EzCatDB: S00150
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DB codeS00150
RLCP classification1.30.36211.992 : Hydrolysis
CATH domainDomain 12.60.120.180 : Jelly RollsCatalytic domain
E.C.3.2.1.4

CATH domainRelated DB codes (homologues)
2.60.120.180 : Jelly RollsS00533,S00151,D00504,D00538

Enzyme Name
UniProtKBKEGG

O33897O00095Q8NJY3Q8NJY6
Protein name



cellulase
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
SynonymsCellulase
EC 3.2.1.4
Endo-beta-1,4-glucanase (Beta-1,4-glucanase)
EC 3.2.1.4
Endoglucanase
Endoglucanase
PfamPF01670 (Glyco_hydro_12)
[Graphical view]
PF01670 (Glyco_hydro_12)
[Graphical view]
PF01670 (Glyco_hydro_12)
[Graphical view]
PF01670 (Glyco_hydro_12)
[Graphical view]
CAZyGH12 (Glycoside Hydrolase Family)
GH12 (Glycoside Hydrolase Family)
GH12 (Glycoside Hydrolase Family)
GH12 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

UniProtKB:Accession NumberO33897O00095Q8NJY3Q8NJY6
Entry nameO33897_RHOMRO00095_TRIREQ8NJY3_9ASCOQ8NJY6_9HYPO
Activity



Subunit



Subcellular location



Cofactor




Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00760C00478C00551C00001C00760C00551

CompoundCelluloseLicheninbeta-D-GlucanH2OCellulosebeta-D-GlucanTransition-state for glycosylated enzymeGlycosylated enzyme intermediate
TypepolysaccharidecarbohydratepolysaccharideH2Opolysaccharidepolysaccharide

ChEBI


15377




PubChem
439241
46173706
962
22247451

46173706


                
1h0bAUnboundUnboundUnbound UnboundUnbound  
1h0bBUnboundUnboundUnbound UnboundUnbound  
2bw8AUnboundUnboundUnbound UnboundUnbound  
2bw8BUnboundUnboundUnbound UnboundUnbound  
2bwaAUnboundUnboundUnbound Bound:GLC-BGC-BGCUnbound  
2bwaBUnboundUnboundUnbound Bound:GLC-BGCUnbound  
2bwcAUnboundUnboundUnbound Bound:GLC-BGC-BGCUnbound  
2bwcBBound:GLC-BGC-BGC-BGCUnboundUnbound Bound:BGC-BGC-BGCUnbound  
1h8vAUnboundUnboundUnbound UnboundUnbound  
1h8vBUnboundUnboundUnbound UnboundUnbound  
1h8vCUnboundUnboundUnbound UnboundUnbound  
1h8vDUnboundUnboundUnbound UnboundUnbound  
1h8vEUnboundUnboundUnbound UnboundUnbound  
1h8vFUnboundUnboundUnbound UnboundUnbound  
1oa2AUnboundUnboundUnbound UnboundUnbound  
1oa2BUnboundUnboundUnbound UnboundUnbound  
1oa2CUnboundUnboundUnbound UnboundUnbound  
1oa2DUnboundUnboundUnbound UnboundUnbound  
1oa2EUnboundUnboundUnbound UnboundUnbound  
1oa2FUnboundUnboundUnbound UnboundUnbound  
1olqAUnboundUnboundUnbound UnboundUnbound  
1olqBUnboundUnboundUnbound UnboundUnbound  
1olrAUnboundUnboundUnbound UnboundUnbound  
1uu4AUnboundUnboundUnbound UnboundBound:BGC-BGC  
1uu5AUnboundUnboundUnbound Bound:BGC-BGC-BGC-BGCUnbound  
1uu6ABound:BGC-BGC-BGC-BGCUnboundUnbound UnboundUnbound  
1w2uABound:BGC-BGC-BGC-BGCUnboundUnbound UnboundUnbound  
1oa3AUnboundUnboundUnbound UnboundUnbound  
1oa3BUnboundUnboundUnbound UnboundUnbound  
1oa3CUnboundUnboundUnbound UnboundUnbound  
1oa3DUnboundUnboundUnbound UnboundUnbound  

Active-site residues
resource
literature [2], [3], [5], [7]
pdbCatalytic residues
         
1h0bAASN 102;ASP 106;GLU 124;GLU 207
1h0bBASN 102;ASP 106;GLU 124;GLU 207
2bw8AASN 102;ASP 106;GLU 124;GLU 207
2bw8BASN 102;ASP 106;GLU 124;GLU 207
2bwaAASN 102;ASP 106;GLU 124;GLU 207
2bwaBASN 102;ASP 106;GLU 124;GLU 207
2bwcAASN 102;ASP 106;GLU 124;GLU 207
2bwcBASN 102;ASP 106;GLU 124;GLU 207
1h8vAASN  95;ASP  99;GLU 116;GLU 200
1h8vBASN  95;ASP  99;GLU 116;GLU 200
1h8vCASN  95;ASP  99;GLU 116;GLU 200
1h8vDASN  95;ASP  99;GLU 116;GLU 200
1h8vEASN  95;ASP  99;GLU 116;GLU 200
1h8vFASN  95;ASP  99;GLU 116;GLU 200
1oa2AASN  95;ASP  99;GLU 116;GLU 200
1oa2BASN  95;ASP  99;GLU 116;GLU 200
1oa2CASN  95;ASP  99;GLU 116;GLU 200
1oa2DASN  95;ASP  99;GLU 116;GLU 200
1oa2EASN  95;ASP  99;GLU 116;GLU 200
1oa2FASN  95;ASP  99;GLU 116;GLU 200
1olqAASN  95;ASP  99;GLU 116;GLU 200
1olqBASN  95;ASP  99;GLU 116;GLU 200
1olrAASN  99;ASP 103;GLU 120;GLU 205
1uu4AASN  99;ASP 103;GLU 120;GLU 205
1uu5AASN  99;ASP 103;GLU 120;GLU 205
1uu6AASN  99;ASP 103;GLU 120;GLU 205
1w2uAASN  99;ASP 103;GLU 120;GLU 205
1oa3AASN  95;ASP  99;GLU 116;GLU 200
1oa3BASN  95;ASP  99;GLU 116;GLU 200
1oa3CASN  95;ASP  99;GLU 116;GLU 200
1oa3DASN  95;ASP  99;GLU 116;GLU 200

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.16037-16038
[3]Scheme 1, p.139-140
[4]p.301
[6]p.888-889
[9]p.1510-1511
[11]Fig.2, p.252-254
[12]p.63-64, p.67

references
[1]
PubMed ID8477842
JournalFEBS Lett
Year1993
Volume321
Pages135-9
AuthorsTorronen A, Kubicek CP, Henrissat B
TitleAmino acid sequence similarities between low molecular weight endo-1,4-beta-xylanases and family H cellulases revealed by clustering analysis.
[2]
PubMed ID9440876
JournalBiochemistry
Year1997
Volume36
Pages16032-9
AuthorsSulzenbacher G, Shareck F, Morosoli R, Dupont C, Davies GJ
TitleThe Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, expression, and X-ray structure at 1.75 A resolution.
[3]
PubMed ID9806895
JournalBiochem J
Year1998
Volume336
Pages139-45
AuthorsZechel DL, He S, Dupont C, Withers SG
TitleIdentification of Glu-120 as the catalytic nucleophile in Streptomyces lividans endoglucanase celB.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 17-234.
PubMed ID11327768
JournalJ Mol Biol
Year2001
Volume308
Pages295-310
AuthorsSandgren M, Shaw A, Ropp TH, Wu S, Bott R, Cameron AD, Stahlberg J, Mitchinson C, Jones TA
TitleThe X-ray crystal structure of the Trichoderma reesei family 12 endoglucanase 3, Cel12A, at 1.9 A resolution.
Related PDB1h8v
Related UniProtKBO00095
[5]
PubMed ID12073090
JournalCurr Genet
Year2002
Volume41
Pages89-98
AuthorsGoedegebuur F, Fowler T, Phillips J, van der Kley P, van Solingen P, Dankmeyer L, Power SD
TitleCloning and relational analysis of 15 novel fungal endoglucanases from family 12 glycosyl hydrolase.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 38-260.
PubMed ID12095262
JournalJ Mol Biol
Year2002
Volume320
Pages883-97
AuthorsCrennell SJ, Hreggvidsson GO, Nordberg Karlsson E
TitleThe structure of Rhodothermus marinus Cel12A, a highly thermostable family 12 endoglucanase, at 1.8 A resolution.
Related PDB1h0b
Related UniProtKBO33897
[7]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 17-234.
PubMed ID14627738
JournalProtein Sci
Year2003
Volume12
Pages2782-93
AuthorsSandgren M, Gualfetti PJ, Paech C, Paech S, Shaw A, Gross LS, Saldajeno M, Berglund GI, Jones TA, Mitchinson C
TitleThe Humicola grisea Cel12A enzyme structure at 1.2 A resolution and the impact of its free cysteine residues on thermal stability.
Related PDB1olr,1olq
Related UniProtKBO00095,Q8NJY3
[8]
CommentsX-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 17-234.
PubMed ID12649442
JournalProtein Sci
Year2003
Volume12
Pages848-60
AuthorsSandgren M, Gualfetti PJ, Shaw A, Gross LS, Saldajeno M, Day AG, Jones TA, Mitchinson C
TitleComparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability.
Related PDB1oa2,1oa3
Related UniProtKBO00095
[9]
CommentsX-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 31-254.
PubMed ID15364577
JournalJ Mol Biol
Year2004
Volume342
Pages1505-17
AuthorsSandgren M, Berglund GI, Shaw A, Stahlberg J, Kenne L, Desmet T, Mitchinson C
TitleCrystal complex structures reveal how substrate is bound in the -4 to the +2 binding sites of Humicola grisea Cel12A.
Related PDB1uu4,1uu5,1uu6,1w2u
Related UniProtKBQ8NJY3,Q8NJY6
[10]
PubMed ID15456402
JournalBiochem J
Year2005
Volume385
Pages581-8
AuthorsHuang Y, Krauss G, Cottaz S, Driguez H, Lipps G
TitleA highly acid-stable and thermostable endo-beta-glucanase from the thermoacidophilic archaeon Sulfolobus solfataricus.
[11]
PubMed ID15950056
JournalProg Biophys Mol Biol
Year2005
Volume89
Pages246-91
AuthorsSandgren M, Stahlberg J, Mitchinson C
TitleStructural and biochemical studies of GH family 12 cellulases: improved thermal stability, and ligand complexes.
[12]
CommentsX-ray crystallography
PubMed ID16343530
JournalJ Mol Biol
Year2006
Volume356
Pages57-71
AuthorsCrennell SJ, Cook D, Minns A, Svergun D, Andersen RL, Nordberg Karlsson E
TitleDimerisation and an increase in active site aromatic groups as adaptations to high temperatures: X-ray solution scattering and substrate-bound crystal structures of Rhodothermus marinus endoglucanase Cel12A.
Related PDB2bw8,2bwa,2bwc

comments
This family belongs to glycosidase family-12, which has a retaining mechanism.
The catalytic domain of this enzyme is homologous to those of another cellulase (S00533 in EzCatDB) and beta-1,4-Glucanase (D00504 in EzCatDB), whose catalytic mechanisms must be similar to that of this enzyme.
According to the literature [2], [3] & [7], the catalytic reaction proceeds as follows:
(1) Asn102 (of 1h0b) may modulate the activity of Glu207 as a acid-base.
(2) Glu207 (of 1h0b) acts as a general acid to protonate the leaving oxygen atom, leading to a oxocarbenium-like transtion state from cellulose substrate.
(3) pKa of Glu124 (of 1h0b), which acts as a nucleophile, is modulated by Asp106.
(4) Glu124 makes a nucleophilic attack on C1 atom of the transition state, forming a glycosyl-enzyme intermediate.
(5) Glu207 acts as a general base to activate a water molecule.
(6) The activated water makes a nucleophilic attack on the C1 atom of the intermediate. This reaction proceeds through an oxocarbenium-like transition state to complete the hydrolysis.

createdupdated
2004-05-172009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
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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