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Information on EC 3.2.1.176 - cellulose 1,4-beta-cellobiosidase (reducing end) and Organism(s) Clostridium cellulovorans and UniProt Accession O65986

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EC Tree
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.
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Clostridium cellulovorans
UNIPROT: O65986
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The taxonomic range for the selected organisms is: Clostridium cellulovorans
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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2
cellohexaose
+
2
H2O
=
2
cellotriose
+
cellotetraose
+
cellobiose
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, cellobiohydrolase cels, 1,4-beta-d-glucan cellobiohydrolase i, 1,4-beta-d-glucan-cellobiohydrolase i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cel48A
-
-
-
-
cellobiohydrolase CelS
-
-
-
-
Cellulase SS
-
-
-
-
celS
-
-
-
-
CelSS
-
-
-
-
endoglucanase SS
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O65986_CLOCL
727
0
80486
TrEMBL
Secretory Pathway (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures in complex with cellobiose, cellotetraose and triethylene glycol molecules. The product cellobiose occupies subsites +1 and +2 in the open active-site cleft of the enzyme-cellotetraose complex structure, and three triethylene glycol molecules and one pentaethylene glycol molecule are located at active-site subsites -2 to -6 in the structure of the ExgS-triethylene glycol complex. Glu50 acts as a proton donor and Asp222 plays a nucleophilic role
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsai, L.C.; Amiraslanov, I.; Chen, H.R.; Chen, Y.W.; Lee, H.; Liang, P.H.; Liaw, Y.C.
Structures of exoglucanase from Clostridium cellulovorans: cellotetraose binding and cleavage
Acta Crystallogr. Sect. F
71
1264-1272
2015
Clostridium cellulovorans (O65986), Clostridium cellulovorans
Manually annotated by BRENDA team