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Information on EC 3.2.1.B42 - cellulose 1,4-beta-cellotetraosidase (non-reducing end) and Organism(s) Thermobifida fusca and UniProt Accession P26221

for references in articles please use BRENDA:EC3.2.1.B42
preliminary BRENDA-supplied EC number
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Thermobifida fusca
UNIPROT: P26221 not found.
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The taxonomic range for the selected organisms is: Thermobifida fusca
The expected taxonomic range for this enzyme is: Thermobifida fusca
Reaction Schemes
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processive hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, releasing cellotetraose from the non-reducing ends of the glucan chains
Synonyms
Cel9A, CelD, E4, endo/exoglucosidase, non-reducing end acting processive exocellulase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
endo/exoglucosidase
misleading
non-reducing end acting processive exocellulase
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SYSTEMATIC NAME
IUBMB Comments
4-beta-D-glucan cellotetraosylhydrolase (non-reducing end)
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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
bacterial cellulose + H2O
cellotetraose + ?
show the reaction diagram
-
-
-
?
carboxymethyl cellulose + H2O
cellotetraose + ?
show the reaction diagram
-
-
-
?
cellulose + H2O
cellotetraose + ?
show the reaction diagram
bacterial microcrystalline cellulose
-
-
?
filter paper + H2O
cellotetraose + ?
show the reaction diagram
-
-
-
?
swollen cellulose paper + H2O
cellotetraose + ?
show the reaction diagram
-
-
-
?
additional information
?
-
substrate is fixed at the nonreducing end, and the fixation acts as a measuring stick, resulting in cleavage products that are not any longer than cellotetraose, whereas the remaining chain is held in place by the C-terminal CBM and is fed to the active-site in a processive manner
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GUN4_THEFU
880
1
95203
Swiss-Prot
Chloroplast (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90400
calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 90400, calculated from sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparative in silico analysis of modular architecture. Substrate is fixed at the nonreducing end, and the fixation acts as a measuring stick, resulting in cleavage products that are not any longer than cellotetraose, whereas the remaining chain is held in place by the C-terminal CBM and is fed to the active-site in a processive manner
structure of a mutant lacking the family II cellulose binding domain, to 1.9 A resolution. The fragment contains both a family 9 catalytic domain, exhibiting an (alpha/alpha)6 barrel fold, and a family III cellulose binding domain, having an antiparallel beta-sandwich fold. The catalytic and cellulose binding domains interact. Upon binding of cellopentaose, cellotriose and cellobiose conformational changes occur
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D55C
mutation in proposed catalytic site, low activity, mutant is able to bind bacterial microcrystalline cellulose
additional information
Removal of the internal family IIIc CBD decreases activity markedly on every substrate. Constructs which lack the family IIIc CBD have almost no activity on bacterial microcrystalline cellulose
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56
16 h, 50% of the activity is retained for constructions lacking the type IIIc CBD
63
16 h, 50% of the activity is retained for constructions containing the type IIIc CBD
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Streptomyces lividans and Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kostylev, M.; Wilson, D.
A distinct model of synergism between a processive endocellulase (TfCel9A) and an exocellulase (TfCel48A) from Thermobifida fusca
Appl. Environ. Microbiol.
80
339-44
2014
Thermobifida fusca (P26221)
Manually annotated by BRENDA team
Guerriero, G.; Sergeant, K.; Legay, S.; Hausman, J.F.; Cauchie, H.M.; Ahmad, I.; Siddiqui, K.S.
Novel insights from comparative in silico analysis of green microalgal cellulases
Int. J. Mol. Sci.
19
E1782
2018
Thermobifida fusca (P26221)
Manually annotated by BRENDA team
Irwin, D.; Shin,D.-H.; Zhang, S.; Barr,b.K.; Sakon,j.; Karplus, P.A.; Wilson, D.B.
Roles of the catalytic domain and two cellulose binding domains of Thermomonospora fusca E4 in cellulose hydrolysis
J. Bacteriol.
180
1709-1714
1998
Thermobifida fusca (P26221)
Manually annotated by BRENDA team
Sakon, J; Irwin, D.; Wilson, D.B.; Karplus, P.A.
Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca
Nat. Struct. Biol.
4
810-818
1997
Thermobifida fusca (P26221)
Manually annotated by BRENDA team