EzCatDB: D00499

DB codeD00499
CATH domainDomain 12.70.100.10Catalytic domain
Domain 22.-.-.-
E.C.3.2.1.91
CSA1cel

CATH domainRelated DB codes (homologues)
2.70.100.10S00162

Enzyme Name
Swiss-protKEGG

P62694Q09431Q7LIJ0Q8TFL9
Protein nameExoglucanase 1


cellulose 1,4-beta-cellobiosidase
exo-cellobiohydrolase
beta-1,4-glucan cellobiohydrolase
beta-1,4-glucan cellobiosylhydrolase
1,4-beta-glucan cellobiosidase
exoglucanase
avicelase
CBH 1
C1 cellulase
cellobiohydrolase I
cellobiohydrolase
exo-beta-1,4-glucan cellobiohydrolase
1,4-beta-D-glucan cellobiohydrolase
cellobiosidase
SynonymsEC 3.2.1.91
Exoglucanase I
Exocellobiohydrolase I
CBHI
1,4-beta-cellobiohydrolase
Cellulase
EC 3.2.1.91
Major cellobiohydrolase (Cellulase)
EC 3.2.1.91
Cellobiohydrolase I catalytic domain (Cellobiohydrolase 1 catalytic domain)
EC 3.2.1.91

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

Swiss-prot:Accession NumberP62694Q09431Q7LIJ0Q8TFL9
Entry nameGUX1_TRIREQ09431_PHACHQ7LIJ0_PHACHQ8TFL9_TALEM
ActivityHydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non- reducing ends of the chains.


Subunit



Subcellular locationSecreted.


Cofactor





SubstratesProducts
KEGG-idC00760C02013C00001C00185C00760
CompoundCelluloseCellotetraoseH2OCellobioseCellulose
TypepolysaccharidepolysaccharideH2Opolysaccharidepolysaccharide
1celAUnboundUnbound
Analogue:IBZ-GLCUnbound
1celBUnboundUnbound
Analogue:IBZ-GLCUnbound
1dy4AUnboundUnbound
Analogue:SNPUnbound
1egnAUnboundUnbound
UnboundUnbound
1q2bAUnboundUnbound
UnboundUnbound
1q2eAUnboundUnbound
Analogue:MGL-SGC-GLC-GLCUnbound
1q2eBUnboundUnbound
Analogue:MGL-SGC-GLC-GLCUnbound
2celAUnboundUnbound
UnboundUnbound
2celBUnboundUnbound
UnboundUnbound
3celAUnboundUnbound
Bound:GLC-GLCUnbound
4celAUnboundUnbound
UnboundUnbound
4celBUnboundUnbound
UnboundUnbound
5celAUnboundBound:GLC-GLC-GLC-GLC 455
UnboundUnbound
6celAUnboundUnbound
Analogue:GLC-GLC-GLC-GLCBound:GLC-GLC-GLC-GLC-GLC
7celAUnboundUnbound
Bound:GLC-GLCBound:GLC-GLC-GLC-GLC-GLC-GLC
1gpiAUnboundUnbound
UnboundUnbound
1h46XUnboundUnbound
UnboundUnbound
1z3tAUnboundUnbound
Bound:CBIUnbound
1z3vAUnboundUnbound
Analogue:LATUnbound
1z3wAUnboundUnbound
Analogue:IDCUnbound
1q9hAUnboundUnbound
UnboundUnbound
1az6AUnboundUnbound
UnboundUnbound
1azhAUnboundUnbound
UnboundUnbound
1azkAUnboundUnbound
UnboundUnbound
1cbhAUnboundUnbound
UnboundUnbound
2cbhAUnboundUnbound
UnboundUnbound

Active-site residues
resource
literature [14], [18]
pdbCatalytic residuescomment
1celAGLU 212;ASP 214;GLU 217;HIS 228

1celBGLU 212;ASP 214;GLU 217;HIS 228

1dy4AGLU 212;ASP 214;GLU 217;HIS 228

1egnAGLU 212;ASP 214;GLU 217;HIS 228
mutant E223S,A224H,L225V,T226A,D262G
1q2bAGLU 212;ASP 214;GLU 217;HIS 228
mutant D241C,D249C
1q2eAGLU 212;ASP 214;GLU 217;HIS 228
mutant deletion 245-252
1q2eBGLU 212;ASP 214;GLU 217;HIS 228
mutant deletion 245-252
2celA       ;ASP 214;GLU 217;HIS 228
mutant E212Q
2celB       ;ASP 214;GLU 217;HIS 228
mutant E212Q
3celA       ;ASP 214;GLU 217;HIS 228
mutant E212Q
4celAGLU 212;       ;GLU 217;HIS 228
mutant D214N
4celBGLU 212;       ;GLU 217;HIS 228
mutant D214N
5celA       ;ASP 214;GLU 217;HIS 228
mutant E212Q
6celA       ;ASP 214;GLU 217;HIS 228
mutant E212Q
7celAGLU 212;ASP 214;       ;HIS 228
mutant E217Q
1gpiAGLU 207;ASP 209;GLU 212;HIS 223

1h46XGLU 207;ASP 209;GLU 212;HIS 223

1z3tAGLU 207;ASP 209;GLU 212;HIS 223

1z3vAGLU 207;ASP 209;GLU 212;HIS 223

1z3wAGLU 207;ASP 209;GLU 212;HIS 223

1q9hAGLU 209;ASP 211;GLU 214;HIS 225

1az6A
mutant Y5A,Y31A,Y32A
1azhA
mutant Y5A,Y31A,Y32A
1azkA
mutant Y5A,Y31A,Y32A
1cbhA
mutant E126Q,D130N,D132A
2cbhA


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[8]p.887
[14]p.526
[17]p.342-344
[21]Scheme 1
[23]p.317-319
[25]Scheme 1
[26]p.1101
[27]p.88
[34]p.1960

references
[1]
PubMed ID3178831
JournalBiochem Biophys Res Commun
Year1988
Volume156
Pages180-5
AuthorsAbuja PM, Pilz I, Claeyssens M, Tomme P
TitleDomain structure of cellobiohydrolase II as studied by small angle X-ray scattering: close resemblance to cellobiohydrolase I.
[2]
PubMed ID2597150
JournalBiochem Biophys Res Commun
Year1989
Volume165
Pages615-23
AuthorsAbuja PM, Pilz I, Tomme P, Claeyssens M
TitleStructural changes in cellobiohydrolase I upon binding of a macromolecular ligand as evident by SAXS investigations.
[3]
CommentsSTRUCTURE BY NMR OF 478-513.
Medline ID90057416
PubMed ID2554967
JournalBiochemistry
Year1989
Volume28
Pages7241-57
AuthorsKraulis J, Clore GM, Nilges M, Jones TA, Pettersson G, Knowles J, Gronenborn AM
TitleDetermination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing.
Related PDB1cbh,2cbh
Related Swiss-protP62694
[4]
CommentsACTIVE SITE
JournalFEBS Lett
Year1989
Volume243
Pages239-43
AuthorsTomme P, Clayssens M
TitleIdentification of a functionally important carboxyl group in cellobiohydrolase I from Trichoderma reesei.
Related Swiss-protP62694
[5]
PubMed ID2332056
JournalFEBS Lett
Year1990
Volume263
Pages89-92
AuthorsClaeyssens M, Tomme P, Brewer CF, Hehre EJ
TitleStereochemical course of hydrolysis and hydration reactions catalysed by cellobiohydrolases I and II from Trichoderma reesei.
[6]
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.
[7]
PubMed ID1567377
JournalBiochem J
Year1992
Volume283
Pages31-4
AuthorsBrooks MM, Tuohy MG, Savage AV, Claeyssens M, Coughlan MP
TitleThe stereochemical course of reactions catalysed by the cellobiohydrolases produced by Talaromyces emersonii.
[8]
PubMed ID8489514
JournalBiochem J
Year1993
Volume291
Pages883-8
AuthorsKonstantinidis AK, Marsden I, Sinnott ML
TitleHydrolyses of alpha- and beta-cellobiosyl fluorides by cellobiohydrolases of Trichoderma reesei.
[9]
PubMed ID8252556
JournalCarbohydr Res
Year1993
Volume249
Pages77-90
AuthorsMcCarter JD, Adam MJ, Braun C, Namchuk M, Tull D, Withers SG
TitleSyntheses of 2-deoxy-2-fluoro mono- and oligo-saccharide glycosides from glycals and evaluation as glycosidase inhibitors.
[10]
PubMed ID8407900
JournalJ Biol Chem
Year1993
Volume268
Pages20756-61
AuthorsSrisodsuk M, Reinikainen T, Penttila M, Teeri TT
TitleRole of the interdomain linker peptide of Trichoderma reesei cellobiohydrolase I in its interaction with crystalline cellulose.
[11]
PubMed ID8254686
JournalJ Mol Biol
Year1993
Volume234
Pages905-7
AuthorsDivne C, Sinning I, Stahlberg J, Pettersson G, Bailey M, Siika-aho M, Margolles-Clark E, Teeri T, Jones TA
TitleCrystallization and preliminary X-ray studies on the core proteins of cellobiohydrolase I and endoglucanase I from Trichoderma reesei.
[12]
PubMed ID8037459
JournalArch Biochem Biophys
Year1994
Volume312
Pages459-66
AuthorsEvans BR, Margalit R, Woodward J
TitleVeratryl alcohol oxidase activity of a chemically modified cellulase protein.
[13]
PubMed ID8192865
JournalBiotechnol Appl Biochem
Year1994
Volume19
Pages141-53
AuthorsWoodward J, Brown JP, Evans BR, Affholter KA
TitlePapain digestion of crude Trichoderma reesei cellulase: purification and properties of cellobiohydrolase I and II core proteins.
[14]
CommentsX-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 18-452.
Medline ID94310436
PubMed ID8036495
JournalScience
Year1994
Volume265
Pages524-8
AuthorsDivne C, Stahlberg J, Reinikainen T, Ruohonen L, Pettersson G, Knowles JK, Teeri TT, Jones TA
TitleThe three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei.
Related PDB1cel
Related Swiss-protP62694
[15]
PubMed ID7549870
JournalProtein Sci
Year1995
Volume4
Pages1056-64
AuthorsLinder M, Mattinen ML, Kontteli M, Lindeberg G, Stahlberg J, Drakenberg T, Reinikainen T, Pettersson G, Annila A
TitleIdentification of functionally important amino acids in the cellulose-binding domain of Trichoderma reesei cellobiohydrolase I.
[16]
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.
[17]
CommentsX-ray crystallography
PubMed ID8951380
JournalJ Mol Biol
Year1996
Volume264
Pages337-49
AuthorsStahlberg J, Divne C, Koivula A, Piens K, Claeyssens M, Teeri TT, Jones TA
TitleActivity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei.
Related PDB2cel,3cel,4cel
[18]
PubMed ID9449766
JournalCarbohydr Res
Year1997
Volume304
Pages143-54
AuthorsKlarskov K, Piens K, Stahlberg J, Hoj PB, Beeumen JV, Claeyssens M
TitleCellobiohydrolase I from Trichoderma reesei: identification of an active-site nucleophile and additional information on sequence including the glycosylation pattern of the core protein.
[19]
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.
[20]
CommentsSTRUCTURE BY NMR OF 478-513.
Medline ID97194052
PubMed ID9041630
JournalProtein Sci
Year1997
Volume6
Pages294-303
AuthorsMattinen ML, Kontteli M, Kerovuo J, Linder M, Annila A, Lindeberg G, Reinikainen T, Drakenberg T
TitleThree-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei.
Related PDB1az6,1azh,1azj,1azk
Related Swiss-protP62694
[21]
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.
[22]
PubMed ID9760165
JournalEur J Biochem
Year1998
Volume256
Pages279-86
AuthorsMattinen ML, Linder M, Drakenberg T, Annila A
TitleSolution structure of the cellulose-binding domain of endoglucanase I from Trichoderma reesei and its interaction with cello-oligosaccharides.
[23]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 18-452.
Medline ID98128795
PubMed ID9466911
JournalJ Mol Biol
Year1998
Volume275
Pages309-25
AuthorsDivne C, Stahlberg J, Teeri TT, Jones TA
TitleHigh-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei.
Related PDB5cel,6cel,7cel
Related Swiss-protP62694
[24]
PubMed ID9989594
JournalFEBS Lett
Year1999
Volume443
Pages149-53
AuthorsHarjunpaa V, Helin J, Koivula A, Siika-aho M, Drakenberg T
TitleA comparative study of two retaining enzymes of Trichoderma reesei: transglycosylation of oligosaccharides catalysed by the cellobiohydrolase I, Cel7A, and the beta-mannanase, Man5A.
[25]
CommentsX-ray crystallography
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.
Related PDB1egn
[26]
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.
Related PDB1gpi
[27]
CommentsX-ray crystallography
PubMed ID11114249
JournalJ Mol Biol
Year2001
Volume305
Pages79-93
AuthorsStahlberg J, Henriksson H, Divne C, Isaksson R, Pettersson G, Johansson G, Jones TA
TitleStructural basis for enantiomer binding and separation of a common beta-blocker: crystal structure of cellobiohydrolase Cel7A with bound (S)-propranolol at 1.9 A resolution.
Related PDB1dy4
[28]
PubMed ID12832787
JournalActa Crystallogr D Biol Crystallogr
Year2003
Volume59
Pages1283-4
AuthorsGrassick A, Birrane G, Tuohy M, Murray P, Higgins T
TitleCrystallization and preliminary crystallographic analysis of the catalytic domain cellobiohydrolase I from Talaromyces emersonii.
[29]
PubMed ID12657782
JournalActa Crystallogr D Biol Crystallogr
Year2003
Volume59
Pages637-43
AuthorsMunoz IG, Mowbray SL, Stahlberg J
TitleThe catalytic module of Cel7D from Phanerochaete chrysosporium as a chiral selector: structural studies of its complex with the beta blocker (R)-propranolol.
Related PDB1h46
[30]
PubMed ID14501131
JournalActa Crystallogr D Biol Crystallogr
Year2003
Volume59
Pages1838-9
AuthorsYaoi K, Kondo H, Suzuki M, Noro N, Tsuda S, Mitsuishi Y
TitleCrystallization and preliminary X-ray crystallographic study on a xyloglucan-specific exo-beta-glycosidase, oligoxyloglucan reducing-end specific cellobiohydrolase.
[31]
PubMed ID12603317
JournalEur J Biochem
Year2003
Volume270
Pages841-8
AuthorsBoer H, Koivula A
TitleThe relationship between thermal stability and pH optimum studied with wild-type and mutant Trichoderma reesei cellobiohydrolase Cel7A.
[32]
CommentsX-ray crystallography
PubMed ID14568538
JournalJ Mol Biol
Year2003
Volume333
Pages817-29
Authorsvon Ossowski I, Stahlberg J, Koivula A, Piens K, Becker D, Boer H, Harle R, Harris M, Divne C, Mahdi S, Zhao Y, Driguez H, Claeyssens M, Sinnott ML, Teeri TT
TitleEngineering the exo-loop of Trichoderma reesei cellobiohydrolase, Cel7A. A comparison with Phanerochaete chrysosporium Cel7D.
Related PDB1q2b,1q2e
[33]
PubMed ID15560790
JournalEur J Biochem
Year2004
Volume271
Pages4495-506
AuthorsGrassick A, Murray PG, Thompson R, Collins CM, Byrnes L, Birrane G, Higgins TM, Tuohy MG
TitleThree-dimensional structure of a thermostable native cellobiohydrolase, CBH IB,and molecular characterization of the cel7 gene from the filamentous fungus,Talaromyces emersonii.
Related PDB1q9h
[34]
PubMed ID15819888
JournalFEBS J
Year2005
Volume272
Pages1952-64
AuthorsUbhayasekera W, Munoz IG, Vasella A, Stahlberg J, Mowbray SL
TitleStructures of Phanerochaete chrysosporium Cel7D in complex with product andinhibitors.
Related PDB1z3t,1z3v,1z3w

comments
This enzyme is composed of the N-terminal catalytic domain and the C-terminal small domain, CBM.
This enzyme has got a similar catalytic site to that of alpha-amylase, although they are never homologous enzymes. Both enzymes have got three acidic residues. However, the catalytic mechanism is slightly different from that of alpha-amylase.
Two of the acidic residues act as a nucleophile and an acid-base, respectively, whereas the other acts as a pKa modulator for the nucleophile.

createdupdated
2004-01-212009-09-29
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
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 2010)
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)

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