EzCatDB: S00162
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DB codeS00162
RLCP classification1.30.36210.990 : Hydrolysis
CATH domainDomain 12.70.100.10 : 1,4-Beta-D-Glucan Cellobiohydrolase I; Chain ACatalytic domain
E.C.3.2.1.4

CATH domainRelated DB codes (homologues)
2.70.100.10 : 1,4-Beta-D-Glucan Cellobiohydrolase I; Chain AD00499

Enzyme Name
UniProtKBKEGG

P56680P46237
Protein nameEndoglucanase 1Endoglucanase type Ccellulase
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 I
Endo-1,4-beta-glucanase 1
Cellulase 1
EC 3.2.1.4
Endo-1,4-beta-glucanase
Endoglucanase I
EG I
Cellulase
PfamPF00840 (Glyco_hydro_7)
[Graphical view]
PF00840 (Glyco_hydro_7)
[Graphical view]
CAZyGH7 (Glycoside Hydrolase Family)
GH7 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

UniProtKB:Accession NumberP56680P46237
Entry nameGUN1_HUMINGUNC_FUSOX
ActivityEndohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
SubunitMonomer.
Subcellular locationSecreted.
Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00760C00478C00551C00001C00760C00551


CompoundCelluloseLicheninbeta-D-GlucanH2OCellulosebeta-D-GlucanTransition-state in glycosylationGlycosyl-enzyme intermediateTransition-state in deglycosylation
TypepolysaccharidecarbohydratepolysaccharideH2Opolysaccharidepolysaccharide


ChEBI


15377





PubChem
439241
46173706
962
22247451

46173706



                 
1a39AUnboundUnboundUnbound UnboundUnbound Unbound 
1dymAUnboundUnboundUnbound UnboundUnbound Unbound 
1ojiAUnboundUnboundUnbound UnboundUnbound Unbound 
1ojjAUnboundUnboundUnbound Analogue:GAL-GLCAnalogue:GAL-BGC Unbound 
1ojjBUnboundUnboundUnbound Analogue:GAL-GLCAnalogue:GAL-BGC Unbound 
1ojkAUnboundUnboundUnbound Analogue:BGC-GLCBound:BGC-BGC Unbound 
1ojkBUnboundUnboundUnbound Analogue:BGC-GLCBound:BGC-BGC Unbound 
2a39AUnboundUnboundUnbound UnboundUnbound Unbound 
2a39BUnboundUnboundUnbound UnboundUnbound Unbound 
1ovwAAnalogue:DP5UnboundUnbound UnboundUnbound Unbound 
1ovwBAnalogue:DP5UnboundUnbound UnboundUnbound Unbound 
1ovwCAnalogue:DP5UnboundUnbound UnboundUnbound Unbound 
1ovwDAnalogue:DP5UnboundUnbound UnboundUnbound Unbound 
2ovwAUnboundUnboundUnbound Bound:CBIUnbound Unbound 
2ovwBUnboundUnboundUnbound Bound:CBIUnbound Unbound 
2ovwCUnboundUnboundUnbound Bound:CBIUnbound Unbound 
2ovwDUnboundUnboundUnbound Bound:CBIUnbound Unbound 
3ovwAUnboundUnboundUnbound UnboundUnbound Unbound 
3ovwBUnboundUnboundUnbound UnboundUnbound Unbound 
4ovwAUnboundUnboundUnbound UnboundUnbound Intermediate-analogue:IN1 
4ovwBUnboundUnboundUnbound UnboundUnbound Intermediate-analogue:IN1 

Active-site residues
resource
literature [11]
pdbCatalytic residuescomment
          
1a39AGLU 197;ASP 199;GLU 202;HIS 213
mutant S37W, P39W
1dymA       ;ASP 199;GLU 202;HIS 213
mutant E197A
1ojiA       ;ASP 199;GLU 202;HIS 213
mutant E197S
1ojjA       ;ASP 199;GLU 202;HIS 213
mutant E197S
1ojjB       ;ASP 199;GLU 202;HIS 213
mutant E197S
1ojkA       ;ASP 199;GLU 202;HIS 213
mutant E197S
1ojkB       ;ASP 199;GLU 202;HIS 213
mutant E197S
2a39AGLU 197;ASP 199;GLU 202;HIS 213
 
2a39BGLU 197;ASP 199;GLU 202;HIS 213
 
1ovwAGLU 197;ASP 199;GLU 202;HIS 213
 
1ovwBGLU 197;ASP 199;GLU 202;HIS 213
 
1ovwCGLU 197;ASP 199;GLU 202;HIS 213
 
1ovwDGLU 197;ASP 199;GLU 202;HIS 213
 
2ovwAGLU 197;ASP 199;GLU 202;HIS 213
 
2ovwBGLU 197;ASP 199;GLU 202;HIS 213
 
2ovwCGLU 197;ASP 199;GLU 202;HIS 213
 
2ovwDGLU 197;ASP 199;GLU 202;HIS 213
 
3ovwAGLU 197;ASP 199;GLU 202;HIS 213
 
3ovwBGLU 197;ASP 199;GLU 202;HIS 213
 
4ovwAGLU 197;ASP 199;GLU 202;HIS 213
 
4ovwBGLU 197;ASP 199;GLU 202;HIS 213
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]Fig.1, Fig.7, p.15284-15285
[7]Fig.1, p.5900
[8]Fig.4, p.5909-5910
[11]p.388-389
[12]Scheme 1, p.415-416
[13]Scheme 1, p.27
[14]p.1101
[15]Fig.1, p.622-624

references
[1]
JournalFEBS Lett
Year1989
Volume243
Pages239-43
AuthorsTomme P, Clayssens M
TitleIdentification of a functionally important carboxyl group in cellobiohydrolase I from Trichoderma reesei.
[2]
PubMed ID2396985
JournalBiochem J
Year1990
Volume270
Pages251-6
AuthorsClaeyssens M, van Tilbeurgh H, Kamerling JP, Berg J, Vrsanska M, Biely P
TitleStudies of the cellulolytic system of the filamentous fungus Trichoderma reesei QM 9414. Substrate specificity and transfer activity of endoglucanase I.
[3]
PubMed ID2261982
JournalFEBS Lett
Year1990
Volume275
Pages135-8
AuthorsMitsuishi Y, Nitisinprasert S, Saloheimo M, Biese I, Reinikainen T, Claeyssens M, Keranen S, Knowles JK, Teeri TT
TitleSite-directed mutagenesis of the putative catalytic residues of Trichoderma reesei cellobiohydrolase I and endoglucanase I.
[4]
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.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
Medline ID97110317
PubMed ID8952478
JournalBiochemistry
Year1996
Volume35
Pages15280-7
AuthorsSulzenbacher G, Driguez H, Henrissat B, Schulein M, Davies GJ
TitleStructure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group.
Related PDB1ovw
Related UniProtKBP46237
[6]
PubMed ID8706890
JournalFEBS Lett
Year1996
Volume390
Pages339-44
AuthorsHenriksson H, Stahlberg J, Isaksson R, Pettersson G
TitleThe active sites of cellulases are involved in chiral recognition: a comparison of cellobiohydrolase 1 and endoglucanase 1.
[7]
PubMed ID9153431
JournalBiochemistry
Year1997
Volume36
Pages5893-901
AuthorsMackenzie LF, Davies GJ, Schulein M, Withers SG
TitleIdentification of the catalytic nucleophile of endoglucanase I from Fusarium oxysporum by mass spectrometry.
[8]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID97297800
PubMed ID9153432
JournalBiochemistry
Year1997
Volume36
Pages5902-11
AuthorsSulzenbacher G, Schulein M, Davies GJ
TitleStructure of the endoglucanase I from Fusarium oxysporum: native, cellobiose, and 3,4-epoxybutyl beta-D-cellobioside-inhibited forms, at 2.3 A resolution.
Related PDB2ovw,3ovw,4ovw
Related UniProtKBP46237
[9]
PubMed ID9006908
JournalJ Biol Chem
Year1997
Volume272
Pages2709-13
AuthorsArmand S, Drouillard S, Schulein M, Henrissat B, Driguez H
TitleA bifunctionalized fluorogenic tetrasaccharide as a substrate to study cellulases.
[10]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT S37W/P39W.
Medline ID97475713
PubMed ID9335168
JournalJ Biotechnol
Year1997
Volume57
Pages91-100
AuthorsDavies GJ, Ducros V, Lewis RJ, Borchert TV, Schulein M
TitleOligosaccharide specificity of a family 7 endoglucanase: insertion of potential sugar-binding subsites.
Related PDB1a39
Related UniProtKBP56680
[11]
PubMed ID9325098
JournalJ Mol Biol
Year1997
Volume272
Pages383-97
AuthorsKleywegt GJ, Zou JY, Divne C, Davies GJ, Sinning I, Stahlberg J, Reinikainen T, Srisodsuk M, Teeri TT, Jones TA
TitleThe crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 A resolution, and a comparison with related enzymes.
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND MUTAGENESIS.
Medline ID98437137
PubMed ID9761741
JournalBiochem J
Year1998
Volume335
Pages409-16
AuthorsMacKenzie LF, Sulzenbacher G, Divne C, Jones TA, Woldike HF, Schulein M, Withers SG, Davies GJ
TitleCrystal structure of the family 7 endoglucanase I (Cel7B) from Humicola insolens at 2.2 A resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate.
Related PDB1dym,2a39
Related UniProtKBP56680
[13]
PubMed ID11336632
JournalBiochem J
Year2001
Volume356
Pages19-30
AuthorsBecker D, Braet C, Brumer H 3rd, Claeyssens M, Divne C, Fagerstrom BR, Harris M, Jones TA, Kleywegt GJ, Koivula A, Mahdi S, Piens K, Sinnott ML, Stahlberg J, Teeri TT, Underwood M, Wohlfahrt G
TitleEngineering of a glycosidase Family 7 cellobiohydrolase to more alkaline pH optimum: the pH behaviour of Trichoderma reesei Cel7A and its E223S/ A224H/L225V/T226A/D262G mutant.
[14]
PubMed ID11743726
JournalJ Mol Biol
Year2001
Volume314
Pages1097-111
AuthorsMunoz IG, Ubhayasekera W, Henriksson H, Szabo I, Pettersson G, Johansson G, Mowbray SL, Stahlberg J
TitleFamily 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 A resolution and homology models of the isozymes.
[15]
CommentsX-ray crystallography
PubMed ID12890535
JournalChem Biol
Year2003
Volume10
Pages619-28
AuthorsDucros VM, Tarling CA, Zechel DL, Brzozowski AM, Frandsen TP, von Ossowski I, Schulein M, Withers SG, Davies GJ
TitleAnatomy of glycosynthesis: structure and kinetics of the Humicola insolens Cel7B E197A and E197S glycosynthase mutants.
Related PDB1oji,1ojj,1ojk

comments
This enzyme belongs to the glycosidase family-7.
According to the literature [7], [8], [11], [12] & [14], the catalytic reaction proceeds as follows:
(0) Asp199 modulates the pKa of Glu197, which is a nucleophile. His213 modulates these residues, Asp199 and Glu197.
(1) Glu202 acts as a general acid, to protonate the leaving group, through a water molecule, to give an oxacarbenium ion-like transition state. (SN1-like reaction)
(2) Glu197 makes a nucleophilic attack on the C2 atom of the transition-state, to form a glycosyl-enzyme intermediate.
(3) Glu202 acts as a general base, to activate the water.
(4) The activated water makes a nucleophilic attack on the intermediate, through an oxacarbenium ion-like transition-state, to complete the hydrolysis.

createdupdated
2004-03-222009-02-26


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Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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