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Information on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase and Organism(s) Bacillus subtilis and UniProt Accession O05512

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Bacillus subtilis
UNIPROT: O05512 not found.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
beta-mannanase, endo-beta-mannanase, man5a, endo-mannanase, manb-1601, endo-beta-1,4-mannanase, man26a, man26b, man5c, caman, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-beta-D-mannan mannanohydrolase
-
-
-
-
beta-1,4-mannan 4-mannanohydrolase
-
-
-
-
beta-D-mannanase
-
-
-
-
Beta-mannanase
beta-mannanase B
-
-
-
-
endo-1,4-beta-mannanase
endo-1,4-mannanase
-
-
-
-
endo-beta-1,4-mannanase
-
-
endo-beta-1,4-mannase
-
-
-
-
endo-beta-mannanase
-
-
-
-
mannanase, endo-1,4-beta-
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
4-beta-D-mannan mannanohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37288-54-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4-beta-D-mannan + H2O
?
show the reaction diagram
-
-
-
?
glucomannan + H2O
?
show the reaction diagram
-
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
products are various manno-oligosaccharides of M2-M6 size and mannose
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
carrageenan gum + H2O
?
show the reaction diagram
-
71% activity compared to locust bean gum
-
-
?
ceratonia siliqua gum + H2O
?
show the reaction diagram
-
46.6% activity compared to locust bean gum
-
-
?
fenugreek gum + H2O
?
show the reaction diagram
-
268.1% activity compared to locust bean gum
-
-
?
galactoglucomannan + H2O
?
show the reaction diagram
-
-
-
-
?
galactomannan + H2O
?
show the reaction diagram
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
glucomannan + H2O
?
show the reaction diagram
glucomannan + H2O
oligosaccharides
show the reaction diagram
-
-
-
-
?
guar gum + H2O
?
show the reaction diagram
ivory nut mannan + H2O
?
show the reaction diagram
-
-
-
?
konjac powder + H2O
mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose + mannoheptaose
show the reaction diagram
-
85.1% activity compared to locust bean gum
-
-
?
locust bean gum + H2O
?
show the reaction diagram
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
-
?
locust bean gum + H2O
mannose + mannobiose + mannotriose + mannotetraose + mannopentaose + mannohexaose + mannoheptaose
show the reaction diagram
-
100% activity
-
-
?
mannan + H2O
mannotetraose + mannobiose + mannotriose
show the reaction diagram
-
source of substrate: copra
-
-
?
mannan + H2O
oligosaccharides
show the reaction diagram
mannopentaose + H2O
mannose + mannobiose + mannotriose + mannotetraose
show the reaction diagram
-
-
-
-
?
mannotetraose + H2O
mannobiose + mannose + mannotriose
show the reaction diagram
-
-
-
-
?
starch + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
xanthan gum + H2O
mannose + mannobiose
show the reaction diagram
-
345.6% activity compared to locust bean gum
-
-
?
xylan + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
locust bean gum + H2O
mannose + galactose
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
228.3% activity at 1 mM
Cu2+
38% residual activity
EDTA
64% residual activity
Fe2+
-
1 mM, 124% of initial activity
K+
-
119.8% activity at 1 mM
Mg2+
-
137.1% activity at 1 mM
Mn2+
53% residual activity
Na+
-
121.9% activity at 1 mM
NaCl
activates 150% at 100 mg/ml
Zn2+
79% residual activity
additional information
Na+, Li+, NH4+, Ca2+, Mg2+ and Ba2+ have no effect on the recombinant mannanase activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
85.5% residual activity at 5 mM
Li+
-
96.3% residual activity at 1 mM
methanol
-
-
Mg2+
-
1 mM, 53% residual activity
N-bromosuccinimide
-
1 mM, 3% residual activity
n-butanol
-
complete inhibition at 20-30% v/v
Ni2+
-
1 mM, 61% residual activity
phenylmethylsulfonyl fluoride
-
80.3% residual activity at 5 mM
sodium dodecylsulfate
Triton X-100
-
-
Tween 20
-
-
additional information
-
not inhibitory: EDTA, 2-mercaptoethanol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
123.7% activity at 1 mM
Tween 20
-
109.9% activity at 1 mM
Tween 40
-
125.4% activity at 1 mM
Tween 60
-
106.8% activity at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2223
pH 6.0, 60°C, substrate 1,4-beta-D-mannan
635
pH 6.0, 60°C, substrate locust bean gum
962
pH 6.0, 60°C, substrate glucomannan
2718
-
purified recombinant enzyme, pH 6.5, 45°C
4449
purified recombinant enzyme, pH 6.3, 70°C
8302
-
pH 6.0, 50°C
928
-
pH 6.4, 50°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
recombinant enzyme
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
44% of maximum activity
3 - 8
-
more than 60% activity between pH 3.0 and 8.0, no activity at pH 10.0
3 - 9
more than 60% 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
8
50% of maximum activity
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
recombinant enzyme
50 - 60
-
for four enzyme forms
70
recombinant enzyme
additional information
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
about 50% of maximum activity
40 - 60
-
more than 80% activity between 40 and 60°C, less than 10% activity at 65°C
40 - 80
recombinant enzyme, over 80% of maximal activity within this range
45 - 60
-
about 60% activity at 45°C, about 80% activity at 50°C, 100% activity at 55°C, about 80% activity at 60°C, about 20% activity at 65°C
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
-
SDS-PAGE
38000
-
x * 38013, calculated, x * 38000, SDS-PAGE, mature protein
38013
-
x * 38013, calculated, x * 38000, SDS-PAGE, mature protein
39000
-
SDS-PAGE, 40000 by gel filtration
39600
-
x * 39600, SDS-PAGE
41000
-
x * 41000, recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E167A
about 60% loss of catalytic efficiency
E266A
complete loss of activity
H1A/H23A
about 10% loss of catalytic efficiency
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 10
50°C, stable for 30 min
714384
3 - 9
-
after 1 h incubation at pH 3.0, 4.0, 5.0, 6.0, 7.0, 8.0 and 9.0, the enzyme retains about 68%, 82%, 93%, 95%, 90%, 68%, and 42% activity, respectively
752074
5 - 9
-
purified recombinant enzyme, 50°C, 8 h, stable at
732323
5.5 - 10.1
-
-
679046
5.5 - 7.8
purified recombinant enzyme, over 80% remaning after 1 h
731739
6 - 9
-
the enzyme is highly stable with 100% activity remaining after 1 h within a pH range of 6.0-9.0 and about 80-90% activity remaining after 1 h within a pH range of 4.0-5.0. No residual activity is detected at pH 3.0
752077
6.3 - 7.1
purified recombinant enzyme, over 80% remaning after 2 h
731739
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
pH 6.0, stable for 30 min, incubation without substrate
60
hlaf-life 4 min
35 - 45
-
the relatively high thermostability is retained after 1 h in the temperature range of 35-45°C and the stability rapidly decreases above 60°C
40 - 60
-
the enzyme is stable up to 60°C and retains 85% of its activity after 1.0 h of incubation
45
30 min, 60% rsidual activity
70
-
30 min, 20% residual activity
75
-
30 min, 90% loss of activity
80
-
20 min, 18% residual activity, 30 min, complete loss of activity
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the fused signal sequence of metalloprotease PrtA does not affect the enzymatic properties of the enzyme
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE column chromatography and Sephadex G75 gel filtration
-
ammonium sulfate precipitation, DEAE-Sepharose column chromatography and Q-Sepharose column chromatography
-
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
cloning in Escherichia coli strain JM109, functional overexpression in Pichia pastoris strain GS115, the enzyme is secreted
expressed in Escherichia coli JM109 cells
-
expressed in Escherichia coli XL10-Gold cells
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McCleary, B.V.
Modes of action of beta-mannanase enzymes of diverse origin on legume seed galactomannans
Phytochemistry
18
757-763
1979
Bacillus subtilis, Basidiomycota, Gleditsia triacanthos, Helix pomatia, Leucaena leucocephala, Medicago sativa
-
Manually annotated by BRENDA team
McCleary, B.V.
beta-D-Mannanase
Methods Enzymol.
160
596-610
1988
Aspergillus niger, Bacillus subtilis, Cyamopsis tetragonoloba, Helix pomatia, Irpex lacteus, Medicago sativa
-
Manually annotated by BRENDA team
Zakaria, M.M.; Yamamoto, S.; Yagi, T.
Purification and characterization of an endo-1,4-beta-mannanase from Bacillus subtilis KU-1
FEMS Microbiol. Lett.
158
25-31
1998
Bacillus subtilis, Bacillus subtilis KU-1
-
Manually annotated by BRENDA team
Hossain, M.Z.; Abe, J.; Hizukuri, S.
Multiple forms of beta-mannanase from Bacillus sp. KK01
Enzyme Microb. Technol.
18
95-98
1996
Bacillus subtilis, Bacillus subtilis KK01
-
Manually annotated by BRENDA team
Jiang, Z.; Wei, Y.; Li, D.; Li, L.; Chai, P.; Kusakabe, I.
High-level production, purification and characterization of a thermostable beta-mannanase from the newly isolated Bacillus subtilis WY34
Carbohydr. Polym.
66
88-96
2006
Bacillus subtilis, Bacillus subtilis WY34
-
Manually annotated by BRENDA team
Li, Y.N.; Meng, K.; Wang, Y.R.; Yao, B.
A beta-mannanase from Bacillus subtilis B36: purification, properties, sequencing, gene cloning and expression in Escherichia coli
Z. Naturforsch. C
61
840-846
2007
Bacillus subtilis, Bacillus subtilis B36
Manually annotated by BRENDA team
Yan, X.X.; An, X.M.; Gui, L.L.; Liang, D.C.
From structure to function: insights into the catalytic substrate specificity and thermostability displayed by Bacillus subtilis mannanase BCman
J. Mol. Biol.
379
535-544
2008
Bacillus subtilis (Q5PSP8), Bacillus subtilis
Manually annotated by BRENDA team
Qiao, J.; Rao, Z.; Dong, B.; Cao, Y.
Expression of Bacillus subtilis MA139 beta-mannanase in Pichia pastoris and the enzyme characterization
Appl. Biochem. Biotechnol.
160
1362-1370
2010
Bacillus subtilis (B5LX62), Bacillus subtilis, Bacillus subtilis MA139 (B5LX62), Bacillus subtilis MA139
Manually annotated by BRENDA team
Yamabhai, M.; Buranabanyat, B.; Jaruseranee, N.; Songsiriritthigul, C.
Efficient E. coli expression systems for the production of recombinant beta-mannanases and other bacterial extracellular enzymes
Bioeng. Bugs
2
45-49
2011
Bacillus subtilis (O05512)
Manually annotated by BRENDA team
Li, H.; Liu, Z.; Wang, C.; Huang, S.; Zhao, M.
Secretory expression and characterization of a novel thermo-stable, salt-tolerant endo-1,4-beta-mannanase of Bacillus subtilis WD23 by Pichia pastoris
Eur. Food Res. Technol.
240
671-677
2015
Bacillus subtilis (D0UH99), Bacillus subtilis WD23 (D0UH99)
-
Manually annotated by BRENDA team
Vu, T.T.; Quyen, D.T.; Dao, T.T.; Nguyen, S.l.e.T.
Cloning, high-level expression, purification, and properties of a novel endo-beta-1,4-mannanase from Bacillus subtilis G1 in Pichia pastoris
J. Microbiol. Biotechnol.
22
331-338
2012
Bacillus subtilis, Bacillus subtilis G1
Manually annotated by BRENDA team
Liu, H.; Gong, J.; Li, H.; Lu, Z.; Li, H.; Qian, J.; Xu, Z.; Shi, J.
Biochemical characterization and cloning of an endo-1,4-beta-mannanase from Bacillus subtilis YH12 with unusually broad substrate profile
Process Biochem.
50
712-721
2015
Bacillus subtilis, Bacillus subtilis YH12
-
Manually annotated by BRENDA team
Eom, G.; Oh, J.; Park, J.; Jegal, J.; Song, J.
Secretory production of enzymatically active endo-beta-1,4-mannanase from Bacillus subtilis by ABC exporter in Escherichia coli
Process Biochem.
51
999-1005
2016
Bacillus subtilis, Bacillus subtilis WL7
-
Manually annotated by BRENDA team