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Information on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase and Organism(s) Cryptopygus antarcticus and UniProt Accession B4XC07
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3.2.1.78 mannan endo-1,4-beta-mannosidaseSpecify your search results
Word Map
- 3.2.1.78
- mannans
- galactomannans
- locust
- glucomannans
- guar
- konjac
- mannobiose
- alpha-galactosidase
- reesei
- manno-oligosaccharides
- carob
- radicle
-
micropylar
-
mannan-degrading
-
ivory
-
kraft
- mannotetraose
- beta-mannans
- mannopentaose
-
hemicellulase
-
softwood
-
endohydrolases
- cellulosome
- cellvibrio
- endo-1,4-beta-glucanase
-
copra
-
thermomonospora
-
mannan-binding
- food industry
- agriculture
- synthesis
- pharmacology
- degradation
- biotechnology
- paper production
- nutrition
- medicine
- industry
- drug development
The taxonomic range for the selected organisms is: Cryptopygus antarcticus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
beta-mannanase, endo-beta-mannanase, man5a, endo-mannanase, manb-1601, endo-beta-1,4-mannanase, man26a, man26b, man5c, caman, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-beta-D-mannan mannanohydrolase
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beta-1,4-mannan 4-mannanohydrolase
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beta-D-mannanase
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Beta-mannanase
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-
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beta-mannanase B
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endo-1,4-beta-mannanase
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endo-1,4-mannanase
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endo-beta-1,4-mannase
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endo-beta-mannanase
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mannanase, endo-1,4-beta-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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SYSTEMATIC NAME
IUBMB Comments
4-beta-D-mannan mannanohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
37288-54-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 60
the enzyme shows 20-40% of its maximum activity at 0-4°C and has its optimum at 30°C, about 10% of maximal activity at 50-60°C, inactivation at 70°C, profile overview
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the glycosyl hydrolae famiyl 5, GH5
additional information
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
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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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MANA_CRYAT
382
0
41833
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme adopts a TIM (beta/alpha)8-barrel fold
additional information
-
the enzyme adopts a TIM (beta/alpha)8-barrel fold
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Song, J.M.; Nam, K.W.; Kang, S.G.; Kim, C.G.; Kwon, S.T.; Lee, Y.H.
Molecular cloning and characterization of a novel cold-active beta-1,4-D-mannanase from the Antarctic springtail, Cryptopygus antarcticus
Comp. Biochem. Physiol. B
151
32-40
2008
Cryptopygus antarcticus (B4XC07), Cryptopygus antarcticus
Kim, M.K.; An, Y.J.; Song, J.M.; Jeong, C.S.; Kang, M.H.; Kwon, K.K.; Lee, Y.H.; Cha, S.S.
Structure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-beta-1,4-D-mannanase from the Antarctic springtail, Cryptopygus antarcticus
Proteins
82
3217-3223
2014
Cryptopygus antarcticus (B4XC07), Cryptopygus antarcticus
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Release 2023.1 (January 2023)
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