Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.1.176 - cellulose 1,4-beta-cellobiosidase (reducing end) and Organism(s) Thermoclostridium stercorarium and UniProt Accession P50900

for references in articles please use BRENDA:EC3.2.1.176
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Thermoclostridium stercorarium
UNIPROT: P50900
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Thermoclostridium stercorarium
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
recombination of the catalytic domains of three glycoside hydrolase family 48 bacterial cellulases (Cel48), i.e. Clostridium cellulolyticum CelF, Clostridium stercorarium CelY, and Clostridium thermocellum CelS, to create a diverse library of Cel48 enzymes with an average of 106 mutations from the closest native enzyme. The library is based on the Clostridium thermocellum CelS architecture, which consists of a 70-kDa catalytic domain connected to the organism's respective dockerin domain. Large variations in properties such as the functional temperature range, stability, and specific activity on crystalline cellulose are found. Functional status and stability are predictable from simple linear models of the sequence-property data. Recombined protein fragments contribute additively to these properties in a given chimera
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Smith, M.A.; Rentmeister, A.; Snow, C.D.; Wu, T.; Farrow, M.F.; Mingardon, F.; Arnold, F.H.
A diverse set of family 48 bacterial glycoside hydrolase cellulases created by structure-guided recombination
FEBS J.
279
4453-4465
2012
Acetivibrio thermocellus (A3DH67), Thermoclostridium stercorarium (P50900), Acetivibrio thermocellus DSM 1237 (A3DH67), Thermoclostridium stercorarium DSM 8532 (P50900)
Manually annotated by BRENDA team