3.2.1.78: mannan endo-1,4-beta-mannosidase
This is an abbreviated version!
For detailed information about mannan endo-1,4-beta-mannosidase, go to the full flat file.
Word Map on EC 3.2.1.78
-
3.2.1.78
-
mannans
-
galactomannans
-
locust
-
glucomannans
-
guar
-
konjac
-
mannobiose
-
alpha-galactosidase
-
reesei
-
manno-oligosaccharides
-
carob
-
radicle
-
micropylar
-
mannan-degrading
-
ivory
-
kraft
-
mannotetraose
-
beta-mannans
-
mannopentaose
-
hemicellulase
-
softwood
-
endohydrolases
-
cellulosome
-
cellvibrio
-
endo-1,4-beta-glucanase
-
copra
-
thermomonospora
-
mannan-binding
-
food industry
-
agriculture
-
synthesis
-
pharmacology
-
degradation
-
biotechnology
-
paper production
-
nutrition
-
medicine
-
industry
-
drug development
- 3.2.1.78
- mannans
- galactomannans
- locust
- glucomannans
- guar
- konjac
- mannobiose
- alpha-galactosidase
- reesei
- manno-oligosaccharides
- carob
- radicle
-
micropylar
-
mannan-degrading
-
ivory
-
kraft
- mannotetraose
- beta-mannans
- mannopentaose
-
hemicellulase
-
softwood
-
endohydrolases
- cellulosome
- cellvibrio
- endo-1,4-beta-glucanase
-
copra
-
thermomonospora
-
mannan-binding
- food industry
- agriculture
- synthesis
- pharmacology
- degradation
- biotechnology
- paper production
- nutrition
- medicine
- industry
- drug development
Reaction
Synonyms
(1,4)-beta-D-mannan mannanohydrolase, 1,4-beta-D-mannan mannanohydrolase, 1,4-beta-mannanase, beta-1,4-D-mannanase, beta-1,4-mannan 4-mannanohydrolase, beta-1,4-mannanase, beta-D-mannanase, Beta-mannanase, beta-mannanase B, CaMan, CelB, cold-adapted beta-mannanase, CsMan5, CtManf, Dtur_0671, em26a, endo-1,4-beta-D-mannanase, 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)-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-mannase, endo-beta-D-1,4-mannanase, endo-beta-D-mannanase, endo-beta-mannanase, endo-mannanase, GH 134 beta-1,4-mannanase, GH134, GH5-CBM27, KMAN-3, LeMAN4, LeMAN4a, Man, MAN I, Man II, MAN-P, Man1, Man113A, Man134A, Man26A, Man26A-50K, Man26b, Man4A, Man5, Man5A, Man5C, man5D, Man5P1, Man5XZ3, Man5_8, Man7, ManA, ManA/HmA, ManB, ManB-1601, ManC, ManEM17, ManF, ManH, ManIII, mannan endo-1,4-beta-mannanase, mannan endo-1,4-beta-mannosidase, mannan endo-1.4-beta-D-mannosidase, mannanase, mannanase, endo-1,4-beta-, ManP, ManS2, MYCTH_99077, PoMan5A, Rman, TpMan, TrMan5A
ECTree
3.2.1.78 mannan endo-1,4-beta-mannosidaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C143A
the mutant shows reduced activity compared to the wild type enzyme
N90A
the mutant shows reduced activity compared to the wild type enzyme
W13F
the mutant shows reduced activity compared to the wild type enzyme
Y292A
the mutant shows increased activity with mannotriose and mannotetraose and about 50% reduced activity with mannopentaose and mannohexaose compared to the wild type enzyme
S289W
mutation lowers KM for mannooligosaccharides by 30-45% and increases transglycosylation yield by 50% compared to wild-type
W283S
mutation in subsite +1, mutation results in increase in KM value, reduction in the transglycosylation yield by 30-45% and decrease in activity towards mannans
S289W
-
mutation lowers KM for mannooligosaccharides by 30-45% and increases transglycosylation yield by 50% compared to wild-type
-
W283S
-
mutation in subsite +1, mutation results in increase in KM value, reduction in the transglycosylation yield by 30-45% and decrease in activity towards mannans
-
R171K
the mutant displays retained activity on polymeric galactomannan but reduced activity on oligosaccharides due to an increase of Km. While the wild-type enzyme produces mannobiose as dominant product from mannotetraose, the R171K mutant enzyme produces mannotriose and mannose. The preferred productive binding mode of mannotetraose is shifted from subsite -2 to +2 in the wild-type to subsite -3 to +1 in the R171K mutant. The wild-type enzyme can perform transglycosylation on to saccharide acceptors while the R171K mutant cannot. Wild-type and mutant enzyme show the ability to perform alcoholysis reactions with methanol and butanol, forming new beta-linked glycoconjugates. It appears that the wild-type enzyme produces mainly mannobiose conjugates using mannotetetraoses substrate, while in contrast the R171K mutant produces mainly mannotriose conjugates, due to the altered subsite binding
additional information
additional information
-
generation of two truncated enzyme mutants lacking the family 1 carbohydrate-binding module Man5DELTACBM or the family 1 carbohydrate-binding module and the Thr/Ser-rich linker region, Man5DELTACL, respectively. The mutant enzymes show significantly altered secondary structures compared to the wild-type enzyme, overview. Removal of the family 1 carbohydrate-binding module alone improves the thermostability of the enzyme, but additional removal of the linker region results in worse thermostability. The mutants are less stable in presence of acetone, SDS, Triton X-100, or urea compared to the wild-type enzyme
additional information
-
generation of two truncated enzyme mutants lacking the family 1 carbohydrate-binding module Man5DELTACBM or the family 1 carbohydrate-binding module and the Thr/Ser-rich linker region, Man5DELTACL, respectively. The mutant enzymes show significantly altered secondary structures compared to the wild-type enzyme, overview. Removal of the family 1 carbohydrate-binding module alone improves the thermostability of the enzyme, but additional removal of the linker region results in worse thermostability. The mutants are less stable in presence of acetone, SDS, Triton X-100, or urea compared to the wild-type enzyme
-
additional information
-
gene optimization according to the codon usage bias in Pichia pastoris and synthesis by splicing overlap extension PCR
additional information
construction of a chimeric enzyme of xylanase and mannanase with higher catalytic efficiency and improved properties, the two enzymes are fused together with twelve fusion types
additional information
-
gene optimization according to the codon usage bias in Pichia pastoris and synthesis by splicing overlap extension PCR
-
additional information
-
construction of a chimeric enzyme of xylanase and mannanase with higher catalytic efficiency and improved properties, the two enzymes are fused together with twelve fusion types
-
additional information
optimization of mannanase gene for expression in Pichia pastoris by substitution of 258 nucleotides with their corresponding counterparts according to the codon usage in Pichia pastoris, which has no change on the beta-mannanase amino acid sequence
additional information
-
optimization of mannanase gene for expression in Pichia pastoris by substitution of 258 nucleotides with their corresponding counterparts according to the codon usage in Pichia pastoris, which has no change on the beta-mannanase amino acid sequence
additional information
-
optimization of mannanase gene for expression in Pichia pastoris by substitution of 258 nucleotides with their corresponding counterparts according to the codon usage in Pichia pastoris, which has no change on the beta-mannanase amino acid sequence
-
additional information
mutagenesis of Trp271 at the +1 subsite plays a crucial role in the enhanced transglycosylation activity
additional information
-
mutagenesis of Trp271 at the +1 subsite plays a crucial role in the enhanced transglycosylation activity
additional information
-
mutagenesis of Trp271 at the +1 subsite plays a crucial role in the enhanced transglycosylation activity
-
additional information
deletion of the CBM6 domain increases the enzyme stability while enabling it to retain 80% and 60% of its initial activity after treatment at 80°C and 90°C for 30 min
additional information
-
deletion of the CBM6 domain increases the enzyme stability while enabling it to retain 80% and 60% of its initial activity after treatment at 80°C and 90°C for 30 min
-
additional information
the cultivar Walter displays an inactive enzyme due to the absence of the C-terminal four amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein
additional information
-
the cultivar Walter displays an inactive enzyme due to the absence of the C-terminal four amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein
additional information
mutant MG17 is catalytically inactive, mutant protein is present at wild-type molecular mass
additional information
-
mutant MG17 is catalytically inactive, mutant protein is present at wild-type molecular mass
