopsis thaliana seeds by facilitating the hydrolysis of the mannan-rich endosperm cell walls
physiological function
T-DNA insertion mutant germinates later than the wild type. Enzyme is important for the germination of Arabidopsis thaliana seeds by facilitating the hydrolysis of the mannan-rich endosperm cell walls
physiological function
the enzyme beta-mannanase is responsible for the cleavage of beta-1,4-linked internal linkages of the mannan polymer to produce new chain ends
physiological function
-
strain is not an effective producer of mannan-degrading enzymes. Oat spelt xylan is the best inducer of mannanase, feruloyl esterase, arabinofuranosidase, glucosidase and acetyl xylan esterase
physiological function
-
enzyme strongly binds to ivory nut mannan, Avicel, chitosan, and chitin, but does not attach to curdlan, insoluble oat spelt xylan, lignin, or poly(3-hydroxybutyrate)
-
physiological function
-
strain is not an effective producer of mannan-degrading enzymes. Oat spelt xylan is the best inducer of mannanase, feruloyl esterase, arabinofuranosidase, glucosidase and acetyl xylan esterase
-
physiological function
-
the enzyme beta-mannanase is responsible for the cleavage of beta-1,4-linked internal linkages of the mannan polymer to produce new chain ends
-
additional information
-
catalytic residues are Glu181 as catalytic acid/base and Glu288 as nucleophile, molecular docking study with different manno-configured ligands from mannobiose to mannohexose as well as galactomannan. The ability to accommodate larger ligand molecules in the active site of CtManT is probably due to the long loops enclosing the active site that provides the depth of the cavity, structure overview
additional information
tertiary structure, active site and substrate binding site structures analysis, detailed overview. Two tryptophan residues that provide the hydrophobic stacking of the +1 subsite Trp125 and Trp271,is 9.5 A, making bulkier branched substrates difficult to accommodate
additional information
-
tertiary structure, active site and substrate binding site structures analysis, detailed overview. Two tryptophan residues that provide the hydrophobic stacking of the +1 subsite Trp125 and Trp271,is 9.5 A, making bulkier branched substrates difficult to accommodate
additional information
the enzyme has an extended loop that alters topography of the active site, structural and mutational analyses, overview. The extended loop is linked to the cold-adapted enzymatic activity, structure of mannose-recognition subsites. Glu181 and Glu312 are highly conserved catalytic residues, Glu181 is the catalytic acid/base, and Glu312 is the nucleophile. Trp341, which is located in the vicinity of the catalytic residues, acts as a hydrophobic platform for sugar binding in catalytic site, the enzyme also has a second mannan binding site. Sequence comparisons, overview
additional information
-
the enzyme has an extended loop that alters topography of the active site, structural and mutational analyses, overview. The extended loop is linked to the cold-adapted enzymatic activity, structure of mannose-recognition subsites. Glu181 and Glu312 are highly conserved catalytic residues, Glu181 is the catalytic acid/base, and Glu312 is the nucleophile. Trp341, which is located in the vicinity of the catalytic residues, acts as a hydrophobic platform for sugar binding in catalytic site, the enzyme also has a second mannan binding site. Sequence comparisons, overview
additional information
the enzyme is composed of three distinct domains and shows some level of molecular flexibility in solution, nevertheless it has a preferred conformation, which can be described by the rigid-body modeling procedure, structure analysis. The enzyme contains a linker with a compact structure that occupies a small volume with respect to its large number of amino acids, role of the length and flexibility of the linker on the spatial arrangement of the constitutive domains. The linker can optimize the geometry between the other two domains with respect to the substrate at high temperatures. The hydrodynamic radii of full-length enzyme and single catalytic domain are independent of protein concentration over the range 0.5 to 8 mg/ml at 20°C and pH 6
additional information
-
the enzyme is composed of three distinct domains and shows some level of molecular flexibility in solution, nevertheless it has a preferred conformation, which can be described by the rigid-body modeling procedure, structure analysis. The enzyme contains a linker with a compact structure that occupies a small volume with respect to its large number of amino acids, role of the length and flexibility of the linker on the spatial arrangement of the constitutive domains. The linker can optimize the geometry between the other two domains with respect to the substrate at high temperatures. The hydrodynamic radii of full-length enzyme and single catalytic domain are independent of protein concentration over the range 0.5 to 8 mg/ml at 20°C and pH 6
additional information
the structure of the catalytic domain reveals a canonical (alpha/beta)8-barrel scaffold surrounded by loops and short helices that form the catalytic interface, subsites forming the active-site cleft with residues W134, E198, R200, E235, H283 and W284 are directly involved in glucose binding, structure analysis of full-length enzyme and catalytic domain, overview
additional information
-
the structure of the catalytic domain reveals a canonical (alpha/beta)8-barrel scaffold surrounded by loops and short helices that form the catalytic interface, subsites forming the active-site cleft with residues W134, E198, R200, E235, H283 and W284 are directly involved in glucose binding, structure analysis of full-length enzyme and catalytic domain, overview
additional information
-
tertiary structure, active site and substrate binding site structures analysis, detailed overview. Two tryptophan residues that provide the hydrophobic stacking of the +1 subsite Trp125 and Trp271,is 9.5 A, making bulkier branched substrates difficult to accommodate
-
additional information
-
catalytic residues are Glu181 as catalytic acid/base and Glu288 as nucleophile, molecular docking study with different manno-configured ligands from mannobiose to mannohexose as well as galactomannan. The ability to accommodate larger ligand molecules in the active site of CtManT is probably due to the long loops enclosing the active site that provides the depth of the cavity, structure overview
-
additional information
-
the structure of the catalytic domain reveals a canonical (alpha/beta)8-barrel scaffold surrounded by loops and short helices that form the catalytic interface, subsites forming the active-site cleft with residues W134, E198, R200, E235, H283 and W284 are directly involved in glucose binding, structure analysis of full-length enzyme and catalytic domain, overview
-
additional information
-
the enzyme is composed of three distinct domains and shows some level of molecular flexibility in solution, nevertheless it has a preferred conformation, which can be described by the rigid-body modeling procedure, structure analysis. The enzyme contains a linker with a compact structure that occupies a small volume with respect to its large number of amino acids, role of the length and flexibility of the linker on the spatial arrangement of the constitutive domains. The linker can optimize the geometry between the other two domains with respect to the substrate at high temperatures. The hydrodynamic radii of full-length enzyme and single catalytic domain are independent of protein concentration over the range 0.5 to 8 mg/ml at 20°C and pH 6
-
Show AA Sequence and Transmembrane Helices (8658 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
113000
x * 113000, deduced from gene sequence, upon expression in Escherichia coli, two fragments of 45000 and 50000 Da
33000
35500
-
x * 35500, recombinant His6-tagged enzyme, SDS-PAGE, x * 33000, about, enzyme without signal sequence, sequence calculation
37000
38000
39000
39500
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE
40000
41000
41389
x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
43000
44000
45000
48000
x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
50000
53000
55000
56000
58000
60000
63000
65000
70000
72000
x * 72000, recombinant enzyme, SDS-PAGE, x * 43000, about, sequence calculation of the mature enzyme
73000
73588
1 * 76309, calculated including signal peptide, 1 * 73588, calculated, mature protein, 1 * 73000, SDS-PAGE
76309
1 * 76309, calculated including signal peptide, 1 * 73588, calculated, mature protein, 1 * 73000, SDS-PAGE
33000
-
x * 35500, recombinant His6-tagged enzyme, SDS-PAGE, x * 33000, about, enzyme without signal sequence, sequence calculation
38000
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
39000
x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
40000
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE
41000
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
43000
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE
43000
x * 72000, recombinant enzyme, SDS-PAGE, x * 43000, about, sequence calculation of the mature enzyme
45000
x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
50000
-
SDS-PAGE, a stable fragment corresponding to about 460 residues and comprising the catalytic domain and 50 to 60 extra residues at the C-terminus
50000
x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
55000
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
58000
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
60000
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
63000
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
73000
1 * 76309, calculated including signal peptide, 1 * 73588, calculated, mature protein, 1 * 73000, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
?
-
x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
-
?
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE
?
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE
-
?
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
?
-
x * 63000, glycosylated recombinant wild-type enzyme, SDS-PAGE, x * 58000, glycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 41000, glycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE, x * 60000, deglycosylated recombinant wild-type enzyme, SDS-PAGE, x * 55000, deglycosylated mutant lacking the CBM1 domain, SDS-PAGE, x * 38000, deglycosylated mutant lacking the CBM1 domain and linker region, SDS-PAGE
-
?
x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
?
-
x * 35500, recombinant His6-tagged enzyme, SDS-PAGE, x * 33000, about, enzyme without signal sequence, sequence calculation
?
x * 72000, recombinant enzyme, SDS-PAGE, x * 43000, about, sequence calculation of the mature enzyme
?
-
x * 72000, recombinant enzyme, SDS-PAGE, x * 43000, about, sequence calculation of the mature enzyme
-
?
x * 113000, deduced from gene sequence, upon expression in Escherichia coli, two fragments of 45000 and 50000 Da
?
x * 60000, SDS-PAGE of recombinant protein, x * 50605, calculated
monomer
1 * 76309, calculated including signal peptide, 1 * 73588, calculated, mature protein, 1 * 73000, SDS-PAGE
monomer
-
1 * 76309, calculated including signal peptide, 1 * 73588, calculated, mature protein, 1 * 73000, SDS-PAGE
-
additional information
-
the three-dimensional enzyme structure contains a (beta/alpha)8 TIM barrel folding motif
additional information
-
the three-dimensional enzyme structure contains a (beta/alpha)8 TIM barrel folding motif
-
additional information
-
the multimodular enzyme consists of a family 1 carbohydrate-binding module (CBM1), a Thr/Ser-rich linker region, and a catalytic domain
additional information
-
the multimodular enzyme consists of a family 1 carbohydrate-binding module (CBM1), a Thr/Ser-rich linker region, and a catalytic domain
-
additional information
-
Trp360 is critical in substrate binding at -1 subsite, Tyr285 works as nucleophile catalyst, Trp217 and Trp162 are important for the activity against mannooligosaccharides but less important for activity against polysaccharides
additional information
the enzyme adopts a TIM (beta/alpha)8-barrel fold
additional information
-
the enzyme adopts a TIM (beta/alpha)8-barrel fold
additional information
the enzyme adopts the (beta/alpha)8-barrel fold
additional information
-
the enzyme adopts the (beta/alpha)8-barrel fold
additional information
-
the enzyme adopts the (beta/alpha)8-barrel fold
-
additional information
C-terminal domain of 550 amino acid residues with homology to glycosidase family 26
additional information
the enzyme shows some level of molecular flexibility in solution and is composed of three distinct domains, a GH5 catalytic domain (373 amino acid residues) and a carbohydrate-binding domain (172 amino acid residues) connected through a linker (102 amino acid residues). Secondary structure, overview
additional information
-
the enzyme shows some level of molecular flexibility in solution and is composed of three distinct domains, a GH5 catalytic domain (373 amino acid residues) and a carbohydrate-binding domain (172 amino acid residues) connected through a linker (102 amino acid residues). Secondary structure, overview
additional information
the two-domain enzyme encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, structure analysis and comparisons, overview
additional information
-
the two-domain enzyme encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, structure analysis and comparisons, overview
additional information
-
the two-domain enzyme encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, structure analysis and comparisons, overview
-
additional information
-
the enzyme shows some level of molecular flexibility in solution and is composed of three distinct domains, a GH5 catalytic domain (373 amino acid residues) and a carbohydrate-binding domain (172 amino acid residues) connected through a linker (102 amino acid residues). Secondary structure, overview
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
treatment with PNGaseF results in a shift to 41000 Da, both for native and recombinant protein
glycoprotein
-
treatment with PNGaseF results in a shift to 41000 Da, both for native and recombinant protein
-
glycoprotein
-
the enzyme contains two putative N-glycosylation sites and no O-glycosylation site, deglycosylation by endo-beta-N-acetylglucosaminidase H
glycoprotein
-
the enzyme contains two putative N-glycosylation sites and no O-glycosylation site, deglycosylation by endo-beta-N-acetylglucosaminidase H
-
glycoprotein
treatment by endoglycosidase H decreases molecular mass to 46000 Da
glycoprotein
treatment by endoglycosidase H decreases molecular mass to 51000 Da
glycoprotein
-
one potential N-glycosylation site, Asn98-Phe99-Thr100, the enzyme is deglycosylated by endo-beta-N-acetylglucosaminidase H. The Thr/Ser-rich linker region has numerous putative O-glycosylation sites
glycoprotein
-
treatment by endoglycosidase H decreases molecular mass to 51000 Da
-
glycoprotein
-
treatment by endoglycosidase H decreases molecular mass to 46000 Da
-
glycoprotein
-
one potential N-glycosylation site, Asn98-Phe99-Thr100, the enzyme is deglycosylated by endo-beta-N-acetylglucosaminidase H. The Thr/Ser-rich linker region has numerous putative O-glycosylation sites
-
glycoprotein
-
deglycosylation by endo-beta-N-acetylglucosaminidase H
-
glycoprotein
treatment with Endo H leads to 30% loss of enzymic activity and a reduction in molecular weight by about 9 kDa
glycoprotein
-
the enzyme has three N-glycosylation sites (N173, N242, N313) and two O-glycosylation sites (S5, S334)
glycoprotein
Aspergillus sulphureus CGMCC0608
-
the enzyme has three N-glycosylation sites (N173, N242, N313) and two O-glycosylation sites (S5, S334)
-
glycoprotein
the enzyme shows two different N-glycosylation sites. The first site Asn63 contains two linked N-acetylglucosamine residues. This glycosylation may have a structural role in stabilizing structural elements, as there are hydrogen bonds between the glucosamine residues and Ile67 and Leu71, which both belong to a very long loop (residues 64-84), and Val136 located on helix 4. The other site Asn319 is not fully occupied, suggesting disorder or perhaps different populations of glycosylation
glycoprotein
-
the enzyme shows two different N-glycosylation sites. The first site Asn63 contains two linked N-acetylglucosamine residues. This glycosylation may have a structural role in stabilizing structural elements, as there are hydrogen bonds between the glucosamine residues and Ile67 and Leu71, which both belong to a very long loop (residues 64-84), and Val136 located on helix 4. The other site Asn319 is not fully occupied, suggesting disorder or perhaps different populations of glycosylation
-
glycoprotein
treatment with EndoH leads to a mass reduction of 7000 Da
proteolytic modification
sequence contains a N-terminal signal peptide of 17 amino acids
proteolytic modification
sequence contains a N-terminal signal peptide of 24 amino acids
proteolytic modification
-
sequence contains a N-terminal signal peptide of 24 amino acids
-
proteolytic modification
-
sequence contains a signal peptide of 17 amino acids
proteolytic modification
sequence contains a secretory signal peptide
proteolytic modification
amino acid sequence contains a signal peptide cleavage site between residues 21-22, targeting sequence for cell wall
proteolytic modification
sequence contains a signal peptide of 26 amino acids
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native and selenomethionyl enzyme, to 1.9 and 1.99 A resolution, respectively
-
to 1.45 A resolution, crystal shows a typical (beta/alpha)8 folding type. The catalytic acid/base Glu167 and nucleophile Glu266 are positioned on the beta4 and beta7 strands, respectively
enzyme in apoform and in complex with mannopentaose, the precipitant solution contains 25% w/v PEG 3350, 0.1 M Tris-HCl, pH 8.5, X-ray diffraction structure determination and analysis, modelling
hanging drop vapor diffusion method, using 1 M ammonium citrate, 15% (v/v) isopropanol, and 0.1M Tris-HCl (pH 8.5)
both native protein and selenomethionyl derivative, enzyme expressed in Pichia pastoris
-
hanging drop vapour diffusion method, mixing of 6.5 mg/ml protein in 20 mM Tris-HCl, pH 7.6, with reservoir solution containing 0.1 M magnesium chloride, 0.1 M sodium acetate pH 4.5, 23% w/v PEG 3350, 20°C, method optimization, X-ray diffraction structure determination and analysis at 1.40 A resolution, molecular replacement
molecular dynamic simulation of wild-type and mutant lacking the C-terminal amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein
crystallization of catalytic domain. Crystals from conditions with phosphate or citrate salts as precipitant belong to space group P212121, resolution to 1.4 A, while a crystal from a condition with ethanol as precipitant belongs to space group I212121, resolution to 1.45 A
purified recombinant His-tagged full-length enzyme and catalytic domain, X-ray diffraction structure determination and analysis by dynamic light scattering and small-angle X-ray scattering. molecular modelling
purified recombinant isolated His-tagged catalytic domain in apoform and complexed with iodine, glucose, maltose, and maltose + gycerol, sitting drop vapor diffusion method, mixing of 0.0005 ml of 12 mg/ml protein in 25 mM Tris-HCl, pH 7.5, with 0.0005 ml of precipitant solution containing 0.1 M citrate, pH 5.5, 1 M ammonium phosphate, and 0.2 M sodium chloride, 20°C, soaking of crystals in ligand solutions, X-ray diffraction structure determination and analysis at 1.40-1,92 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C143A
the mutant shows reduced activity compared to the wild type enzyme
N90A
the mutant shows reduced activity compared to the wild type enzyme
W13F
the mutant shows reduced activity compared to the wild type enzyme
Y292A
the mutant shows increased activity with mannotriose and mannotetraose and about 50% reduced activity with mannopentaose and mannohexaose compared to the wild type enzyme
S289W
mutation lowers KM for mannooligosaccharides by 30-45% and increases transglycosylation yield by 50% compared to wild-type
W283S
mutation in subsite +1, mutation results in increase in KM value, reduction in the transglycosylation yield by 30-45% and decrease in activity towards mannans
S289W
-
mutation lowers KM for mannooligosaccharides by 30-45% and increases transglycosylation yield by 50% compared to wild-type
-
W283S
-
mutation in subsite +1, mutation results in increase in KM value, reduction in the transglycosylation yield by 30-45% and decrease in activity towards mannans
-
R171K
the mutant displays retained activity on polymeric galactomannan but reduced activity on oligosaccharides due to an increase of Km. While the wild-type enzyme produces mannobiose as dominant product from mannotetraose, the R171K mutant enzyme produces mannotriose and mannose. The preferred productive binding mode of mannotetraose is shifted from subsite -2 to +2 in the wild-type to subsite -3 to +1 in the R171K mutant. The wild-type enzyme can perform transglycosylation on to saccharide acceptors while the R171K mutant cannot. Wild-type and mutant enzyme show the ability to perform alcoholysis reactions with methanol and butanol, forming new beta-linked glycoconjugates. It appears that the wild-type enzyme produces mainly mannobiose conjugates using mannotetetraoses substrate, while in contrast the R171K mutant produces mainly mannotriose conjugates, due to the altered subsite binding
additional information
additional information
-
generation of two truncated enzyme mutants lacking the family 1 carbohydrate-binding module Man5DELTACBM or the family 1 carbohydrate-binding module and the Thr/Ser-rich linker region, Man5DELTACL, respectively. The mutant enzymes show significantly altered secondary structures compared to the wild-type enzyme, overview. Removal of the family 1 carbohydrate-binding module alone improves the thermostability of the enzyme, but additional removal of the linker region results in worse thermostability. The mutants are less stable in presence of acetone, SDS, Triton X-100, or urea compared to the wild-type enzyme
additional information
-
generation of two truncated enzyme mutants lacking the family 1 carbohydrate-binding module Man5DELTACBM or the family 1 carbohydrate-binding module and the Thr/Ser-rich linker region, Man5DELTACL, respectively. The mutant enzymes show significantly altered secondary structures compared to the wild-type enzyme, overview. Removal of the family 1 carbohydrate-binding module alone improves the thermostability of the enzyme, but additional removal of the linker region results in worse thermostability. The mutants are less stable in presence of acetone, SDS, Triton X-100, or urea compared to the wild-type enzyme
-
additional information
-
gene optimization according to the codon usage bias in Pichia pastoris and synthesis by splicing overlap extension PCR
additional information
construction of a chimeric enzyme of xylanase and mannanase with higher catalytic efficiency and improved properties, the two enzymes are fused together with twelve fusion types
additional information
-
gene optimization according to the codon usage bias in Pichia pastoris and synthesis by splicing overlap extension PCR
-
additional information
-
construction of a chimeric enzyme of xylanase and mannanase with higher catalytic efficiency and improved properties, the two enzymes are fused together with twelve fusion types
-
additional information
optimization of mannanase gene for expression in Pichia pastoris by substitution of 258 nucleotides with their corresponding counterparts according to the codon usage in Pichia pastoris, which has no change on the beta-mannanase amino acid sequence
additional information
-
optimization of mannanase gene for expression in Pichia pastoris by substitution of 258 nucleotides with their corresponding counterparts according to the codon usage in Pichia pastoris, which has no change on the beta-mannanase amino acid sequence
additional information
-
optimization of mannanase gene for expression in Pichia pastoris by substitution of 258 nucleotides with their corresponding counterparts according to the codon usage in Pichia pastoris, which has no change on the beta-mannanase amino acid sequence
-
additional information
mutagenesis of Trp271 at the +1 subsite plays a crucial role in the enhanced transglycosylation activity
additional information
-
mutagenesis of Trp271 at the +1 subsite plays a crucial role in the enhanced transglycosylation activity
additional information
-
mutagenesis of Trp271 at the +1 subsite plays a crucial role in the enhanced transglycosylation activity
-
additional information
deletion of the CBM6 domain increases the enzyme stability while enabling it to retain 80% and 60% of its initial activity after treatment at 80°C and 90°C for 30 min
additional information
-
deletion of the CBM6 domain increases the enzyme stability while enabling it to retain 80% and 60% of its initial activity after treatment at 80°C and 90°C for 30 min
-
additional information
the cultivar Walter displays an inactive enzyme due to the absence of the C-terminal four amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein
additional information
-
the cultivar Walter displays an inactive enzyme due to the absence of the C-terminal four amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein
additional information
mutant MG17 is catalytically inactive, mutant protein is present at wild-type molecular mass
additional information
-
mutant MG17 is catalytically inactive, mutant protein is present at wild-type molecular mass
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 2
-
purified recombinant wild-type enzyme, 37°C, 1 h, 50% activity remaining
731205
1.5 - 11
the enzyme is stable over the pH range 1.5-11.0. The enzyme retains 84 % of its activity at 50°C for 12 h in the pH range 3.5-9.0
750154
11 - 12
purified reocmbinant enzyme, 37°C, 1 h, without substrate, more than 40% of the initial activity remaning
732202
2 - 12
2.2 - 11
purified recombinant chimeric enzymes display similar high pH stability as the wild-type mannanase with over 80% activity in this range, profiles overview
732348
3
-
purified recombinant wild-type enzyme, 37°C, 1 h, 50% activity remaining
731205
3 - 10
-
the enzyme retains more than 80% of the maximum activity after 90 min at 30°C within a pH range of 3.0-10.0
751143
3 - 9
4 - 10
4 - 8
4 - 9
4.5 - 9
Caldicellulosiruptor sp.
-
-
208810
4.5 - 9.5
Paenibacillus sp. HY-8
-
the enzyme maintains over 85 % of its original biocatalytic activity toward locust bean gum after pre-incubation for 1 h from pH 4.5 to 9.5
750157
5 - 10
5 - 9
5 - 9.5
long-term (15 h) pre-exposure to acidic and alkaline conditions (pH 5.0-9.5 at 4°C) does not significantly affect enzymatic function, and at least 65% residual activity is retained
750162
6 - 10
6 - 11.5
-
the enzyme is stable over an alkaline pH range from 6.0 to 11.5, in which more than 55% of the original enzyme activity is retained after 6 h at 30°C. The residual activity declines when the pH values are lower than 5.5 or higher than 11.5, and 20.5% and 25.8% of original activity is retained after pretreatment at pH 5.0 and 12.0, respectively
751481
6 - 9
additional information
3 - 9
-
after 1 h incubation at pH 3.0, 4.0, 5.0, 6.0, 7.0, 8.0 and 9.0, the enzyme retains about 68%, 82%, 93%, 95%, 90%, 68%, and 42% activity, respectively
752074
4 - 10
-
purified recombinant enzyme, 30 min, without substrate, over 80% activity remaining
731967
4 - 9
purified reocmbinant enzyme, 37°C, 1 h, without substrate, more than 86% of the initial activity remaning
732202
5 - 10
the enzyme is stable over a pH range from 5.0 to 10.0 for 1 h, since it retains more than 60% of the initial activity after incubation without substrate at 37°C for 1 h
749657
5 - 10
-
after incubation for 90 min at 30°C at pHs ranging from 5.0 to 10.0, the enzyme retains more than 75% of its maximal activity
749688
6 - 10
retains more than 75% of maximum activity after 1 h incubation
695697
6 - 9
-
the enzyme is highly stable with 100% activity remaining after 1 h within a pH range of 6.0-9.0 and about 80-90% activity remaining after 1 h within a pH range of 4.0-5.0. No residual activity is detected at pH 3.0
752077
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 50
the enzyme retains 100% activity after 30 min at 10-50°C, at 60°C the activity drops to about 50%
10 - 80
varying residual activities of recombinant chimeric enzymes, overview
100
-
the enzyme shows 30% and 60% of the maximal activity after an incubation at 100°C for 120 min and 80°C for 60 min, respectively
20 - 70
the enzyme shows good stability along 20-65°C and retains more than 60% of its activity for up to 1 h at 60°C. The enzyme has a half-life of 26xa0min at 70°C
30 - 60
the enzyme is stable up to 60°C for 1 h. At 70°C, the activity drops to less than 40% after 1h
30 - 90
-
purified recombinant wild-type enzyme, pH 5.0, 1 h, more than 45% of maximal activity at 50-80°C and over 30% activity at 90°C
35 - 45
-
the relatively high thermostability is retained after 1 h in the temperature range of 35-45°C and the stability rapidly decreases above 60°C
37
37 - 60
Paenibacillus sp. HY-8
-
the enzyme shows 100%, 80%, 50%, 20% and no activity after 1 h at 37°C, 45°C, 50°C, 55°C, and 60°C, respectively
40
40 - 60
45
45 - 55
below 45°C, the recombinant enzyme remains stable with 95% glycosyl hydrolase activity for 1 h, but quickly loses this function above 55°C
50
50 - 85
the enzyme retains 60% activity at 80°C for 2 h and almost full enzyme activity remains after 4 h at 50°C. The enzyme retains 52 % enzyme activity at 85°C after 15 min
55
60
65
70
70 - 85
the free enzyme retains 42.5% residual activity after 35 min at 70-75°C. The half-lives of the free enzyme at 70, 75, 80 and 85°C are 138.6, 77, 24.7 and 25.6 min, respectively
70 - 90
-
after incubation at 70°C for 120 min, the enzyme activity toward glucomannan decreases to 50% of the maximal activity at 30°C. After incubation at 70°C for 120 min, the activity of the enzyme toward glucomannan decreases to 50% of the maximal activity at 30°C. The activity of the enzyme toward mannohexaose decreases to 73% after incubation at 70°C for 60 min. Further increases of temperature to 80 and 90°C for 60 min result in 70 and 26% of the enzyme activity remaining, respectively
80
85
pH 6.0, the full-length enzyme is completely stable, while the isolated catalytic domain starts to precipitate
90
additional information
40 - 60
the enzyme maintains thermostability with 80% activity remaining at 40°C after 1 h and 60% activity remaining at 50°C after 1 h. When incubated at 60°C without substrate, the enzyme loses activity rapidly (about 25% residual activity after 10 min, no activity after 30 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
40 - 60
-
the enzyme is stable up to 60°C and retains 85% of its activity after 1.0 h of incubation
50
after incubation for 30 min, stable at pH 5-12. After incubation for 24 h, stable at pH 6-9. Half-life about 80 h at pH 6.0
50
purified reocmbinant enzyme, pH 4.5, 90 min, loss of 50% activity
55
-
purified recombinant enzyme, without substrate, stable up to, 90% activity remaning at 55°C after 30 min
60
-
a combination of mannanase with 0.2% sodium benzoate and 30% or 35% sorbitol presents the highest relative activity of about 150% when incubated at 60°C for 4 h, the control retains 63% of the initial activity
60
purified reocmbinant enzyme, pH 4.5, 30 min, complete loss of activity
60
-
purified recombinant His6-tagged enzyme, half-life is approximately 58 h at pH 4.0
70
-
the enzyme exhibits god thermal stability at temperatures up to 70°C
70
-
purified recombinant enzyme, 80% activity remaining after 1 h, inactivation after 2 h
70
1 h, 70% residual activity, truncated protein fragments produced in Escherichia coli, 1 h, 87% residual activity, protein derived from Rhodothermus marinus
90
1 h, 25% residual activity, truncated protein fragments produced in Escherichia coli
additional information
-
glycerol at 30-40%, potassium sorbate/sodium benzoate at 0.2%, and sorbitol at 30-35% enhances enzyme thermostability and activity, overview
additional information
-
the glycosylation status of the enzyme has no effect on the thermostability
additional information
-
removal of the family 1 carbohydrate-binding module alone improves the thermostability of the enzyme, but additional removal of the linker region results in worse thermostability
additional information
the CBM27 accessory domain is critical for thermal stability, it reduces the melting temperature from 100°C to 88°C
additional information
-
the CBM27 accessory domain is critical for thermal stability, it reduces the melting temperature from 100°C to 88°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
although deleting carbohydrate binding module 10 increases the catalytic efficiency, its disruption decreases the pH, solvent and detergent stability of the enzyme
-
enzyme immobilization using cross-linked aggregated form (MB-C) and chitosan magnetic nanocomposites of MB-C leads to 73.2% higher activity (pH 4.0-9.0), up to 95.6% higher stability (pH 3.0-10.0, 9 h incubation at room temperature), up to 15°C higher optimal temperature, higher stability (up to 83%) in the presence of solvents and up to 1.62fold higher deactivation energy, as compared to the free enzyme. Immobilized enzymes are able to repeatedly hydrolyze locust bean gum till 12 cycles
enzyme is rather unstable and steadily loses activity during the purification process. Addition of 0.2% bovine serum albumine stabilizes
the activity of enzyme immobilized onto chitosan coated magnetic nanoparticles is lost 21.4% after 10 cycles of reuse
-
the fused signal sequence of metalloprotease PrtA does not affect the enzymatic properties of the enzyme
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
dimethyl formamide
the enzyme activity remains stable in the presence of 10% (v/v)
dimethyl sulfoxide
the enzyme activity remains stable in the presence of 10% (v/v)
Ethanol
isopropanol
-
the enzyme retains about 65% activity in the presence of 20% (v/v) isopropanol
Methanol
propanol
the enzyme activity remains stable in the presence of 10% (v/v)
additional information
-
the enzyme activity is unaffected by up to 20% (v/v) acetone
Acetone
the enzyme activity remains stable in the presence of 10% (v/v)
Acetone
-
the enzyme retains 100% activity in the presence of 20% (v/v) acetone
Ethanol
the enzyme activity remains stable in the presence of 10% (v/v)
Ethanol
-
the enzyme retains about 85% activity in the presence of 20% (v/v) ethanol
Methanol
the enzyme activity remains stable in the presence of 10% (v/v)
Methanol
-
the enzyme retains about 80% activity in the presence of 20% (v/v) methanol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, a single freeze-thawing cycle results in loss of 80% of activity. Bovine serum albumine stabilizes
4°C, 10 mM HEPES, 4 days, no loss of activity at pH 8.0, 75% loss of activity at pH 6.0
-
cold
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE column chromatography and Sephadex G75 gel filtration
-
ammonium sulfate precipitation, DEAE-cellulose column chromatography and Sephacryl S200 gel filtration
-
ammonium sulfate precipitation, DEAE-Sephadex column chromatography and Sephacryl S-200 gel filtration
-
ammonium sulfate precipitation, DEAE-Sephadex column chromatography, and Sephacryl S-200 gel filtration
-
ammonium sulfate precipitation, DEAE-Sepharose column chromatography and Q-Sepharose column chromatography
-
ammonium sulfate precipitation, HisTrap column chromatography, HiTrap DEAE column chromatography, and Superdex 75 gel filtration
butyl-Toyopearl 650 M column chromatography, DEAE-Toyopearl 650 M column chromatography, Mono Q column chromatography, Mono S column chromatography, Superdex 75 gel filtration, and HisTrap column chromatography
HisTrap column chromatography and Superdex G75 gel filtration
-
native enzyme by ultrafiltration and anion exchange chromatography
nickel-nitrilotriacetic acid agarose column chromatography and HiTrap Q column chromatography
-
recombinant chimeric enzymes from Pichia pastoris strain X33 culture supernatant by ammonium sulfate fractionation and gel filtration
recombinant enzyme
recombinant enzyme 9.7fold from Pichia pastoris strain GS115 culture supernatant to homogeneity by ammonium sulfate fractionation, dialysis, PEG 20000 fractionation, anion exchange chromatography, ultrafiltration, and gel filtration
recombinant extracellular enzyme from Pichia pastoris strain GS115 culture supernatant by ultrafiltration
recombinant extracellular enzyme from Pichia pastoris strain GS115 culture supernatant by ultrafiltration and anion exchange chromatography
-
recombinant extracellular enzyme from Yarrowia lipolytica culture supernatant by ultrafiltration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
-
recombinant His-tagged full-length enzyme and catalytic domain by nickel affinity chromatography
recombinant His-tagged full-length enzyme and isolated catalytic domain from Escerichia coli strain BL21(DE3)DELTASlyD by nickel affinity chromatography, gel filtration, and ultrafiltration
recombinant His6-tagged extracellular enzyme from Pichia pastoris strain GS115 culture supernatant by nickel affinity chromatography to homogeneity
-
recombinant protein
recombinant wild-type and mutant enzymes from Pichia pastoris strain GS115 culture supernatant by ultrafiltration and anion exchange chromatography to homogeneity
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning in Escherichia coli strain JM109, functional overexpression in Pichia pastoris strain GS115, the enzyme is secreted
expressed in Arabidopsis thaliana transformed with Agrobacterium tumefaciens
expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells and Bacillus subtilis WB600 cells
-
expressed in Pichia pastoris
expression in Aspergillus niger
expression in Escherichia coli
expression in Pichia pastoris
gene An15g07760, cloning in Escherichia coli, and expression of recombinant chimeric xylanase/mannanase fusion enzymes in Pichia pastoris strain X33 using GAP promoter, secretion to the medium
gene HhMan, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of C-terminally His6-tagged extracellular enzyme in and secretion from Pichia pastoris strain GS115
-
gene man5, DNA and amino acid sequence determination and analysis
gene man5A, DNA and amino acid sequence determination and analysis, recombinant expression in Pichia pastoris strain GS115
-
gene man5F63, DNA and amino acid sequence determination and analysis, sequence comparisons, cloning in Escherichia coli strain Trans1-T1, overexpression in Pichia pastoris strain GS115 and secretion to the culture medium
gene man5P1, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of extracellular enzyme in Pichia pastoris strain GS115
-
gene man5XZ3, sequence comparisons, cloning in Escherichia coli strain Trans1-T1, and recombinant expression of wild-type and mutant enzymes fused in frame to the DNA sequence for the Saccharomyces cerevisiae alpha-factor secretory signal peptide and under the control of the methanol-inducible alcohol oxidase promoter in Pichia pastoris strain GS115, induction by methanol, the proteins are secreted
-
gene manA, recombinant expression in and secretion from Yarrowia lipolytica
-
gene poman5A, recombinant expression of C-terminally His6-tagged extracellular enzyme in and secretion from Pichia pastoris strain GS115
-
gene RmMan5A, DNA and amino acid sequence determination and analysis, sequence comparisons, expression of His-tagged enzyme in Escherichia coli strain BL21
-
gene Tpet_1542, recombinant expression of His-tagged full-length enzyme and isolated catalytic domain in Escerichia coli strain BL21(DE3)DELTASlyD
recombinant expression of His-tagged full-length enzyme and catalytic domain
the full-length gene (Man1) and two truncated genes (Man1DELTACBM lacking CBM domain and Man1DELTALCBM lacking linker and CBM domains) from Trichoderma reesei Rut C30 are cloned and expressed in Pichia pastoris
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform manA transcription is positively regulated by Clp and RpfF and induced by locust bean gum
recombinant enzyme production is improved by 150% via supplementation with 0.2% sodium benzoate and 35% sorbitol as a preservative and stabiliser, respectively
-
two truncated genes (Man1DELTACBM lacking carbohydrate-binding module domain and Man1DELTALCBM lacking linker and CBM domains) from Trichoderma reesei Rut C30 are cloned and expressed in Pichia pastoris. The expression efficiency is improved after truncating carbohydrate-binding module. Activities of Man1 and Man1DELTACBM in the culture supernatant after 168 h of induction are 34.5 and 42.9 U/ml. A value of 0.36 U/ml is detected for Man1DELTALCBM (lacking carbohydrate-binding module and linker). Man1 shows higher thermostability than Man1DELTACBM at low temperature, whereas Man1DELTACBM has a higher specificity for galactomannan (Km: 2.5 mg/ml) than Man1 (Km: 4.0 mg/mL)
two truncated genes (Man1DELTACBM lacking carbohydrate-binding module domain and Man1DELTALCBM lacking linker and CBM domains) from Trichoderma reesei Rut C30 are cloned and expressed in Pichia pastoris. The expression efficiency is improved after truncating carbohydrate-binding module. Activities of Man1 and Man1DELTACBM in the culture supernatant after 168 h of induction are 34.5 and 42.9 U/ml. A value of 0.36 U/ml is detected for Man1DELTALCBM (lacking carbohydrate-binding module and linker). Man1 shows higher thermostability than Man1DELTACBM at low temperature, whereas Man1DELTACBM has a higher specificity for galactomannan (Km: 2.5 mg/ml) than Man1 (Km: 4.0 mg/mL)
two truncated genes (Man1DELTACBM lacking carbohydrate-binding module domain and Man1DELTALCBM lacking linker and CBM domains) from Trichoderma reesei Rut C30 are cloned and expressed in Pichia pastoris. The expression efficiency is improved after truncating carbohydrate-binding module. Activities of Man1 and Man1DELTACBM in the culture supernatant after 168 h of induction are 34.5 and 42.9 U/ml. A value of 0.36 U/ml is detected for Man1DELTALCBM (lacking carbohydrate-binding module and linker). Man1 shows higher thermostability than Man1DELTACBM at low temperature, whereas Man1DELTACBM has a higher specificity for galactomannan (Km: 2.5 mg/ml) than Man1 (Km: 4.0 mg/mL)
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
can be completely renatured after denaturation in 6 M guanidine hydrochloride
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biotechnology
degradation
drug development
-
the enzyme is a target for the development of inhibitor molecules to be used in pest control strategies to reduce the serious damage caused by the coffee berry borer during coffee cultivation
food industry
industry
medicine
pharmacology
-
tailoring of hydrogel release profiles of potential interest for intestine drug delivery. The rate of hydrolysis of O-acetyl-galactomannan hydrogels modified with alpha-galactosidase increases with decreasing degree of substitution. The addition of alpha-mannanase significantly enhances the release of bovine serum albumin encapsulated in hydrogels with a degree of substitution of 0.36, reaching a maximum of 95% released bovine serum albumin after eight hours compared to 60% without enzyme
synthesis
agriculture
-
10 U/mg enzyme can hydrolyze more than 90% of 10 mg/ml konjac flour at 50°C in 24 h
agriculture
when endo-beta-mannanase activity is much reduced by RNAi and antisense RNA strategies, their firmness is higher compared to those of control fruits at the turning and orange-color stages, but at the red-ripe stage firmness is similar between the two fruit-types
agriculture
-
the recombinant enzyme can be an additive in the feed for monogastric animals
agriculture
-
the recombinant enzyme can be an additive in the feed for monogastric animals
-
agriculture
-
10 U/mg enzyme can hydrolyze more than 90% of 10 mg/ml konjac flour at 50°C in 24 h
-
biotechnology
optimization of mannanase gene for expression in Pichia pastoris by substitution of 258 nucleotides with their corresponding counterparts according to the codon usage in Pichia pastoris, which has no change on the beta-mannanase amino acid sequence. Compared to the activity of wild-type, the expression enzyme of the optimized beta-mannanase gene acquires approximately 35% more activity
biotechnology
-
optimization of mannanase gene for expression in Pichia pastoris by substitution of 258 nucleotides with their corresponding counterparts according to the codon usage in Pichia pastoris, which has no change on the beta-mannanase amino acid sequence. Compared to the activity of wild-type, the expression enzyme of the optimized beta-mannanase gene acquires approximately 35% more activity
-
degradation
-
when assembled with the mini-CbpA, which contains a carbohydrate-binding module that provides proximity to insoluble substrates, a mixture of endoglucanase E and ManB at a molar ratio of 1:2 shows the highest synergistic effect of 2.4fold on locust bean gum degradation. The mixture at a ratio of 1:3 shows the highest synergistic effect of 2.8fold on guar gum
degradation
the addition of Man26A as a supplement to the commercial enzyme mixture Celluclast 1.5 L and Novozyme 188 results in enhanced enzymatic hydrolysis of pretreated beechwood sawdust, the release of total reducing sugars and glucose is improved by 13 and 12%, respectively
food industry
-
the enzyme is involved in the degradation of plant cell wall, resulting in an increase in feed conversion efficiency of animal feed and improvement in the growth performance of broilers. The enzyme can also be used for hydrolyzing galactomannans present in coffee extract to inhibit gel formation during freezed-drying of the instant coffee
food industry
-
the enzyme is used for clarification of fruit juices such as grape, peach, orange and pomegranate juices
food industry
-
the purified enzyme can be used in clarifying kiwi juice
food industry
-
the purified enzyme is used to clarify some fruit juices like orange, grape fruit and apple juices
food industry
-
the purified enzyme is used to clarify some fruit juices like orange, grape fruit and apple juices
-
food industry
-
the purified enzyme can be used in clarifying kiwi juice
-
industry
when used to treat softwood pulp, enzyme hydrolyzes mainly glucomannan and exhibits a positive effect as a prebleaching agent
industry
-
the enzyme is highly useful in the food/feed, paper and pulp, and detergent industries
medicine
-
mixed maltooligosacchrides produced by the enzyme exhibit in vitro anti-tumorigenic activity on human colon cancer HT29 cells
medicine
-
mixed maltooligosacchrides produced by the enzyme exhibit in vitro anti-tumorigenic activity on human colon cancer HT29 cells
-
synthesis
-
production of enzyme by expression in Aspergillus niger under control of the Aspergillus niger glyceraldehyde-3-phosphate dehydrogenase promoter gpdP and the Aspergillus awamori glucoamylase terminator glaAT. The glucose concentration and the organic nitrogen source have an effect on both the volumetric enzyme activity and the specific enzyme activity. The highest mannanase activity levels of 16596 nkat ml-1 and 574 nkat mg-1 dcw are obtained for Aspergillus niger when cultivated in a process-viable medium containing corn steep liquor as the organic nitrogen source and high glucose concentrations
synthesis
-
expression in Yarrowia lipolytica using beta-mannosidase's own secretion signal. Fed batch fermentations result in a 3.9fold increase in volumetric enzyme activity compared with batch fermentation, and a maximum titre of 26,139 nkat/ml
synthesis
-
production of beta-mannanase using palm kernel cake as substrate in solid substrate fermentation. Optimal conditions are incubation temperature of 32°C, initial moisture level of 59% and aeration rate of 0.5 l/min, resulting in a beta-mannanase yield of 2231.26 U/g
synthesis
-
development of a fed-batch strategy for engineered enzyme, using high cell-density fermentation. Mannanase activity reaches 5069 U/ml after cultivation for 56 h in 50 l fermenter
synthesis
expression in Escherichia coli based on T7 RNA polymerase promoter and tac promoter systems. Both Escherichia coli OmpA signal peptide and native Bacillus signal peptide can be used efficiently for secretion of recombinant protein. Enzyme can be harvested from whole cell lysate, periplasmic extract or culture broth 4-20 h after induction by IPTG
synthesis
-
production of beta-mannanase from palm kernel cake as a substrate in solid substrate fermentation. A statistical model suggests that the optimal conditions for attaining the highest level of beta-mannanase are incubation temperature of 32°C, initial moisture level of 59% and aeration rate of 0.5 l/min. A beta-mannanase yield of 2231.26 U/g is obtained under these optimal conditions
synthesis
-
production of beta-mannanase using palm kernel cake as substrate in solid substrate fermentation. Optimal conditions are incubation temperature of 32°C, initial moisture level of 59% and aeration rate of 0.5 l/min, resulting in a beta-mannanase yield of 2231.26 U/g
-
synthesis
-
production of beta-mannanase from palm kernel cake as a substrate in solid substrate fermentation. A statistical model suggests that the optimal conditions for attaining the highest level of beta-mannanase are incubation temperature of 32°C, initial moisture level of 59% and aeration rate of 0.5 l/min. A beta-mannanase yield of 2231.26 U/g is obtained under these optimal conditions
-
synthesis
-
development of a fed-batch strategy for engineered enzyme, using high cell-density fermentation. Mannanase activity reaches 5069 U/ml after cultivation for 56 h in 50 l fermenter
-
synthesis
-
production of enzyme by expression in Aspergillus niger under control of the Aspergillus niger glyceraldehyde-3-phosphate dehydrogenase promoter gpdP and the Aspergillus awamori glucoamylase terminator glaAT. The glucose concentration and the organic nitrogen source have an effect on both the volumetric enzyme activity and the specific enzyme activity. The highest mannanase activity levels of 16596 nkat ml-1 and 574 nkat mg-1 dcw are obtained for Aspergillus niger when cultivated in a process-viable medium containing corn steep liquor as the organic nitrogen source and high glucose concentrations
-
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Release 2023.1 (January 2023)
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