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Information on EC 3.2.1.4 - cellulase and Organism(s) Melanocarpus albomyces and UniProt Accession Q8J0K8
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3.2.1.4 cellulaseIUBMB Comments
Will also hydrolyse 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
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Word Map
- 3.2.1.4
- cellulose
- trichoderma
- biomass
- reesei
- xylanase
-
cellulolytic
-
saccharification
-
lignocellulosic
- cellobiose
- straw
- lignin
- polysaccharide
- aspergillus
- glycoside
- beta-glucosidase
- corn
-
biofuels
- pectinase
- xylan
- hemicellulose
- bagasse
- penicillium
- endoglucanases
-
bioethanol
- xylose
- amylase
- polygalacturonase
- sugarcane
-
carbohydrate-binding
-
feedstock
- viride
- glucans
- thermocellum
- bran
- carboxymethylcellulose
-
microcrystalline
- exoglucanase
-
cellulose-binding
- laccase
-
biorefinery
- rumen
- biotechnology
- analysis
-
novozyme
-
silage
- endoxylanase
-
compost
- industry
- textile industry
- food industry
- biofuel production
- agriculture
-
deconstruct
- xylobiose
- diagnostics
- harzianum
- degradation
- chrysosporium
- synthesis
- detergent
- environmental protection
- xyloglucans
The taxonomic range for the selected organisms is: Melanocarpus albomyces
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cellulase, cel7a, cellobiohydrolase i, cel5a, cel6a, avicelase, endocellulase, celluclast, cel7b, cbhii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
9.5 cellulase
-
-
-
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Abscission cellulase
-
-
-
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alkali cellulase
-
-
-
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Alkaline cellulase
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-
-
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avicelase
-
-
-
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beta-1,4-endoglucan hydrolase
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-
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beta-1,4-glucanase
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-
-
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Carboxymethyl cellulase
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-
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Carboxymethyl-cellulase
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carboxymethylcellulase
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CEL1
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cellobiohydrolase
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celluase A
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celludextrinase
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-
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Cellulase
cellulase A 3
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-
-
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Cellulase E1
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-
-
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Cellulase E2
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-
-
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Cellulase E4
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-
-
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Cellulase E5
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-
-
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Cellulase SS
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-
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Cellulase V1
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-
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cellulosin AP
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-
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CMCase
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-
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CX-cellulase
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-
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EG1
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-
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EG2
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-
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EG3
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-
-
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EGA
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-
-
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EGB
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-
-
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EGC
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-
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EGCCA
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-
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EGCCC
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-
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EGCCD
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-
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EGCCF
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EGCCG
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EGD
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EGE
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-
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EGF
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-
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EGH
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EGI
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EGIV
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EGM
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EGSS
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EGX
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EGY
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EGZ
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endo-1,4-beta-D-glucanase
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endo-1,4-beta-glucanase
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endo-1,4-beta-glucanase E1
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endo-1,4-beta-glucanase V1
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endocellulase E1
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endoglucanase
endoglucanase D
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FI-CMCASE
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pancellase SS
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Thermoactive cellulase
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Cellulase
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endoglucanase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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-
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-
SYSTEMATIC NAME
IUBMB Comments
4-beta-D-glucan 4-glucanohydrolase
Will also hydrolyse 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
CAS REGISTRY NUMBER
COMMENTARY
9012-54-8
-
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
phosphoric acid swollen cellulose + H2O
?
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferone + D-lactose
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferone + D-lactose
very low activity
-
-
?
cellulose + H2O
?
crystalline and amorphous cellulose
-
-
?
additional information
?
-
-
no substrate: 4-methylumbelliferyl-beta-D-lactoside
-
-
?
additional information
?
-
no substrate: 4-methylumbelliferyl-beta-D-lactoside
-
-
?
additional information
?
-
Cel7B has greater activity than the endoglucanases Cel45A and Cel7A against crystalline cellulose, whereas in the case of amorphous substrate the order is reversed
-
-
?
additional information
?
-
Cel7B has greater activity than the endoglucanases Cel45A and Cel7A against crystalline cellulose, whereas in the case of amorphous substrate the order is reversed
-
-
?
additional information
?
-
Cel7B has greater activity than the endoglucanases Cel45A and Cel7A against crystalline cellulose, whereas in the case of amorphous substrate the order is reversed
-
-
?
additional information
?
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Cel7B has greater activity than the endoglucanases Cel45A and Cel7A against crystalline cellulose, whereas in the case of amorphous substrate the order is reversed
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cellobiose
very low activity against 4-methyl-umberriferyl-beta-D-lactoside is almost totally inhibited by 0.005 M cellobiose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
pH 5: about 55% of maximal activity, pH 9.0: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 80
-
50°C: about 70% of maximal activity, 80°C: about 50% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). Q8J0K8_MELAO
235
0
25001
TrEMBL
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
treatment with endoglycosidase H decreases the molecular mass by about 2-5 kDa
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
use to release dye in neutral pH conditions from indigo-dyed cotton-containing fabric in biostoning applications
degradation
use to release dye in neutral pH conditions from indigo-dyed cotton-containing fabric in biostoning applications
industry
-
the purified enzyme performs well in biostoning of denim fabric at neutral pH
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miettinen-Oinonen, A.; Londesborough, J.; Joutsjoki, V.; Lantto, R.; Vehmaanpera, J.
Three cellulases from Melanocarpus albomyces for textile treatment at neutral pH
Enzyme Microb. Technol.
34
332-341
2004
Melanocarpus albomyces, Melanocarpus albomyces ALKO4237
-
Szijarto, N.; Siika-Aho, M.; Tenkanen, M.; Alapuranen, M.; Vehmaanperae, J.; Reczey, K.; Viikari, L.
Hydrolysis of amorphous and crystalline cellulose by heterologously produced cellulases of Melanocarpus albomyces
J. Biotechnol.
136
140-147
2008
Melanocarpus albomyces (Q8J0K6), Melanocarpus albomyces (Q8J0K7), Melanocarpus albomyces (Q8J0K8), Melanocarpus albomyces
Miettinen-Oinonen, A.; Londesborough, J.; Joutsjoki, V.; Lantto, R.; Vehmaanpera, J.
Three cellulases from Melanocarpus albomyces for textile treatment at neutral pH
Enzyme Microb. Technol.
34
332-341
2004
Melanocarpus albomyces, Melanocarpus albomyces (Q8J0K8), Melanocarpus albomyces ALKO4237, Melanocarpus albomyces ALKO4237 (Q8J0K8)
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EXTERNAL LINKS (specific for EC-Number 3.2.1.4)
Transporter Classification Database (TCDB): 4.D.3.1.6
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