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Information on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase and Organism(s) Phanerodontia chrysosporium and UniProt Accession Q0PQY8

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Phanerodontia chrysosporium
UNIPROT: Q0PQY8 not found.
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The taxonomic range for the selected organisms is: Phanerodontia chrysosporium
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
beta-mannanase, endo-beta-mannanase, man5a, endo-mannanase, manb-1601, man26a, endo-beta-1,4-mannanase, man26b, man5c, endo-1,4-beta-mannanase, 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
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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 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
galactomannan + H2O
hydrolyzed galactomannan
show the reaction diagram
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?
glucomannan + H2O
oligosaccharides
show the reaction diagram
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?
locust bean gum + H2O
?
show the reaction diagram
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?
mannan + H2O
oligosaccharides
show the reaction diagram
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?
additional information
?
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enzyme exhibits substantial transglycosylase activity
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q0PQY8_PHACH
460
0
49057
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
x * 65000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 65000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
sequence contains a secretory signal peptide
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Aspergillus niger
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
when used to treat softwood pulp, enzyme hydrolyzes mainly glucomannan and exhibits a positive effect as a prebleaching agent
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Benech, R.; Li, X.; Patton, D.; Powlowski, J.; Storms, R.; Bourbonnais, R.; Paice, M.; Tsang, A.
Recombinant expression, characterization, and pulp prebleaching property of a Phanerochaete chrysosporium endo-beta -1,4-mannanase
Enzyme Microb. Technol.
41
740-747
2007
Phanerodontia chrysosporium (Q0PQY8)
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Manually annotated by BRENDA team