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Information on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase and Organism(s) Caldicellulosiruptor saccharolyticus and UniProt Accession P77847

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This record set is specific for:
Caldicellulosiruptor saccharolyticus
UNIPROT: P77847 not found.
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The taxonomic range for the selected organisms is: Caldicellulosiruptor saccharolyticus
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
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beta-1,4-mannan 4-mannanohydrolase
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beta-D-mannanase
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Beta-mannanase
beta-mannanase B
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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 hide
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
4-beta-D-mannan mannanohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
37288-54-3
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SUBSTRATE
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
?
show the reaction diagram
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?
mannan + H2O
?
show the reaction diagram
the amino-terminal catalytic domain has beta-mannanase activity, and the carboxy-terminal domain acts as an endoglucanase
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-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
substrate: locust bean gum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 65
substrate: locust bean gum, pH 6.5
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 70
40°C: about 45% of maximal activity, 70°C: about 55% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
closely related to Caldicellulosiruptor sp. Rt8B.4
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vanfossen, A.L.; Lewis, D.L.; Nichols, J.D.; Kelly, R.M.
Polysaccharide degradation and synthesis by extremely thermophilic anaerobes
Ann. N.Y. Acad. Sci.
1125
322-337
2008
Caldicellulosiruptor saccharolyticus (P22533)
Manually annotated by BRENDA team
Gibbs, M.D.; Saul, D.J.; Lthi, E.; Bergquist, P.L.
The beta-mannanase from "Caldocellum saccharolyticum" is part of a multidomain enzyme
Appl. Environ. Microbiol.
58
3864-3867
1992
Caldicellulosiruptor saccharolyticus (P22533)
Manually annotated by BRENDA team
Gibbs, M.; Elinder, A.; Reeves, R.; Bergquist, P.
Sequencing, cloning and expression of a beta-1,4-mannanase gene, manA, from the extremely thermophilic anaerobic bacterium, Caldicellulosiruptor Rt8B.4
FEMS Microbiol. Lett.
141
37-43
1996
Caldicellulosiruptor saccharolyticus (P77847), Caldicellulosiruptor saccharolyticus
Manually annotated by BRENDA team