Any feedback?
Information on EC 3.2.1.176 - cellulose 1,4-beta-cellobiosidase (reducing end) and Organism(s) Phanerodontia chrysosporium and UniProt Accession Q7LIJ0
for references in articles please use BRENDA:EC3.2.1.176Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.2.1.176 cellulose 1,4-beta-cellobiosidase (reducing end)IUBMB Comments
Some exocellulases, most of which belong to the glycoside hydrolase family 48 (GH48, formerly known as cellulase family L), act at the reducing ends of cellulose and similar substrates. The CelS enzyme from Clostridium thermocellum is the most abundant subunit of the cellulosome formed by the organism. It liberates cellobiose units from the reducing end by hydrolysis of the glycosidic bond, employing an inverting reaction mechanism . Different from EC 3.2.1.91, which attacks cellulose from the non-reducing end.
Specify your search results
Word Map
- 3.2.1.176
-
crew
-
subsystem
-
mission
-
hydroponic
- cellulosome
- thermocellum
-
bioregenerative
-
life-support
- cellulases
-
lunar
-
long-duration
-
inedible
- degradation
-
breadboard
- avicel
-
dockerin
-
moon
- synthesis
- biotechnology
- biofuel production
- analysis
- paper production
The taxonomic range for the selected organisms is: Phanerodontia chrysosporium
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
2
+
2
=
2
+
+
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and similar substrates, releasing cellobiose from the reducing ends of the chains.
Synonyms
celss, cel48s, cbh-1, cbhi.1, cel48c, gh7 cbh, cbh7b, 1,4-beta-d-glucan cellobiohydrolase i, cellobiohydrolase cels, tr-cel7a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cel48A
-
-
-
-
cellobiohydrolase CelS
-
-
-
-
Cellulase SS
-
-
-
-
celS
-
-
-
-
CelSS
-
-
-
-
endoglucanase SS
-
-
-
-
additional information
the enzyme Cel7D belongs to the glycoside hydrolase family 7
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
substrate binding structure analysis of Cel7D
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
4-beta-D-glucan cellobiohydrolase (reducing end)
Some exocellulases, most of which belong to the glycoside hydrolase family 48 (GH48, formerly known as cellulase family L), act at the reducing ends of cellulose and similar substrates. The CelS enzyme from Clostridium thermocellum is the most abundant subunit of the cellulosome formed by the organism. It liberates cellobiose units from the reducing end by hydrolysis of the glycosidic bond, employing an inverting reaction mechanism [2]. Different from EC 3.2.1.91, which attacks cellulose from the non-reducing end.
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
bacterial cellulose + H2O
?
-
from Acetobacter xylinum strain ATCC53582
-
-
?
additional information
?
-
substrate binding structure analysis of Cel7D
-
-
?
additional information
?
-
-
the enzyme employs reducing-end exo- and endo-mode initiation in parallel
-
-
?
NATURAL SUBSTRATE
NATURAL 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
bacterial cellulose + H2O
?
-
from Acetobacter xylinum strain ATCC53582
-
-
?
additional information
?
-
-
the enzyme employs reducing-end exo- and endo-mode initiation in parallel
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cellobioimidazole
i.e. (5R,6R,7S,8S)-6-(beta-D-glucopyranosyloxy)-5,6,7,8-tetrahydro-5-[(hydroxy)methyl]imidazol[1,2a] pyridine-7,8-diol, the disaccharide binds in the glycosyl-binding subsites +1 and +2 close to the exit of the cellulose-binding tunnel/cleft of Cel7D, binding structure analysis
lactose
the disaccharide binds in the glycosyl-binding subsites +1 and +2 close to the exit of the cellulose-binding tunnel/cleft of Cel7D, binding structure analysis
methyl (4S)-beta-cellobiosyl-4-thio-beta-cellobioside
a thio-linked substrate analogue, the disaccharide binds in the glycosyl-binding subsites +1 and +2 close to the exit of the cellulose-binding tunnel/cleft of Cel7D, binding structure analysis
cellobiose
-
strong inhibitor for the hydrolysis of 4-nitrophenyl beta-D-lactoside
additional information
-
4-nitrophenyl beta-D-lactoside (0.5 mM) does not influence the hydrolysis of cellulose
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
amorphous cellulose
-
in 50 mM sodium acetate, pH 5.0, at 30°C
-
2.6
bacterial cellulose
-
in 50 mM sodium acetate, pH 5.0, at 30°C
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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). SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 80000, SDS-PAGE, recombinant protein fused to glutathione S-transferase
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
deglycosylated Cel7D complexed with cellobiose, or with inhibitors cellobioimidazole, lactose, or methyl (4S)-beta-cellobiosyl-4-thio-beta-cellobioside, hanging drop vapour diffusion method, 18 mg/ml protein in 10 mM Tris-HCl, pH 7.0, 5 mM CaCl2, 15-22.5% PEG 5000, and 12% glycerol, soaking of crystals in ligand solution containing 10 mM ligand, X-ray diffraction structure determination and analysis at -173°C and 1.7-1.8 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ubhayasekera, W.; Munoz, I.G.; Vasella, A.; Stahlberg, J.; Mowbray, S.L.
Structures of Phanerochaete chrysosporium Cel7D in complex with product and inhibitors
FEBS J.
272
1952-1964
2005
Phanerodontia chrysosporium (Q7LIJ0)
Jalak, J.; Vaeljamaee, P.
Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis
Biotechnol. Bioeng.
106
871-883
2010
Phanerodontia chrysosporium, Trichoderma reesei
Kurasin, M.; Vaeljamaee, P.
Processivity of cellobiohydrolases is limited by the substrate
J. Biol. Chem.
286
169-177
2011
Phanerodontia chrysosporium, Trichoderma reesei, Phanerodontia chrysosporium K3
Howard, R.; Masoko, P.; Mowa, M.; Abotsi, E.; Howard, S.
Characterisation of a chimeric Phanerochaete chrysosporium cellobiohydrolase expressed from Escherichia coli
Afr. J. Biotechnol.
3
349-352
2004
Phanerodontia chrysosporium (P13860)
-
EXTERNAL LINKS (specific for EC-Number 3.2.1.176)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
