Information on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.2.1.78
-
RECOMMENDED NAME
GeneOntology No.
mannan endo-1,4-beta-mannosidase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mannan degradation
-
-
Fructose and mannose metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
4-beta-D-mannan mannanohydrolase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
(1,4)-beta-D-mannan mannanohydrolase
-
-
1,4-beta-D-mannan mannanohydrolase
-
-
-
-
beta-1,4-D-mannanase
-
beta-1,4-mannan 4-mannanohydrolase
-
-
-
-
beta-D-mannanase
-
-
-
-
Beta-mannanase
-
-
-
-
Beta-mannanase
-
Beta-mannanase
-
-
Beta-mannanase
-
-
-
Beta-mannanase
-
Beta-mannanase
Bacillus subtilis MA139
-
-
Beta-mannanase
-
-
Beta-mannanase
Neosartorya fischeri P1
-
-
-
Beta-mannanase
Reinekea sp.
-
-
Beta-mannanase
Reinekea sp. KIT-YO10
-
-
-
Beta-mannanase
-
-
Beta-mannanase
;
-
beta-mannanase B
-
-
-
-
cold-adapted beta-mannanase
-
CsMan5
Neurospora sitophila DSM 16514
-
-
endo-1,4-beta-D-mannanase
Reinekea sp.
-
-
endo-1,4-beta-D-mannanase
Reinekea sp. KIT-YO10
-
-
-
endo-1,4-beta-D-mannanase
-
endo-1,4-beta-D-mannanase
-
-
endo-1,4-beta-mannanase
-
-
-
-
endo-1,4-beta-mannanase
-
endo-1,4-beta-mannanase
-
-
endo-1,4-beta-mannanase
-
endo-1,4-beta-mannanase
Bacillus subtilis WD23
-
-
endo-1,4-beta-mannanase
-
-
endo-1,4-beta-mannanase
-
-
endo-1,4-beta-mannanase
Penicillium oxalicum GZ-2
-
-
-
endo-1,4-beta-mannanase
-
-
Endo-1,4-mannanase
-
-
-
-
endo-acting beta-1,4-mannanase
-
-
endo-beta-(1->4)-mannanase
-
-
endo-beta-(1->4)-mannanase
-
-
-
endo-beta-1,4,D-mannanase
-
-
endo-beta-1,4-D-mannanase
-
endo-beta-1,4-mannanase
-
-
endo-beta-1,4-mannanase
-
-
endo-beta-1,4-mannanase
Bacillus subtilis G1
-
-
-
endo-beta-1,4-mannanase
-
-
endo-beta-1,4-mannanase
-
-
endo-beta-1,4-mannanase
-
endo-beta-1,4-mannanase
Penicillium freii F63
-
-
endo-beta-1,4-mannanase
-
endo-beta-1,4-mannanase
-
-
endo-beta-1,4-mannase
-
-
-
-
endo-beta-D-1,4-mannanase
-
endo-beta-D-1,4-mannanase
Neurospora sitophila DSM 16514
-
-
endo-beta-D-mannanase
-
-
endo-beta-mannanase
-
-
-
-
endo-beta-mannanase
-
-
endo-beta-mannanase
-
-
-
endo-beta-mannanase
-
-
MAN I
-
isozyme, major form
Man II
-
isozyme, minor form
Man1
-
-
Man26A-50K
-
-
Man5
-
-
Man5
Bacillus sp. MSK-5
-
-
-
Man5P1
-
gene name
Man5P1
Neosartorya fischeri P1
-
gene name
-
Man5XZ3
-
gene name
Man5XZ3
Aspergillus nidulans XZ3
-
gene name
-
ManA
Alicyclobacillus acidocaldarius Tc-12-31
-
-
-
ManA
Orpinomyces sp.
-
-
ManH
Cellulosimicrobium sp.
-
ManIII
Penicillium occitanis Pol6
-
-
-
mannan endo-1,4-beta-mannanase
-
mannan endo-1,4-beta-mannanase
-
-
mannanase
Orpinomyces sp.
-
-
mannanase, endo-1,4-beta-
-
-
-
-
PoMan5A
Penicillium oxalicum GZ-2
-
-
-
Rman
Reinekea sp.
-
-
Rman
Reinekea sp. KIT-YO10
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37288-54-3
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
anearogenes
-
-
Manually annotated by BRENDA team
Alicyclobacillus acidocaldarius Tc-12-31
strain Tc-12-31
-
-
Manually annotated by BRENDA team
member of glycosyl hydrolase family 5
-
-
Manually annotated by BRENDA team
MRC 11624
Uniprot
Manually annotated by BRENDA team
strain MRC11624
-
-
Manually annotated by BRENDA team
Aspergillus aculeatus MRC 11624
MRC 11624
Uniprot
Manually annotated by BRENDA team
Aspergillus aculeatus MRC11624
strain MRC11624
-
-
Manually annotated by BRENDA team
strain IMI 385708, formerly Thermomyces lanuginosus strain IMI 158749
-
-
Manually annotated by BRENDA team
gene man5XZ3
-
-
Manually annotated by BRENDA team
member of glycosyl hydrolase family 5
UniProt
Manually annotated by BRENDA team
member of glycosyl hydrolase family 5
UniProt
Manually annotated by BRENDA team
Aspergillus nidulans XZ3
gene man5XZ3
-
-
Manually annotated by BRENDA team
; strain FTCC 5003
-
-
Manually annotated by BRENDA team
commercial preparations
-
-
Manually annotated by BRENDA team
gene An15g07760
SwissProt
Manually annotated by BRENDA team
strain gr
-
-
Manually annotated by BRENDA team
stran BK01
UniProt
Manually annotated by BRENDA team
Aspergillus niger BK01
stran BK01
UniProt
Manually annotated by BRENDA team
gene An15g07760
SwissProt
Manually annotated by BRENDA team
Aspergillus niger FTCC
strain FTCC 5003
-
-
Manually annotated by BRENDA team
Aspergillus niger FTCC 5003
-
-
-
Manually annotated by BRENDA team
strain CGMCC 1416
UniProt
Manually annotated by BRENDA team
strain CGMCC1554
Uniprot
Manually annotated by BRENDA team
Bacillus circulans CGMCC
strain CGMCC 1416
UniProt
Manually annotated by BRENDA team
Bacillus circulans CGMCC1554
strain CGMCC1554
Uniprot
Manually annotated by BRENDA team
gene name ydhT
UniProt
Manually annotated by BRENDA team
M-I, M-II, M-III
-
-
Manually annotated by BRENDA team
strain MSK-5
-
-
Manually annotated by BRENDA team
strain N16-5
-
-
Manually annotated by BRENDA team
Bacillus sp. MSK-5
strain MSK-5
-
-
Manually annotated by BRENDA team
strain N16-5
-
-
Manually annotated by BRENDA team
beta-mannanase; strain MA139
UniProt
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
gene manA
-
-
Manually annotated by BRENDA team
isoform BCman-GH26
Uniprot
Manually annotated by BRENDA team
isolated from soil sample of Heilongjiang Liangshui National Nature Reserve
UniProt
Manually annotated by BRENDA team
strain B36
-
-
Manually annotated by BRENDA team
strain WY34, induced by growth on konjac powder as carbon source at 50C
-
-
Manually annotated by BRENDA team
Bacillus subtilis B36
strain B36
-
-
Manually annotated by BRENDA team
Bacillus subtilis G1
gene manA
-
-
Manually annotated by BRENDA team
Bacillus subtilis KK01
KK01
-
-
Manually annotated by BRENDA team
Bacillus subtilis KU-1
KU-1
-
-
Manually annotated by BRENDA team
Bacillus subtilis MA139
beta-mannanase; strain MA139
UniProt
Manually annotated by BRENDA team
Bacillus subtilis WD23
isolated from soil sample of Heilongjiang Liangshui National Nature Reserve
UniProt
Manually annotated by BRENDA team
Bacillus subtilis WY34
strain WY34, induced by growth on konjac powder as carbon source at 50C
-
-
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
Bispora sp.
strain MEY-1
UniProt
Manually annotated by BRENDA team
Caldicellulosiruptor sp.
Rt8B.4
-
-
Manually annotated by BRENDA team
Cellulosimicrobium sp.
member of glycosyl hydrolase family 5
UniProt
Manually annotated by BRENDA team
member of glycosyl hydrolase family 5
UniProt
Manually annotated by BRENDA team
member of glycoyl hydrolase family 26
-
-
Manually annotated by BRENDA team
isozymes ManA, ManB with at least 7 isomers
-
-
Manually annotated by BRENDA team
Dictyoglomus thermophilum Rt46B.1
Rt46B.1
-
-
Manually annotated by BRENDA team
Fusicoccum sp.
-
-
-
Manually annotated by BRENDA team
Gyoerffyella speciosa
-
-
-
Manually annotated by BRENDA team
isoform MAN1
Uniprot
Manually annotated by BRENDA team
gene HhMan
-
-
Manually annotated by BRENDA team
Lilium testaceum
-
-
-
Manually annotated by BRENDA team
blue mussel
Uniprot
Manually annotated by BRENDA team
isozymes ManA, ManB
-
-
Manually annotated by BRENDA team
gene man5P1
-
-
Manually annotated by BRENDA team
Neosartorya fischeri P1
gene man5P1
-
-
Manually annotated by BRENDA team
i.e. Neurospora sitophila, gene man5
UniProt
Manually annotated by BRENDA team
Neurospora sitophila DSM 16514
i.e. Neurospora sitophila, gene man5
UniProt
Manually annotated by BRENDA team
no activity in Escherichia coli
harboring a manA-containing plasmid
-
-
Manually annotated by BRENDA team
Orpinomyces sp.
strain PC-2
-
-
Manually annotated by BRENDA team
strain GS01, 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
-
-
Manually annotated by BRENDA team
Paenibacillus polymyxa GS01
strain GS01, 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
-
-
Manually annotated by BRENDA team
sequence consists of a carbohydrate binding module belonging to family 6 and a family 26 catalytic domain
UniProt
Manually annotated by BRENDA team
sequence consists of a carbohydrate binding module belonging to family 6 and a family 26 catalytic domain
UniProt
Manually annotated by BRENDA team
gene man5F63
UniProt
Manually annotated by BRENDA team
Penicillium freii F63
gene man5F63
UniProt
Manually annotated by BRENDA team
Penicillium occitanis Pol6
Pol6
-
-
Manually annotated by BRENDA team
gene poman5A
-
-
Manually annotated by BRENDA team
Penicillium oxalicum GZ-2
gene poman5A
-
-
Manually annotated by BRENDA team
Penicillium wortmanni
-
-
-
Manually annotated by BRENDA team
Reinekea sp.
isolated from the seashore of Kanazawa Port in Japan
-
-
Manually annotated by BRENDA team
Reinekea sp. KIT-YO10
isolated from the seashore of Kanazawa Port in Japan
-
-
Manually annotated by BRENDA team
gene RmMan5A
-
-
Manually annotated by BRENDA team
ATCC 43812
Swissprot
Manually annotated by BRENDA team
var. Mill.
Swissprot
Manually annotated by BRENDA team
Thermotoga neapolitana 5068
5068
-
-
Manually annotated by BRENDA team
gene Tpet_1542
UniProt
Manually annotated by BRENDA team
isolated from the Kubiki oil reservoir in Niigata (Japan)
UniProt
Manually annotated by BRENDA team
gene Tpet_1542
UniProt
Manually annotated by BRENDA team
isolated from the Kubiki oil reservoir in Niigata (Japan)
UniProt
Manually annotated by BRENDA team
Tyromyces palustris
-
-
-
Manually annotated by BRENDA team
strain MA-138
-
-
Manually annotated by BRENDA team
strain MA-138
UniProt
Manually annotated by BRENDA team
strain MA-138
-
-
Manually annotated by BRENDA team
strain MA-138
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
evolution
the enzyme belongs to the glycosyl hydrolase family 5, GH5
evolution
-
the enzyme belongs to the glycosyl hydrolae famiyl 5, GH5
evolution
Aspergillus nidulans XZ3, Neosartorya fischeri P1
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
-
evolution
Neurospora sitophila DSM 16514
-
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
-
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
Cellulosimicrobium sp.
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; 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; 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
-
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
-
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
-
evolution
Penicillium freii F63, Penicillium oxalicum GZ-2, Thermotoga petrophila RKU-1
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
-
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 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
-
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 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 20C and pH 6
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
Neurospora sitophila DSM 16514
-
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 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 20C and pH 6; 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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4-beta-D-mannan + H2O
?
show the reaction diagram
-
-
-
?
1,4-beta-D-mannan + H2O
?
show the reaction diagram
-
-
-
?
1,4-beta-D-mannan + H2O
?
show the reaction diagram
Aspergillus niger BK01
-
-
-
?
2,4-dinitrophenyl-beta-mannobioside + H2O
2,4-dinitrophenol + beta-mannobiose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
show the reaction diagram
Neurospora sitophila, Neurospora sitophila DSM 16514
-
-
?
azo-carob galactomannan + H2O
?
show the reaction diagram
Neurospora sitophila, Neurospora sitophila DSM 16514
-
-
-
?
azurine-crosslinked galactomannan + H2O
?
show the reaction diagram
-
hydrolysis
-
-
?
beta-1,4-D-mannan + H2O
?
show the reaction diagram
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
show the reaction diagram
-
-
-
?
birch wood xylan + H2O
?
show the reaction diagram
Aspergillus niger, Aspergillus niger BK01
9.1% of the activity with locust bean gum
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis WY34
-
poor substrate
-
-
?
carob galactomannan + H2O
?
show the reaction diagram
-
-
-
?
carob-galactomannan + H2O
?
show the reaction diagram
i.e. locust bean gum
-
-
?
copra mannan + H2O
?
show the reaction diagram
-
90% of the activity with locust bean gum
-
-
?
copra meal defatted with n-hexane + H2O
?
show the reaction diagram
-
better substrate than locust bean gum and guar gum
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactoglucomannan + oligosaccharide
[3H]-labelled polysaccharide
show the reaction diagram
-
transglucosylation
-
?
galactomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactomannan + H2O
?
show the reaction diagram
-
-
-
?
galactomannan + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis MA139
-
-
-
?
galactomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
-
-
?
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
Dictyoglomus thermophilum Rt46B.1
-
-
-
?
galactomannan + H2O
galactosyl-mannosyl oligosaccharides
show the reaction diagram
-
products show a degree of polymerization of 2-6
?
galactomannan + H2O
galactosyl-mannosyl oligosaccharides
show the reaction diagram
-
enzyme prefers galactomannans with lower degree of galactosylation e.g. from carob gum
-
?
galactomannan + H2O
galactosyl-mannosyl oligosaccharides
show the reaction diagram
-
source of substrate locust bean gum
-
?
galactomannan + H2O
mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose
show the reaction diagram
-
different contents of glucose and mannose, overview
product ratio overview
?
glucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
glucomannan + H2O
?
show the reaction diagram
-
-
-
?
glucomannan + H2O
?
show the reaction diagram
-
-
-
?
glucomannan + H2O
?
show the reaction diagram
-
-
-
?
glucomannan + H2O
?
show the reaction diagram
from konjac flour
-
-
?
glucomannan + H2O
?
show the reaction diagram
from konjac flour
-
-
?
glucomannan + H2O
?
show the reaction diagram
Bispora sp.
from konjac flour
70% of the activity with locust bean gum
-
?
glucomannan + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
219% of the activity with locust bean gum
-
-
?
glucomannan + H2O
?
show the reaction diagram
Aspergillus niger BK01
-
-
-
?
glucomannan + H2O
?
show the reaction diagram
Bacillus sp. MSK-5
-
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
?
show the reaction diagram
from konjac flour
-
-
?
glucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
Lilium testaceum
-
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
of various size
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
Tyromyces palustris
-
-
of various size
?
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
glucomannan + H2O
glucosyl-mannosyl oligosaccharides
show the reaction diagram
-
products show a degree of polymerization of 2-6
?
glucomannan + H2O
glucosyl-mannosyl oligosaccharides
show the reaction diagram
-
source of substrate konjac
-
?
guar gum + H2O
mannose + mannobiose + mannotriose
show the reaction diagram
Talaromyces funiculosus, Penicillium wortmanni
-
-
-
-
guar gum + H2O
mannose + mannobiose + mannotriose
show the reaction diagram
-
-
mannobiose + mannotriose + mannotetraose
-
guar gum + H2O
?
show the reaction diagram
-
-
-
-
?
guar gum + H2O
?
show the reaction diagram
-
-
-
-
?
guar gum + H2O
?
show the reaction diagram
-
-
-
-
?
guar gum + H2O
?
show the reaction diagram
-
-
-
?
guar gum + H2O
?
show the reaction diagram
-
-
-
-
?
guar gum + H2O
?
show the reaction diagram
-
-
-
-
?
guar gum + H2O
?
show the reaction diagram
Bispora sp.
-
14.8% of the activity with locust bean gum
-
?
guar gum + H2O
?
show the reaction diagram
-
26% of the activity with locust bean gum
-
?
guar gum + H2O
?
show the reaction diagram
-
21% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
show the reaction diagram
18% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
show the reaction diagram
-
90% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
show the reaction diagram
Reinekea sp.
-
1.7% activity compared to konjac glucomannan
-
-
?
guar gum + H2O
?
show the reaction diagram
-
41.2% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
show the reaction diagram
Aspergillus niger BK01
18% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
show the reaction diagram
Aspergillus nidulans XZ3
-
41.2% of the activity with locust bean gum
-
-
?
guar gum + H2O
?
show the reaction diagram
Reinekea sp. KIT-YO10
-
1.7% activity compared to konjac glucomannan
-
-
?
guar gum + H2O
?
show the reaction diagram
Penicillium oxalicum GZ-2
-
-
-
-
?
guar gum + H2O
?
show the reaction diagram
Bacillus circulans CGMCC
-
26% of the activity with locust bean gum
-
?
guar gum + H2O
?
show the reaction diagram
Bacillus subtilis B36
-
21% of the activity with locust bean gum
-
-
?
guar gum + H2O
mannobiose + mannotriose
show the reaction diagram
-
-
mannobiose, mannotriose, and a mixture of various mannose-linked oligosaccharides
?
guar gum + H2O
mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose
show the reaction diagram
-
-
product ratio overview
?
guar gum galactomannan + H2O
?
show the reaction diagram
-
-
-
-
?
guar gum glucomannan + H2O
?
show the reaction diagram
-
-
-
?
guar gum glucomannan + H2O
?
show the reaction diagram
-
-
-
?
ivory nut mannan + H2O
mannobiose + mannotriose
show the reaction diagram
-
-
-
?
ivory nut mannan + H2O
?
show the reaction diagram
-
-
-
?
ivory nut mannan + H2O
?
show the reaction diagram
-
-
-
-
?
ivory nut mannan + H2O
?
show the reaction diagram
-
-
-
?
ivory nut mannan + H2O
?
show the reaction diagram
Reinekea sp., Reinekea sp. KIT-YO10
-
46% activity compared to konjac glucomannan
-
-
?
ivory nut mannan + H2O
mannotriose + mannotetraose + mannopentaose + mannohexaose
show the reaction diagram
Cellulosimicrobium sp., Cellulosimicrobium sp. HY-13
-
main products, at 14%, 25%, 20%, and 13%, respectively
?
konjac glucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
konjac glucomannan + H2O
?
show the reaction diagram
-
-
-
?
konjac glucomannan + H2O
?
show the reaction diagram
-
-
-
?
konjac glucomannan + H2O
?
show the reaction diagram
Reinekea sp.
-
best substrate
-
-
?
konjac glucomannan + H2O
?
show the reaction diagram
-
-
-
?
konjac glucomannan + H2O
?
show the reaction diagram
Reinekea sp. KIT-YO10
-
-
-
-
?
konjac glucomannan + H2O
?
show the reaction diagram
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
Bacillus subtilis KK01
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Bispora sp.
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
76% of products are oligomannosides
-
?
locust bean gum + H2O
?
show the reaction diagram
-
hydrolysis products are mainly oligosaccharides plus one monosaccharide
-
?
locust bean gum + H2O
?
show the reaction diagram
-
main products are manno-oligosaccharides of 2-6 residues and mannose
-
?
locust bean gum + H2O
?
show the reaction diagram
-
products are various manno-oligosaccharides of M2-M6 size and mannose
-
?
locust bean gum + H2O
?
show the reaction diagram
-
enzyme is highly specific for substrate
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Reinekea sp.
-
9.6% activity compared to konjac glucomannan
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Paenibacillus polymyxa GS01
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Reinekea sp. KIT-YO10
-
9.6% activity compared to konjac glucomannan
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Penicillium oxalicum GZ-2
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Bacillus sp. MSK-5
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Penicillium occitanis Pol6
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Bacillus circulans CGMCC
-
hydrolysis products are mainly oligosaccharides plus one monosaccharide
-
?
locust bean gum + H2O
?
show the reaction diagram
Bacillus subtilis WY34
-
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
Bacillus subtilis B36
-
enzyme is highly specific for substrate
-
-
?
locust bean gum + H2O
mannopentaose
show the reaction diagram
Cellulosimicrobium sp., Cellulosimicrobium sp. HY-13
-
44%, main product
?
locust bean gum + H2O
mannobiose + mannotriose
show the reaction diagram
-
52.7% mannobiose, 18.1% mannotriose and 29.2% other unidentifiable oligosaccharides
?
locust bean gum + H2O
mannobiose + mannotriose
show the reaction diagram
-
best substrate
mannobiose, mannotriose, and a mixture of various mannose-linked oligosaccharides
?
locust bean gum + H2O
mannobiose + mannotriose
show the reaction diagram
Penicillium freii F63
-
52.7% mannobiose, 18.1% mannotriose and 29.2% other unidentifiable oligosaccharides
?
locust bean gum + H2O
mannobiose + mannotriose + mannotetraose
show the reaction diagram
Aspergillus nidulans, Aspergillus nidulans XZ3
-
best substrate
hydrolysis products are 17.2% mannobiose, 37.4% mannotriose, 9.9% mannotetraose, and 35.5% other unidentified oligosaccharides
?
locust bean gum + H2O
mannose + mannobiose + mannotriose + mannotetraose + galactose-linked mannotetraose + mannopentaose + mannohexaose
show the reaction diagram
-
-
product ratio overview
?
locust bean gum galactomannan + H2O
mannobiose
show the reaction diagram
-
main product, with low amounts of mannotirose and higher manno-oligosaccarides
?
locust bean gum glucomannan + H2O
?
show the reaction diagram
-
-
-
?
locust bean gum glucomannan + H2O
?
show the reaction diagram
-
-
-
?
low viscosity locust bean galactomannan + H2O
?
show the reaction diagram
-
-
-
-
?
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man + H2O
2 Man-beta-1,4-Man
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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)Man + H2O
?
show the reaction diagram
-
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Man + H2O
mannose + Manbeta(1-4)Man
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
Manbeta(1-4)Manbeta(1-4)Man + mannose + Manbeta(1-4)Man
show the reaction diagram
-
-
?
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man + H2O
mannose + Manbeta(1-4)Man + Manbeta(1-4)Manbeta(1-4)Man
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
?
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
show the reaction diagram
-
-
?
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
show the reaction diagram
-
-
-
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
?
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
show the reaction diagram
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
dimers, trimers and other
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
codium, coffee
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
Bacillus subtilis KK01
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
mannan + H2O
?
show the reaction diagram
-
-
-
-
?
mannan + H2O
?
show the reaction diagram
-
-
-
?
mannan + H2O
mannosyl oligosaccharides
show the reaction diagram
-
products show a degree of polymerization of 2-6
?
mannan + H2O
mannotetraose + mannobiose + mannotriose
show the reaction diagram
Bacillus subtilis, Bacillus subtilis WY34
-
source of substrate: copra
-
?
mannan A + H2O
?
show the reaction diagram
-
-
-
-
?
mannohexaose + H2O
mannotriose
show the reaction diagram
-
-
main product
?
mannohexaose + H2O
?
show the reaction diagram
-
-
-
-
?
mannopentaose + H2O
?
show the reaction diagram
Neosartorya fischeri, Neosartorya fischeri P1
-
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
?
mannopentaose + H2O
mannotriose + mannobiose
show the reaction diagram
-
-
main products
?
mannopentaose + H2O
mannose + mannotetraose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
?
show the reaction diagram
Neosartorya fischeri, Neosartorya fischeri P1
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
small amounts of mannose and mannotriose
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
small amounts of mannose and mannotriose
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
small amounts of mannose and mannotriose
?
mannotriose + H2O
mannobiose + mannose
show the reaction diagram
-
-
-
?
mannotriose + H2O
mannobiose + mannose
show the reaction diagram
-
-
-
?
mannotriose + H2O
mannobiose + mannose
show the reaction diagram
-
-
-
?
mannotriose + H2O
mannobiose + mannose
show the reaction diagram
-
-
not
?
palm kernel cake + H2O
?
show the reaction diagram
Aspergillus niger, Aspergillus niger FTCC 5003, Aspergillus niger FTCC
-
-
-
-
?
starch + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis WY34
-
poor substrate
-
-
?
tara gum galactomannan + H2O
?
show the reaction diagram
-
-
-
-
?
xylan + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis WY34
-
poor substrate
-
-
?
mannotriose + H2O
?
show the reaction diagram
Neosartorya fischeri, Neosartorya fischeri P1
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
not: mannobiose
-
-
?
additional information
?
-
-
not: mannobiose
-
-
?
additional information
?
-
-
not: mannobiose
-
-
?
additional information
?
-
-
transglycosylation reaction, Streptomyces: transfer of one mannose unit from oligosaccharides, fenugreek: transfer of oligomannose residues
-
-
-
additional information
?
-
-
no substrate: mannotriose, mannobiose, enzyme requires a minimum of four sugar units in substrates
-
-
-
additional information
?
-
-
no substrate: xylan, caroxymethyl cellulose, cellulose, mannan
-
-
-
additional information
?
-
requires at least five sugar moieties for effective catalytic activity, no substrate: yeast mannan
-
-
-
additional information
?
-
during hydrolysis of 1,4-beta-manno-oligosaccharides, transglycosylation reactions occur
-
-
-
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
?
-
enzyme exhibits substantial transglycosylase activity
-
-
-
additional information
?
-
-
no substrate: carboxymethyl cellulose
-
-
-
additional information
?
-
enzyme has the ability to bind soluble beta-mannans, 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
?
-
no substrate: soluble starch, methylcellulose
-
-
-
additional information
?
-
no substrates: mannobiose, mannotriose, mannotetraose, mannohexaose
-
-
-
additional information
?
-
negligible activity with starch, carboxymethyl cellulose, and alpha-cellulose
-
-
-
additional information
?
-
-
no substrate: carboxymethyl cellulose, oat spelt xylan, starch, pectin, 4-nitrophenyl-beta-D-mannopyranoside
-
-
-
additional information
?
-
-
enzyme is active in hydrolyzing the beta-mannan-rich cell wall of soybean seeds
-
-
-
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
?
-
no substrate: guar gum, copra meal
-
-
-
additional information
?
-
Cellulosimicrobium sp.
no substrate: mannobiose, or 4-nitrophenyl sugar derivatives
-
-
-
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 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 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 hydrolyzes high-molecular weight polysaccharides with beta-1,4-glycosidic bonds
-
-
-
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 involved in release of mannooligosaccharides from spent coffee ground cleaving the backbone at random locations in galactomannan, glucomannan, galactoglucomannan and 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
?
-
-
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 beechwood xylan, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-mannoside, and carboxymethyl cellulose
-
-
-
additional information
?
-
Reinekea sp.
-
no activity with tamarind xyloglucan, sodium arginate, carboxymethylcellulose, low-melting point agarose, gellan gum, xylan, carrageenan, and laminaran
-
-
-
additional information
?
-
-
production of mannooligosaccharides from pretreated and defatted copra meal hydrolysis by the enzyme
-
-
-
additional information
?
-
the enzyme also show transglycosylation activity
-
-
-
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 shows requirement of four mannose residues for hydrolysis, and is also capable of catalyzing transglycosylation reactions
-
-
-
additional information
?
-
no substrate: mannobiose, or 4-nitrophenyl sugar derivatives
-
-
-
additional information
?
-
-
production of mannooligosaccharides from pretreated and defatted copra meal hydrolysis by the enzyme
-
-
-
additional information
?
-
Aspergillus niger BK01
negligible activity with starch, carboxymethyl cellulose, and alpha-cellulose
-
-
-
additional information
?
-
Aspergillus nidulans XZ3
-
no activity with beechwood xylan, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-mannoside, and carboxymethyl cellulose
-
-
-
additional information
?
-
Dictyoglomus thermophilum Rt46B.1
-
-
-
-
?
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
?
-
Reinekea sp. KIT-YO10
-
no activity with tamarind xyloglucan, sodium arginate, carboxymethylcellulose, low-melting point agarose, gellan gum, xylan, carrageenan, and laminaran
-
-
-
additional information
?
-
Neurospora sitophila DSM 16514
the native wild-type enzyme shows bifunctional activity as both an endo-glucanase and an endo-mannanase, substrate specificity, overview, the enzyme also show transglycosylation activity
-
-
-
additional information
?
-
Penicillium oxalicum GZ-2
-
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
?
-
Penicillium occitanis Pol6
-
no substrate: carboxymethyl cellulose, oat spelt xylan, starch, pectin, 4-nitrophenyl-beta-D-mannopyranoside
-
-
-
additional information
?
-
enzyme has the ability to bind soluble beta-mannans, 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
?
-
Neosartorya fischeri P1
-
the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides, 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 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
?
-
Bacillus circulans CGMCC
no substrate: soluble starch, methylcellulose
-
-
-
additional information
?
-
Bacillus subtilis B36
-
no substrate: carboxymethyl cellulose
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
guar gum + H2O
mannose + mannobiose + mannotriose
show the reaction diagram
Talaromyces funiculosus, Penicillium wortmanni
-
-
-
-
guar gum + H2O
mannose + mannobiose + mannotriose
show the reaction diagram
-
-
mannobiose + mannotriose + mannotetraose
-
ivory nut mannan + H2O
mannobiose + mannotriose
show the reaction diagram
-
-
-
?
konjac glucomannan + H2O
?
show the reaction diagram
Reinekea sp., Reinekea sp. KIT-YO10
-
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
Bacillus subtilis KK01
-
-
-
?
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
?
mannan + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme is active in hydrolyzing the beta-mannan-rich cell wall of soybean seeds
-
-
-
additional information
?
-
A5IMX7
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 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 hydrolyzes high-molecular weight polysaccharides with beta-1,4-glycosidic bonds
-
-
-
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 involved in release of mannooligosaccharides from spent coffee ground cleaving the backbone at random locations in galactomannan, glucomannan, galactoglucomannan and mannan
-
-
-
additional information
?
-
Neurospora sitophila, Neurospora sitophila DSM 16514
I4IY26
the native wild-type enzyme shows bifunctional activity as both an endo-glucanase and an endo-mannanase, substrate specificity, overview
-
-
-
additional information
?
-
Penicillium oxalicum GZ-2
-
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
?
-
Neosartorya fischeri P1
-
the enzyme is highly active towards galactomannan and glucomannan, and exhibits classic endo-activity producing a mixture of mannooligosaccharides
-
-
-
additional information
?
-
A5IMX7
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ag+
Bispora sp.
stimulation
Ca2+
-
stimulates
Ca2+
-
5 mM, 228% of initial activity
Ca2+
1 mM, 124% of initial activity
Ca2+
-
2.5 mM, 10% stimulation. Inhibition at 2.0 mM
Ca2+
1 mM, 119% of initial activity
Co2+
-
1 mM, 126% of initial activity
Co2+
1 mM, 112% of initial activity
Cu2+
-
5 mM, 151% of initial activity
Cu2+
-
2.5 mM, 9% stimulation
Cu2+
38% residual activity
Cu2+
110% of initial activity
EDTA
64% residual activity
Fe2+
-
1 mM, 124% of initial activity
Fe3+
Bispora sp.
stimulation
Li+
1 mM, 112% of initial activity
Mg2+
-
slight activation
Mg2+
-
5 mM, 178% of initial activity
Mg2+
1 mM, 118% of initial activity
Mn2+
Bispora sp.
stimulation
Mn2+
53% residual activity
NaCl
activates 150% at 100 mg/ml
Ni2+
Bispora sp.
stimulation
Pb2+
slight stimulation
Zn2+
-
5 mM, 220% of initial activity
Zn2+
79% residual activity
Zn2+
slight stimulation
additional information
Na+, Li+, NH4+, Ca2+, Mg2+ and Ba2+ have no effect on the recombinant mannanase activity
additional information
-
poor effects by Na+, Ca2+, and Mn2+
additional information
poor effects by Na+, K+, Ag+, Li+, Ca2+, Ni2+ and EDTA at 1 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
1 mM, 54% residual activity
4-nitrophenyl-thio-beta-D-mannopyranoside
-
-
-
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
Ag+
-
1 mM, 54% residual activity
Ag+
-
1 mM, complete loss of activity
Ag+
-
1 mM, 3% residual activity
Ag+
strong inhibition
Ag+
-
90% inhibition
Ag+
1 mM, more than 80% inhibition
Ag+
-
5 mM, 24.8% residual activity
Ag+
1 mM, 2% residual activity
Ag+
1 mM, 18% residual activity
Ag+
-
complete inhibition
Ag+
-
48% residual activity
Al3+
1 mM, more than 80% inhibition
Al3+
1 mM, 31% residual activity
Ca2+
-
2 mM, 64% residual activity. Stimulating above 2.5 mM
Ca2+
1 mM, 83% residual activity
Co2+
-
1 mM, 50% loss of activity
Co2+
-
2.5 mM, 42% residual activity
Cu2+
-
1 mM, 49% loss of activity
Cu2+
-
35-40% inhibition
Cu2+
1 mM, more than 80% inhibition
Cu2+
1 mM, 12% residual activity
Cu2+
1 mM, 2% residual activity
Cu2+
-
complete inhibition
Cu2+
Cellulosimicrobium sp.
more than 50% inhibtion
Cu2+
1 mM, 76% residual activity
dithiothreitol
-
1 mM, 25% loss of activity
EDTA
-
1 mM, 37% residual activity
EDTA
-
1 mM, 33.9% residual activity
EDTA
-
2.5 mM, 77% residual activity
EDTA
Cellulosimicrobium sp.
5 mM, 20% residaul activity
Fe2+
-
1 mM, 40% loss of activity
Fe2+
Cellulosimicrobium sp.
more than 50% inhibtion
Fe3+
-
90% inhibition
Fe3+
-
2.5 mM, 71% residual activity
Fe3+
1 mM, 37% residual activity
Fe3+
-
30.6% residual activity
Hg2+
-
1 mM, 2% residual activity
Hg2+
strong inhibition
Hg2+
Bispora sp.
strong
Hg2+
1 mM, more than 80% inhibition
Hg2+
-
5 mM, 16.4% residual activity
Hg2+
1 mM, 8% residual activity
Hg2+
1 mM, 1% residual activity
Hg2+
-
complete inhibition
Hg2+
1 mM, 4% residual activity
K+
1 mM, 62% residual activity
methanol
-
-
Mg2+
-
1 mM, 53% residual activity
Mg2+
-
84% residual activity
Mn2+
-
1 mM, 22% residual activity
Mn2+
-
35-40% inhibition
Mn2+
-
5 mM, 32% residual activity
Mn2+
35% of initial activity
Mn2+
-
5 mM, 50% residual activity
N-bromosuccinimide
-
-
N-bromosuccinimide
-
1 mM, 3% residual activity
N-bromosuccinimide
-
complete inhibition
n-butanol
-
complete inhibition at 20-30% v/v
Ni2+
-
1 mM, 61% residual activity
p-chloromercuribenzoate
-
-
Pb2+
1 mM, more than 80% inhibition
SDS
-
complete inhibition at 0.25-1.0% w/v
Sodium dodecyl sulfate
strong inhibition
Sodium dodecyl sulfate
Bispora sp.
strong
Sodium dodecyl sulfate
20% of initial activity
sodium dodecylsulfate
-
1 mM, 55% residual activity
sodium dodecylsulfate
-
1 mM, 79% residual activity
Triton X-100
-
-
Tween 20
-
-
Zn2+
1 mM, more than 80% inhibition
Zn2+
1 mM, 16% residual activity
Zn2+
-
68% residual activity
Zn2+
Cellulosimicrobium sp.
more than 50% inhibtion
Mn2+
1 mM, 63% residual activity
additional information
-
not inhibitory: EDTA, 2-mercaptoethanol
-
additional information
Bispora sp.
enzymatic activity is not significantly affected by ions such as Ca2+, Cr3+, Co2+, Zn2+, Na+, K+, and Mg2+
-
additional information
-
not inhibitory: EDTA, phenyl methyl sulfonyl fluoride, 1,10-phenanthroline
-
additional information
not inhibtory: Mg2+, Co2+, EDTA
-
additional information
Reinekea sp.
-
Ca2+, Mg2+, Mn2+, Fe2+, Ni2+, and Zn2+ have either no effect or a slightly inhibitory effect
-
additional information
-
the purified recombinant enzyme has a strong resistance to SDS and Ag+ and proteases pepsin and trypsin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
1 mM, 11% increase in activity
2-mercaptoethanol
1 mMm, 121% of initial activity
2-mercaptoethanol
-
153% of initial activity
2-mercaptoethanol
-
-
2-mercaptoethanol
-
acetone
-
activates the wild-type enzyme and mutant Man5DELTACBM at 40-60% v/v, no effect on mutant Man5DELTACL
Ca2+
-
1 mM, 20% increase in activity
cysteine
-
slight activation
dithiothreitol
-
129% of initial activity
SDS
-
the wild-type enzyme slightly at 0.5-1.0% v/v, inhibits the mutant enzymes
Sodium azide
Cellulosimicrobium sp.
hydrolysis of locust bean gum is enhanced by approximately 1.45fold in poresence of sodium azide
Triton X-100
1%, 123% of initial activity
Triton X-100
-
activates the wild-type enzyme slightly at 0.5% v/v, inhibits the mutant enzymes
EDTA
236% of initial activity
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00066
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant E212A
0.00074
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant Y285A
0.0014
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant D283H
0.0037
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant H211A/D283A
0.0068
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant H211A
0.0093
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, wild type
0.01
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant H211N
0.0141
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant W162A
0.0149
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant W156A
0.0166
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant D283A
0.0205
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant W217A
3.07
low viscosity locust bean galactomannan
-
isozyme MAN I
-
3.12
low viscosity locust bean galactomannan
-
isozyme MAN II
-
1.6
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37C
1.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
wild-type, pH 5.5, 37C
2.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37C
2.9
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
pH 5.5, 37C
0.6
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
wild-type, pH 5.5, 37C
1
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37C
1.3
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
mutant W283S, pH 5.5, 37C
1.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
pH 5.5, 37C
9
Manbeta(1-4)Manbeta(1-4)Man
-
-
2.49
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
-
1.61
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
-
5.3
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
30C, pH 4.8
1.9
soluble mannan
-
-
-
0.04
2,4-dinitrophenyl-beta-mannobioside
-
pH 6.5, mutant H143A
additional information
locust bean gum
-
KM value is 34.9 mg/ml, pH 5.0, 28C
-
additional information
locust bean gum
KM value is 3.8 mg/ml
-
0.5
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
-
additional information
additional information
-
-
-
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
-
-
-
additional information
additional information
Km value is 0.16 mg/ml for locust-bean galactomannan
-
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
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
Km value for locust bean gum at pH 2.4, 50C is 0.93 mg/ml
-
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 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
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 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 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
Reinekea sp.
-
Michaelis-Menten kinetics
-
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, 80C
-
additional information
additional information
-
Km is 2.074 mg/ml with guar gum for the recombinant enzyme at pH 5.5 and 30C
-
additional information
additional information
-
recombinant enzyme, Km for locust bean gum is 0.83 0.2 mg/ml, pH 4.0, 80C
-
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 of the recombinant enzyme is 7.8 mg/ml for locust bean gum, pH 4.5, 50C
-
additional information
additional information
kinetics of recombinant chimeric enzymes, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
148
1,4-beta-D-Mannan
Aspergillus niger
B6V876
70C
18200
beta-1,4-D-mannan
Bacillus licheniformis
D0UHB3
50C, pH 6.0
292
carob galactomannan
Aspergillus niger
B6V876
70C
-
12.9
galactomannan
Hordeum vulgare
Q2I011
30C, pH 4.8
-
215
glucomannan
Aspergillus niger
B6V876
70C
21000
glucomannan
Bacillus licheniformis
D0UHB3
50C, pH 6.0
4.77
guar gum
Rhizomucor miehei
-
pH 7.0, 55C, recombinant enzyme
-
50.87
guar gum
Hypothenemus hampei
-
pH 5.5, 30C, recombinant enzyme
-
14.9
locust bean gum
Rhizomucor miehei
-
pH 7.0, 55C, recombinant enzyme
-
25.2
locust bean gum
Glycine max
-
pH 5.0, 28C
-
31200
locust bean gum
Bacillus licheniformis
D0UHB3
50C, pH 6.0
-
330
locust bean gum galactomannan
Aspergillus niger
B6V876
70C
-
1935
low viscosity locust bean galactomannan
Aspergillus fumigatus
-
isozyme MAN I
-
2246
low viscosity locust bean galactomannan
Aspergillus fumigatus
-
isozyme MAN II
-
2.8
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
67
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
pH 5.5, 37C
98
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
112
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
wild-type, pH 5.5, 37C
117
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
134
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
wild-type, pH 5.5, 37C
148
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
193
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
pH 5.5, 37C
1.17
Manbeta(1-4)Manbeta(1-4)Man
Cellulomonas fimi
-
-
0.41
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Cellulomonas fimi
-
-
0.7
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Mytilus edulis
Q8WPJ2
-
11.64
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Cellulomonas fimi
-
-
0.26
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Cellulomonas fimi
-
-
3.9
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Hordeum vulgare
Q2I011
30C, pH 4.8
45
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Mytilus edulis
Q8WPJ2
-
52.42
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Cellulomonas fimi
-
-
77
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Cellulomonas fimi
-
-
99
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
Mytilus edulis
Q8WPJ2
-
additional information
additional information
Bacillus subtilis
Q5PSP8
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 37C, pH 7.0
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
23
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
pH 5.5, 37C
7928
27
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
7928
36
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
7928
61
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
wild-type, pH 5.5, 37C
7928
109
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
pH 5.5, 37C
8926
115
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
8926
118
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
mutant W283S, pH 5.5, 37C
8926
215
Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man-beta-1,4-Man
Aspergillus nidulans
Q5AZ53, Q5B7X2
wild-type, pH 5.5, 37C
8926
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.69
-
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man}
1.13
-
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
1.95
-
Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
2.2
-
substrate guar gum, pH 7.0, 40C
3.1
-
Manbeta(1-4)Manbeta(1-4)Man
4.6
-
crude medium
4.8
-
pH 7.0, 30C, substrate beta-1,4-mannan
9.6
-
pH 7.0, 30C, substrate glucomannan
11.48
-
pH 7.0, 30C, substrate galactomannan
12.2
-
substrate locust bean gum, pH 7.0, 40C
18.5
-
substrate glucomannan, pH 7.0, 40C
27.4
-
pH 7.0, 30C
45.7
-
isozyme MAN I, after 9.9fold purification with DEAE Sepharose chromatography
47.5
purified recombinant enzyme, pH 4.5, 50C
56.7
-
isozyme MAN II, after 12.3fold purification with DEAE Sepharose chromatography
64.6
pH 5.0, 50C, recombinant protein
129.3
-
pH 4.0, 40C
190
-
isozyme MAN I, mannan A
215
-
isozyme MAN II, mannan A
225.4
-
isozyme MAN II, after 49fold purification with Phenyl Sepharose chromatography
236
Reinekea sp.
-
pH 8.0, 40C, substrate konjac glucomannan
264.1
pH 5.0, 50C, native protein
294
-
isozyme MAN I, guar gum
317
-
isozyme MAN II, guar gum
380
-
41.9 kDa protein
416.3
-
30C, pH 3.5
420.9
-
purified recombinant enzyme, locust bean gum as substrate, pH 4.0, 80C
471
-
isozyme MAN I, after 102.4fold purification with Phenyl Sepharose chromatography
475
-
61.2 kDa protein
562
-
isozyme MAN I, locust bean gum
627
-
isozyme MAN II, locust bean gum
635
pH 6.0, 60C, substrate locust bean gum
663
-
isozyme MAN I, low viscosity locust bean galactomannan
751
-
isozyme MAN II, low viscosity locust bean galactomannan
768.5 - 1249
purified recombinant chimeric enzymes, pH 5.0, 50C
928
-
pH 6.4, 50C
962
pH 6.0, 60C, substrate glucomannan
1139
-
pH 5.0, 40C
1400
-
ManB, 37C, pH 5.0
1703
-
purified recombinant enzyme, substrate locust bean gum, pH 4.0, 80C
2223
pH 6.0, 60C, substrate 1,4-beta-D-mannan
2718
-
purified recombinant enzyme, pH 6.5, 45C
3373
Bispora sp.
pH 1.5, 65C
4449
purified recombinant enzyme, pH 6.3, 70C
4839
pH 7.6, 60C
5383
-
50C
8302
-
pH 6.0, 50C
8498
Cellulosimicrobium sp.
substrate locust bean gum, pH 6.0, 50C
10760
-
purified recombinant enzyme, pH 7.0, 55C, substrate locust bean gum
14710
Cellulosimicrobium sp.
substrate ivory nut mannan, pH 6.0, 50C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
1638 A550/min/mg optical path 1cm,isozyme MAN I, OBR-LBG; 1763 A550/min/mg optical path 1cm, isozyme MAN II, OBR-LBG; no activity against 4-nitrophenyl-alpha and -beta-mannopyranosides
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
-
84.4 U/ml of recombinant enzyme in the culture supernatant of Pichia pastoris, pH 4.0, 80C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.9
-
61.2 kDa protein
3.3
-
41.9 kDa protein
3.5 - 4.5
-
-
4
-
recombinant enzyme
4
-
recombinant enzyme
4.5
Lilium testaceum
-
-
4.5
recombinant enzyme expressed in Aspergillus sojae
4.5
recombinant enzyme
4.5 - 5.5
-
-
4.8
-
assay at
5
-
recombinant protein
5
-
xylanase and mannanase activities of enzyme
5
recombinant chimeric enzymes
5.2
recombinant enzyme expressed in Pichia pastoris
5.5
-
recombinant enzyme
6
Penicillium wortmanni
-
-
6
Cellulosimicrobium sp.
-
6.3
recombinant enzyme
6.5
-
-
6.5
-
recombinant enzyme
7.5
-
-
8.5
-
M-III, at 65C
9
-
M-I, M-II, at 60C
9
Reinekea sp.
-
-
11.5
Bispora sp.
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 5.5
Bispora sp.
more than 70% of maximum activity within
2 - 7
activity range, recombinant chimeric enzymes, profiles overview
2 - 9
-
recombinant enzyme, over 20% of maximal activity at pH 2.0 and pH 9.0
2.5 - 6
-
more than 50% of maximum activity
3 - 8
-
pH 3: 15% of maximal activity
3 - 9
more than 60% of maximum activity
4 - 10
-
activity range, recombinant enzyme, profile overview
4 - 7.5
-
-
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
-
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
4.5 - 7
more than 95% of maximum activity; more than 95% of maximum activity
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 - 8
-
more than 70% of maximum activity
6
rapid loss of activity above, recombinant enzyme
6 - 10
-
-
6.8 - 8
more than 75% of maximum activity
7 - 8
more than 75% of maximum activity within
7 - 9
Reinekea sp.
-
over 80% of amximal activity
7.5
rapid loss of activity above, native enzyme
8
50% of maximum activity
10
-
44% of maximum activity
additional information
Penicillium wortmanni
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
recombinant enzyme
30
-
cold-adapted beta-mannanase
40
Lilium testaceum
-
-
45
recombinant enzyme expressed in Pichia pastoris
45
recombinant enzyme
45
-
recombinant enzyme
45 - 55
recombinant chimeric enzymes
50
Cellulosimicrobium sp.
-
50 - 60
-
for four enzyme forms
60
-
M-I, M-II
60
-
recombinant protein from Aspergillus oryzae, SDS-PAGE
60
-
at pH 4.5
60
recombinant enzyme expressed in Aspergillus sojae
60
recombinant enzyme
65
-
M-III
65
Bispora sp.
-
70
Reinekea sp.
-
-
70
recombinant enzyme
72
-
41.9 kDa protein
74
-
61.2 kDa protein
80
-
recombinant enzyme
80
-
recombinant enzyme
80
-
recombinant enzyme
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 5
-
20-40% of maximum activity
0 - 60
-
the enzyme shows 20-40% of its maximum activity at 0-4C and has its optimum at 30C, about 10% of maximal activity at 50-60C, inactivation at 70C, profile overview
5 - 60
-
recombinant enzyme, more than 30% of maximum activity within
10 - 50
-
approximately 70% between 10C and 20C, 60% activity at 40C, 30% activity at 50C
10 - 80
activity range, recombinant chimeric enzymes, profiles overview
20 - 30
-
more than 80% of maximum activity
30 - 70
Penicillium wortmanni
-
-
30 - 80
-
30C: about 25% of maximal activity, 80C: about 30% of maximal activity
30 - 80
Reinekea sp.
-
activity range, profile overview
30 - 80
-
activity range, recombinant enzyme, profile overview
30 - 90
-
activity range, profile overview
30 - 90
-
activity range, wild-type enzyme
40
about 50% of maximum activity
40 - 100
activity range, profile overview
40 - 80
recombinant enzyme, over 80% of maximal activity within this range
40 - 90
-
recombinant enzyme, over 20% of maximal activity within this range
50
-
rapid decrease in activity above
50 - 55
-
-
50 - 70
-
-
70
40% of maximum activity
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
-
isoelectric focusing
4.6
Cellulosimicrobium sp.
calculated
4.6 - 4.7
calculated from amino acid sequence
4.75 - 4.9
-
isozyme MAN II
4.9
isoelectric focusing
4.9 - 5.2
-
isozyme MAN I
5.5
-
chromatofocusing, 7 isomers
5.5
-
calculated
5.93
-
sequence calculation
6.9
-
isoelectric focusing
7.8
isoelectric focusing
9
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Lilium testaceum
-
-
Manually annotated by BRENDA team
-
specifically expressed in cotyledons of seedling
Manually annotated by BRENDA team
Bacillus subtilis KK01, Bacillus subtilis KU-1
-
-
-
Manually annotated by BRENDA team
Thermotoga neapolitana 5068
-
;
-
Manually annotated by BRENDA team
Orpinomyces sp.
-
-
Manually annotated by BRENDA team
Bacillus sp. N16-5, Bacillus subtilis B36
-
-
-
Manually annotated by BRENDA team
Tyromyces palustris
-
-
Manually annotated by BRENDA team
red fruit, not during early stages of ripening
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
germinating
Manually annotated by BRENDA team
-
specifically expressed in cotyledons of seedling
Manually annotated by BRENDA team
additional information
not in leaf
Manually annotated by BRENDA team
additional information
solid state fermentation on medium containing microcrystalline cellulose
Manually annotated by BRENDA team
additional information
the temperature range for growth is 47-88C with an optimum at 80C
Manually annotated by BRENDA team
additional information
Neurospora sitophila DSM 16514
-
solid state fermentation on medium containing microcrystalline cellulose
-
Manually annotated by BRENDA team
additional information
-
the temperature range for growth is 47-88C with an optimum at 80C
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
main enzyme activity in the fruit
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
the enzyme is secreted
-
Manually annotated by BRENDA team
-
the enzyme contains a putative 19-residue signal peptide at the N-terminus
-
Manually annotated by BRENDA team
Aspergillus nidulans XZ3
-
the enzyme is secreted
-
-
Manually annotated by BRENDA team
Aspergillus niger BK01
-
recombinant enzyme
-
-
Manually annotated by BRENDA team
Bacillus subtilis B36
-
-
-
-
Manually annotated by BRENDA team
Bacillus subtilis WD23
-
the enzyme is secreted
-
-
Manually annotated by BRENDA team
Neosartorya fischeri P1
-
the enzyme contains a putative 19-residue signal peptide at the N-terminus
-
-
Manually annotated by BRENDA team
Penicillium oxalicum GZ-2
-
the enzyme is secreted
-
-
Manually annotated by BRENDA team
additional information
the enzyme contains a putative 18-residue signal peptide
-
Manually annotated by BRENDA team
additional information
Penicillium freii F63
-
the enzyme contains a putative 18-residue signal peptide
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Cellvibrio japonicus (strain Ueda107)
Cellvibrio japonicus (strain Ueda107)
Cellvibrio japonicus (strain Ueda107)
Cellvibrio japonicus (strain Ueda107)
Cellvibrio japonicus (strain Ueda107)
Cellvibrio japonicus (strain Ueda107)
Cellvibrio japonicus (strain Ueda107)
Cellvibrio japonicus (strain Ueda107)
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18000
-
SDS-PAGE
707194
24000
-
gel filtration
208790
25000
-
gel filtration
208792, 208794
27000
-
gel filtration
208792, 208794
33000
Lilium testaceum
-
gel filtration
208803
36000
-
gel filtration
678989
37000
-
SDS-PAGE
208788
37000
-
SDS-PAGE
208798
38950
-
calculation from sequence of DNA
208805
39000
-
SDS-PAGE, 40000 by gel filtration
208809
39000
-
gel filtration, ManA and ManB
656335
39000
method not mentioned
666074
39000
-
SDS-PAGE
666685
40000
-
-
208804
40000
-
-
208808
40000
SDS-PAGE
666855
41000
-
SDS-PAGE
208788, 208798
41000
-
recombinant protein expressed in E. coli, SDS-PAGE
208806
41900
-
-
136060
42000
-
M-III, SDS-PAGE
208796
43100
-
calculation from sequence of DNA
208806
44000
-
SDS-PAGE
208792, 208794
45000
-
-
208798
45000
-
recombinant protein expressed in Aspergillus oryzae, SDS-PAGE
208807
46000
-
SDS-PAGE
208784, 208787, 208799, 208800
49000
-
SDS-PAGE
208814
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
664068
53000
-
SDS-PAGE
208788
55000
-
-
208813
57000
-
SDS-PAGE
208795
58000
-
M-I, SDS-PAGE
208796
59000
-
M-II, SDS-PAGE
208796
60000
-
isozyme MAN I, SDS-PAGE
664167
61200
-
-
136060
63000
-
isozyme MAN II, SDS-PAGE
664167
65000
-
SDS-PAGE
136061
65000
-
PAGE
709495
70000
-
gel filtration
208792, 208794
70000
gel fitlration
696843
162000
-
dimeric protein, SDS-PAGE
208816
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 113000, deduced from gene sequence, upon expression in Escherichia coli, two fragments of 45000 and 50000 Da
?
x * 42400, deduced from gene sequence, mature protein
?
-
x * 43000, ManB, SDS-PAGE
?
x * 50000, recombinant protein, x * 45000, native protein, SDS-PAGE
?
-
x * 145294, calculated
?
x * 43000, SDS-PAGE
?
-
x * 26000, SDS-PAGE
?
-
x * 39600, SDS-PAGE
?
x * 65000, SDS-PAGE
?
-
x * 39000, SDS-PAGE, x * 39627, calculated for mature protein
?
x * 41389, calculated, x * 48000, SDS-PAGE of glycosylated enzyme, x * 39000, SDS-PAGE of deglycosylated enzyme
?
-
x * 38013, calculated, x * 38000, SDS-PAGE, mature protein
?
-
x * 38000, SDS-PAGE
?
x * 32000, calculated and SDS-PAGE
?
Bispora sp.
x * 46800, SDS-PAGE
?
x * 60000, SDS-PAGE, recombinant enzyme
?
x * 31000, SDS-PAGE
?
x * 33000, SDS-PAGE and calculated
?
x * 53000, SDS-PAGE
?
x * 45000, SDS-PAGE, x * 41000, calculated
?
x * 44000, SDS-PAGE
?
-
x * 70000, SDS-PAGE, recombinant protein including His-tag
?
x * 56000, SDS-PAGE, x * 43847, calculated; x * 56000, SDS-PAGE, x * 46644, calculated
?
-
x * 37700, calculated
?
Cellulosimicrobium sp.
x * 44000, SDS-PAGE, x * 43767, calculated
?
-
x * 40000, SDS-PAGE
?
x * 39961, calculated
?
x * 53600, calculated
?
-
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
?
Reinekea sp.
-
x * 44300, SDS-PAGE
?
-
x * 35500, recombinant His6-tagged enzyme, SDS-PAGE, x * 33000, about, enzyme without signal sequence, sequence calculation
?
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE
?
-
x * 43000, recombinant enzyme, SDS-PAGE
?
x * 72000, recombinant enzyme, SDS-PAGE, x * 43000, about, sequence calculation of the mature enzyme
?
-
x * 41000, recombinant enzyme, SDS-PAGE
?
Alicyclobacillus acidocaldarius Tc-12-31
-
x * 38000, SDS-PAGE
-
?
-
x * 56000, SDS-PAGE, x * 43847, calculated; x * 56000, SDS-PAGE, x * 46644, calculated
-
?
Aspergillus nidulans XZ3
-
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
-
?
Aspergillus niger BK01
-
x * 53000, SDS-PAGE
-
?
-
x * 37700, calculated
-
?
Bacillus circulans CGMCC
-
x * 31000, SDS-PAGE
-
?
Bacillus subtilis B36
-
x * 38013, calculated, x * 38000, SDS-PAGE, mature protein
-
?
Bacillus subtilis G1
-
x * 41000, recombinant enzyme, SDS-PAGE
-
?
Bacillus subtilis WY34
-
x * 39600, SDS-PAGE
-
?
-
x * 44000, SDS-PAGE, x * 43767, calculated
-
?
Neosartorya fischeri P1
-
x * 39500, about, sequence calculation, x * 43000, recombinant glycosylated enzyme, SDS-PAGE, x * 40000, recombinant deglycosylated enzyme, SDS-PAGE
-
?
Paenibacillus polymyxa GS01
-
x * 145294, calculated
-
?
-
x * 53600, calculated
-
?
Penicillium freii F63
-
x * 72000, recombinant enzyme, SDS-PAGE, x * 43000, about, sequence calculation of the mature enzyme
-
?
Reinekea sp. KIT-YO10
-
x * 44300, SDS-PAGE
-
?
-
x * 44000, SDS-PAGE
-
dimer
-
2 * 73000, SDS-PAGE
monomer
-
1 * 39216, ManA, 1 * 39265, ManB, MALDI-TOF spectrometry
monomer
1 * 76309, calculated including signal peptide, 1 * 73588, calculated, mature protein, 1 * 73000, SDS-PAGE
monomer
-
1 * 66000, SDS-PAGE
monomer
-
1 * 76309, calculated including signal peptide, 1 * 73588, calculated, mature protein, 1 * 73000, SDS-PAGE
-
additional information
C-terminal domain of 550 amino acid residues with homology to glycosidase family 26
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 the (beta/alpha)8-barrel fold
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 two-domain enzyme encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, structure analysis and comparisons, overview
additional information
-
the three-dimensional enzyme structure contains a (beta/alpha)8 TIM barrel folding motif
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 adopts a TIM (beta/alpha)8-barrel fold
additional information
Aspergillus nidulans XZ3
-
the multimodular enzyme consists of a family 1 carbohydrate-binding module (CBM1), a Thr/Ser-rich linker region, and a catalytic domain
-
additional information
Neurospora sitophila DSM 16514
-
the enzyme adopts the (beta/alpha)8-barrel fold
-
additional information
-
the three-dimensional enzyme structure contains a (beta/alpha)8 TIM barrel folding motif
-
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; the two-domain enzyme encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, structure analysis and comparisons, overview
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
sequence contains a N-terminal signal peptide of 17 amino acids
glycoprotein
treatment with PNGaseF results in a shift to 41000 Da, both for native and recombinant protein
glycoprotein
treatment by endoglycosidase H decreases molecular mass to 46000 Da; 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 46000 Da; treatment by endoglycosidase H decreases molecular mass to 51000 Da
-
glycoprotein
Aspergillus nidulans XZ3
-
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
Aspergillus niger BK01
-
-
-
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
-
carbohydrate content of 13.1%
glycoprotein
Bacillus subtilis WY34
-
carbohydrate content of 13.1%
-
proteolytic modification
Cellulosimicrobium sp.
sequence contains a N-terminal signal peptide of 24 amino acids
proteolytic modification
-
sequence contains a N-terminal signal peptide of 24 amino acids
-
glycoprotein
-
two putative N-glycosilation sites, ManB
proteolytic modification
-
sequence contains a signal peptide of 17 amino acids
glycoprotein
-
the enzyme contains two putative N-glycosylation sites and no O-glycosylation site, deglycosylation by endo-beta-N-acetylglucosaminidase H
glycoprotein
Neosartorya fischeri P1
-
the enzyme contains two putative N-glycosylation sites and no O-glycosylation site, deglycosylation by endo-beta-N-acetylglucosaminidase H
-
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
Neurospora sitophila DSM 16514
-
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
-
5% carbohydrate content
glycoprotein
Penicillium occitanis Pol6
-
5% carbohydrate content
-
proteolytic modification
sequence contains a secretory signal peptide
glycoprotein
-
-
proteolytic modification
amino acid sequence contains a signal peptide cleavage site between residues 21-22, targeting sequence for cell wall
glycoprotein
-
-
proteolytic modification
sequence contains a signal peptide of 26 amino acids
glycoprotein
-
-
-
proteolytic modification
-
sequence contains a signal peptide of 26 amino acids
-
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
hanging-drop vapor diffusion method at room temperature
-
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
-
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, 20C, method optimization, X-ray diffraction structure determination and analysis at 1.40 A resolution, molecular replacement
hanging drop vapor diffusion
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
-
recombinant enzyme
-
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, 20C, soaking of crystals in ligand solutions, X-ray diffraction structure determination and analysis at 1.40-1,92 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 2
-
purified recombinant wild-type enzyme, 37C, 1 h, 50% activity remaining
731205
2 - 10
50C, stable for 30 min
714384
2 - 12
-
-
707194
2 - 12
-
purified recombinant enzyme, 1 h, over 65% activity remaining
731856
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
2.5 - 10
-
recombinant protein expressed in Aspergillus oryzae
208807
3
-
purified recombinant wild-type enzyme, 37C, 1 h, 50% activity remaining
731205
4
-
40C, 20 min, stable
714768
4 - 10
-
purified recombinant enzyme, 30 min, without substrate, over 80% activity remaining
731967
4 - 5
-
-
136060
4 - 8
-
40C, 1 h
208786, 208798
4 - 9
-
-
656335
4 - 9
-
purified recombinant wild-type enzyme, 37C, 1 h, stable at
731205
4 - 9
purified reocmbinant enzyme, 37C, 1 h, without substrate, more than 86% of the initial activity remaning
732202
4.5 - 8
-
-
208795
4.5 - 8.5
-
-
664167
4.5 - 9
Caldicellulosiruptor sp.
-
-
208810
5
-
30C, 24 h, 50% loss of activity
678989
5 - 12
after incubation at 50C for 30 min
709829
5 - 8
-
-
208798
5 - 9
-
-
208790
5 - 9
-
-
695836
5 - 9
-
purified recombinant enzyme, 50C, 8 h, stable at
732323
5.5 - 10.1
-
-
679046
5.5 - 7.8
purified recombinant enzyme, over 80% remaning after 1 h
731739
5.5 - 9
Cellulosimicrobium sp.
1 h, more than 80% residual activity
714512
6 - 10
retains more than 75% of maximum activity after 1 h incubation
695697
6 - 9
after incubation at 50C for 24 h
709829
6.3 - 7.1
purified recombinant enzyme, over 80% remaning after 2 h
731739
6.5 - 10
more than 80% of original activity after 12 h incubation at 4C
696843
7
-
inactivation above
697461
7.8
-
30C, 96 h, no loss of activity
678989
8
Reinekea sp.
-
purified enzyme, 30C, 30 min, over 90% activity remaining
731505
11 - 12
purified reocmbinant enzyme, 37C, 1 h, without substrate, more than 40% of the initial activity remaning
732202
additional information
-
-
208795
additional information
-
-
208796
additional information
-
-
208800
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 80
varying residual activities of recombinant chimeric enzymes, overview
732348
20 - 50
Reinekea sp.
-
purified enzyme, pH 8.0, 20 min, stable at
731505
30 - 90
-
purified recombinant wild-type enzyme, pH 5.0, 1 h, more than 45% of maximal activity at 50-80C and over 30% activity at 90C
731205
37
-
stable up to
715233
37
purified reocmbinant enzyme, pH 4.5, 2 h, no loss of activity
732202
38
20 min, 50% residual activity, recombinant enzyme
714774
39
-
4 h, stable between pH 5 and 7
208798
40
-
stable up to
208790
40
-
unstable above
656335
40
-
30 min, stable
680962
40
stable below
680974
40
recombinant enzyme expressed in Aspergillus sojae
696916
40
3 h, 95% residual activity; 3 h, 95% residual activity
714350
40 - 70
Bispora sp.
more than 65% of maximum activity within
695823
45
stable up to, for at least 20 min
696843
45
-
half-life less than 10 min
697461
45
30 min, 60% rsidual activity
707199
50
-
stable below
208788
50
-
stable below
208798
50
-
-
208804
50
60 min, 90% residual activity
695697
50
-
pH 6-9, 1 h, 70% residual activity
695836
50
recombinant enzyme expressed in Pichia pastoris
696916
50
retains 90% of its activity after incubation for 60 min
699488
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
709829
50
pH 6.0, stable for 30 min, incubation without substrate
714384
50
Cellulosimicrobium sp.
half-life 15 min
714512
50
-
30 min, 20% residual activity
715233
50
purified reocmbinant enzyme, pH 4.5, 90 min, loss of 50% activity
732202
50
-
purified recombinant enzyme, pH 5.0-9.0, 8 h, stable at
732323
52
-
20 min, 50% residual activity
714768
55
-
stable up to 55C
664167
55
-
15 min, almost complete loss of activity
678989
55
-
6 h, 50% residual activity
709495
55
-
purified recombinant enzyme, without substrate, stable up to, 90% activity remaning at 55C after 30 min
731967
60
-
for 1 h
208788
60
-
stable up to
208788
60
-
for 1 h
208809
60
Orpinomyces sp.
-
rapidly inactivated at 60C
664490
60
-
at pH 6.0, stable up to
679046
60
stable up to
679584
60
half-life 50 min
680974
60
-
60 min, 90% residual activity
683011
60
-
6 h, 50% residual activity
695675
60
-
8 h, 50% residual activity
695675
60
20 min, complete loss of activity
695697
60
-
5 h, more than 50% residual activity
699365
60
but no activity remains after incubation for 20 min
699488
60
30 min, complete loss of activity
707199
60
hlaf-life 4 min
714384
60
half-life 12 min
715882
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 60C for 4 h, the control retains 63% of the initial activity
731163
60
-
purified recombinant His6-tagged enzyme, half-life is approximately 58 h at pH 4.0
731546
60
-
purified recombinant enzyme, 6 h, over 80% activity remaining
731856
60
purified reocmbinant enzyme, pH 4.5, 30 min, complete loss of activity
732202
65
-
stable up to
208795
65
-
completely stable at
208816
65
-
stable below
695836
70
-
stable up to
208785
70
-
-
208798
70
-
recombinant protein from Aspergillus oryzae
208807
70
1 h, 70% residual activity, truncated protein fragments produced in Escherichia coli, 1 h, 87% residual activity, protein derived from Rhodothermus marinus
654287
70
-
30 min, 20% residual activity
683011
70
Bispora sp.
20 min, 50% residual activity
695823
70
-
stable for 30 min
707194
70
half-life 56 h, pH 4.0
709828
70
Reinekea sp.
-
purified enzyme, pH 8.0, 20 min, loss of 50% activity
731505
70
-
purified recombinant enzyme, 80% activity remaining after 1 h, inactivation after 2 h
731856
75
-
30 min, 90% loss of activity
679046
80
-
no loss of activity over 16 h
208808
80
-
20 min, 18% residual activity, 30 min, complete loss of activity
683011
80
-
2 min, complete loss of activity
699365
85
pH 6.0, the full-length enzyme is completely stable, while the isolated catalytic domain starts to precipitate
732786
90
1 h, 25% residual activity, truncated protein fragments produced in Escherichia coli
654287
90
-
half-life 15 min
714510
90
Reinekea sp.
-
purified enzyme, pH 8.0, 20 min, inactivation
731505
91
-
half-life 13 h
136061, 208813
additional information
-
-
208784, 208787
additional information
-
-
208788
additional information
-
-
208795
additional information
-
-
208796
additional information
-
-
208799, 208800
additional information
-
glycerol at 30-40%, potassium sorbate/sodium benzoate at 0.2%, and sorbitol at 30-35% enhances enzyme thermostability and activity, overview
731163
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
731205
additional information
-
the glycosylation status of the enzyme has no effect on the thermostability
731856
additional information
the CBM27 accessory domain is critical for thermal stability, it reduces the melting temperature from 100C to 88C
732395
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is resistant to digestion by trypsin
enzyme is strongly resistant to pepsin and trypsin digestion
Bispora sp.
enzyme is rather unstable and steadily loses activity during the purification process. Addition of 0.2% bovine serum albumine stabilizes
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
Penicillium wortmanni
-
may be used in preparations
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, stable for 18 h, pH 4-10
-
enzyme is stable at room temperature for at least 2 days
cold
Fusicoccum sp.
-
-20C, a single freeze-thawing cycle results in loss of 80% of activity. Bovine serum albumine stabilizes
cold
-
-20C, MES buffer, 4 months, without loss of activity
-
4C, 48h, 20% residual activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both native protein and expressed in Saccharomyces cerevisiae
recombinant extracellular enzyme from Yarrowia lipolytica culture supernatant by ultrafiltration
-
recombinant protein expressed in Aspergillus oryzae
-
fast flow column chromatography
-
recombinant wild-type and mutant enzymes from Pichia pastoris strain GS115 culture supernatant by ultrafiltration and anion exchange chromatography to homogeneity
-
recombinant chimeric enzymes from Pichia pastoris strain X33 culture supernatant by ammonium sulfate fractionation and gel filtration
recombinant enzyme
recombinant enzyme
M-I, M-II, M-III
-
four enzyme forms
-
from culture supernatant
-
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 enzyme from Pichia pastoris strain GS115
-
recombinant protein containing active protein domain
-
from digestive fluid
-
purification from seedling
recombinant extracellular enzyme from Pichia pastoris strain GS115 culture supernatant by ultrafiltration and anion exchange chromatography
-
native enzyme by ultrafiltration and anion exchange chromatography
recombinant protein
-
recombinant extracellular enzyme from Pichia pastoris strain GS115 culture supernatant by ultrafiltration
recombinant His6-tagged extracellular enzyme from Pichia pastoris strain GS115 culture supernatant by nickel affinity chromatography to homogeneity
-
native enzyme 29.4fold by anion exchange chromatography
Reinekea sp.
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
-
cation exchange chromatography
salt extraction, dialysis, cation exchange 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 protein expressed in Escherichia coli
-
recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli
expression in Aspergillus niger
-
expression in Aspergillus oryzae
-
expression in Yarrowia lipolytica
-
gene manA, recombinant expression in and secretion from Yarrowia lipolytica
-
expression in Aspergillus sojae and Pichia pastoris
expression in Pichia pastoris; expression in Pichia pastoris
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
-
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
expression in Pichia pastoris
expression in Escherichia coli
expression in Pichia pastoris and Escherichia coli
expression in Escherichia coli
cloning in Escherichia coli strain JM109, functional overexpression in Pichia pastoris strain GS115, the enzyme is secreted
expression in Escherichia coli
-
expression in Pichia pastoris
gene man5A, DNA and amino acid sequence determination and analysis, recombinant expression in Pichia pastoris strain GS115
-
expression in Escherichia coli
Bispora sp.
-
Caldicellulosiruptor sp.
-
expressed in Escherichia coli
-
expression in Escherichia coli
Cellulosimicrobium sp.
expression in Escherichia coli
-
both ManA and ManB
-
exprression in Escherichia coli fused with thioredoxin gene
-
expression in Escherichia coli
-
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
-
expressed in Pichia pastoris
-
gene man5P1, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of extracellular enzyme in Pichia pastoris strain GS115
-
gene man5, DNA and amino acid sequence determination and analysis
expressed in Saccharomyces cerevisiae and Escherichia coli
Orpinomyces sp.
-
expression in Escherichia coli
-
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 poman5A, recombinant expression of C-terminally His6-tagged extracellular enzyme in and secretion from Pichia pastoris strain GS115
-
expression in Aspergillus niger
gene RmMan5A, DNA and amino acid sequence determination and analysis, sequence comparisons, expression of His-tagged enzyme in Escherichia coli strain BL21
-
expressed in Arabidopsis thaliana transformed with Agrobacterium tumefaciens
expressed in Escherichia coli
-
expressed in Escherichia coli strain BL21
expression in Escherichia coli
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
expression in Escherichia coli
-
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression upon seed imbibition; expression upon seed imbibition; expression upon seed imbibition
recombinant enzyme production is improved by 150% via supplementation with 0.2% sodium benzoate and 35% sorbitol as a preservative and stabiliser, respectively
-
isoform manA transcription is positively regulated by Clp and RpfF and induced by locust bean gum
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
E167A
about 60% loss of catalytic efficiency
E266A
complete loss of activity
D283A
-
increase of Km-value by about 80%
D283H
-
dramatic decrease of Km-value
E212A
-
dramatic decrease of Km-value
H143A
-
decrease of Km-value by about 50%
H211A
-
decrease of Km-value by about 30%
H211N
-
dramatic decrease of Km-value
H211N/D283H
-
decrease of Km-value by about 50%
W156A
-
increase of Km-valueby almost 80%
W162A
-
increase of Km-value by about 50%
W217A
-
increase of Km-value by more than 100%
E222A
-
no catalytic acitivity
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
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
-
additional information
Aspergillus nidulans XZ3
-
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
-
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; gene optimization according to the codon usage bias in Pichia pastoris and synthesis by splicing overlap extension PCR
-
H1A/H23A
about 10% loss of catalytic efficiency
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
Bacillus subtilis MA139
-
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
-
Y285A
-
dramatic decrease of Km-value
additional information
mutagenesis of Trp271 at the +1 subsite plays a crucial role in the enhanced transglycosylation activity
additional information
Neurospora sitophila DSM 16514
-
mutagenesis of Trp271 at the +1 subsite plays a crucial role in the enhanced transglycosylation activity
-
E91A
-
no catalytic acitivity
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 80C and 90C 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 80C and 90C 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
mutant MG17 is catalytically inactive, mutant protein is present at wild-type molecular mass
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
can be completely renatured after denaturation in 6 M guanidine hydrochloride
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Aspergillus aculeatus MRC11624
-
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
-
nutrition
-
pulp production
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
-
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 32C, 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; production of beta-mannanase using palm kernel cake as substrate in solid substrate fermentation. Optimal conditions are incubation temperature of 32C, 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
-
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
Aspergillus niger FTCC, Aspergillus niger FTCC 5003
-
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 32C, 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; production of beta-mannanase using palm kernel cake as substrate in solid substrate fermentation. Optimal conditions are incubation temperature of 32C, initial moisture level of 59% and aeration rate of 0.5 l/min, resulting in a beta-mannanase yield of 2231.26 U/g
-
agriculture
-
10 U/mg enzyme can hydrolyze more than 90% of 10 mg/ml konjac flour at 50C in 24 h
agriculture
Bacillus sp. MSK-5
-
10 U/mg enzyme can hydrolyze more than 90% of 10 mg/ml konjac flour at 50C in 24 h
-
agriculture
-
the recombinant enzyme can be an additive in the feed for monogastric animals
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
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
agriculture
Bacillus subtilis G1
-
the recombinant enzyme can be an additive in the feed for monogastric animals
-
biotechnology
Bacillus subtilis MA139
-
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
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
paper production
cellulose degradation
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
-
agriculture
fruit ripening and seed germination
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
biotechnology
bio-bleaching for kraft pulp production