EzCatDB: S00125
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DB codeS00125
RLCP classification1.30.5100.2 : Hydrolysis
CATH domainDomain 12.40.40.10 : Barwin-like endoglucanasesCatalytic domain
E.C.3.2.1.4
CSA2eng


Enzyme Name
UniProtKBKEGG

P43316
Protein nameEndoglucanase-5cellulase
endo-1,4-beta-D-glucanase
beta-1,4-glucanase
beta-1,4-endoglucan hydrolase
celluase A
cellulosin AP
endoglucanase D
alkali cellulase
cellulase A 3
celludextrinase
9.5 cellulase
avicelase
pancellase SS
1,4-(1,3
1,4)-beta-D-glucan 4-glucanohydrolase
SynonymsEC 3.2.1.4
Endoglucanase V
Endo-1,4-beta-glucanase V
EG V
Cellulase V
PfamPF02015 (Glyco_hydro_45)
[Graphical view]
CAZyGH45 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

UniProtKB:Accession NumberP43316
Entry nameGUN5_HUMIN
ActivityEndohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00760C00001C00760C00185
CompoundCelluloseH2OCelluloseCellobiose
TypepolysaccharideH2Opolysaccharidepolysaccharide
ChEBI
15377

17057
PubChem
962
22247451

439178
            
1hd5AUnbound UnboundUnbound
2engAUnbound UnboundUnbound
3engAUnbound UnboundBound:CBI
4engAUnbound Analogue:CTR 1Analogue:CTR 1

Active-site residues
resource
Swiss-prot;P43316
pdbCatalytic residuescomment
          
1hd5AASP 10;ASP 122
 
2engAASP 10;ASP 121
 
3engAASP 10;ASP 121
 
4engA      ;ASP 121
mutation D10N

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.364
[3]p.224-225
[4]Fig.5, Fig.9, p.16218-16220
[5]p.14-16

references
[1]
PubMed ID8223652
JournalEur J Biochem
Year1993
Volume217
Pages947-53
AuthorsSchou C, Rasmussen G, Kaltoft MB, Henrissat B, Schulein M
TitleStereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
Medline ID93390621
PubMed ID8377830
JournalNature
Year1993
Volume365
Pages362-4
AuthorsDavies GJ, Dodson GG, Hubbard RE, Tolley SP, Dauter Z, Wilson KS, Hjort C, Mikkelsen JM, Rasmussen G, Schulein M
TitleStructure and function of endoglucanase V.
Related UniProtKBP43316
[3]
PubMed ID7984103
JournalMol Microbiol
Year1994
Volume13
Pages219-28
AuthorsSaloheimo A, Henrissat B, Hoffren AM, Teleman O, Penttila M
TitleA novel, small endoglucanase gene, egl5, from Trichoderma reesei isolated by expression in yeast.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID96101453
PubMed ID8519779
JournalBiochemistry
Year1995
Volume34
Pages16210-20
AuthorsDavies GJ, Tolley SP, Henrissat B, Hjort C, Schulein M
TitleStructures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9 A resolution.
Related UniProtKBP43316
[5]
CommentsX-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
JournalActa Crystallogr D Biol Crystallogr
Year1996
Volume52
Pages7-17
AuthorsDavies GJ, Dodson GG, Moore MH, Tolley SP, Dauter Z, Wilson KS, Rasmussen G, Schuelein M
TitleStructure determination and refinement of the Humicola insolens endoglucanase V at 1.5-A resolution.
Related PDB2eng,3eng,4eng
Related UniProtKBP43316
[6]
PubMed ID10424462
JournalElectrophoresis
Year1999
Volume20
Pages1403-11
AuthorsAttanasio F, Bruschi M, Candiano G, Galletto R, Musante L, Schulein M, Rialdi G
TitleAnalytical titration curves of glycosyl hydrolase Cel45 by combined isoelectric focusing-electrophoresis.
[7]
PubMed ID10368289
JournalStructure Fold Des
Year1999
Volume7
Pages227-36
AuthorsCastillo RM, Mizuguchi K, Dhanaraj V, Albert A, Blundell TL, Murzin AG
TitleA six-stranded double-psi beta barrel is shared by several protein superfamilies.
[8]
PubMed ID11807269
JournalActa Crystallogr D Biol Crystallogr
Year2002
Volume58
Pages336-8
AuthorsHirvonen M, Papageorgiou AC
TitleCrystallization and preliminary crystallographic analysis of a family 45 endoglucanase from the thermophilic fungus Melanocarpus albomyces.

comments
This enzyme belongs to the glycosyl hydrolase family-45, with an inverting mechanism.
According to the literature [2], [4] & [5], Asp10 and Asp121 act as a general base and a general acid, respectively. According to the literature [4], the hydrolysis of glycosidic bond proceeds via a transition state with an oxocarbonium ion character, suggesting an SN1-like reaction, as follows:
(1) Asp121 acts as a general acid to protonate the glycosidic oxygen.
(2) Asp10 acts as a general base, which activates a solvent water molecule.
(3) The activated water makes a nucleophilic attack on the glycosidic carbon atom (C1 atom). This reaction occurs via a transition-state with an elongated glycosidic bond, suggesting an SN1-like (dissociative) mechanism.
(4) Finally, sugar product with an inverted configuration at C1 atom is formed.

createdupdated
2004-03-192009-03-17


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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