DB code: D00499

CATH domain 2.70.100.10 : 1,4-Beta-D-Glucan Cellobiohydrolase I; Chain A Catalytic domain
2.-.-.- :
E.C. 3.2.1.91
CSA 1cel
M-CSA 1cel
MACiE

CATH domain Related DB codes (homologues)
2.70.100.10 : 1,4-Beta-D-Glucan Cellobiohydrolase I; Chain A S00162

Uniprot Enzyme Name
UniprotKB Protein name Synonyms CAZy Pfam
P62694 Exoglucanase 1
EC 3.2.1.91
Exoglucanase I
Exocellobiohydrolase I
CBHI
1,4-beta-cellobiohydrolase
CBM1 (Carbohydrate-Binding Module Family 1)
GH7 (Glycoside Hydrolase Family 7)
PF00734 (CBM_1)
PF00840 (Glyco_hydro_7)
[Graphical View]
Q09431
Cellulase
EC 3.2.1.91
CBM1 (Carbohydrate-Binding Module Family 1)
GH7 (Glycoside Hydrolase Family 7)
PF00734 (CBM_1)
PF00840 (Glyco_hydro_7)
[Graphical View]
Q7LIJ0
Major cellobiohydrolase (Cellulase)
EC 3.2.1.91
PF00734 (CBM_1)
PF00840 (Glyco_hydro_7)
[Graphical View]
Q8TFL9
Cellobiohydrolase I catalytic domain (Cellobiohydrolase 1 catalytic domain)
EC 3.2.1.91
GH7 (Glycoside Hydrolase Family 7)
PF00840 (Glyco_hydro_7)
[Graphical View]

KEGG enzyme name
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

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P62694 GUX1_TRIRE Hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non- reducing ends of the chains. Secreted.
Q09431 Q09431_PHACH
Q7LIJ0 Q7LIJ0_PHACH
Q8TFL9 Q8TFL9_TALEM

KEGG Pathways
Map code Pathways E.C.
MAP00500 Starch and sucrose metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00760 C02013 C00001 C00185 C00760
E.C.
Compound Cellulose Cellotetraose H2O Cellobiose Cellulose
Type polysaccharide polysaccharide H2O polysaccharide polysaccharide
ChEBI 62974
15377
17057
PubChem 439626
22247451
962
439178
1celA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:IBZ-GLC Unbound
1celB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:IBZ-GLC Unbound
1dy4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:SNP Unbound
1egnA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1q2bA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1q2eA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:MGL-SGC-GLC-GLC Unbound
1q2eB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:MGL-SGC-GLC-GLC Unbound
2celA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
2celB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
3celA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:GLC-GLC Unbound
4celA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
4celB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
5celA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:GLC-GLC-GLC-GLC_455 Unbound Unbound
6celA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:GLC-GLC-GLC-GLC Bound:GLC-GLC-GLC-GLC-GLC
7celA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:GLC-GLC Bound:GLC-GLC-GLC-GLC-GLC-GLC
1gpiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1h46X Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1z3tA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:CBI Unbound
1z3vA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:LAT Unbound
1z3wA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:IDC Unbound
1q9hA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1az6A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1azhA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1azkA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1cbhA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
2cbhA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [14], [18]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1celA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 212;ASP 214;GLU 217;HIS 228
1celB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 212;ASP 214;GLU 217;HIS 228
1dy4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 212;ASP 214;GLU 217;HIS 228
1egnA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 212;ASP 214;GLU 217;HIS 228 mutant E223S,A224H,L225V,T226A,D262G
1q2bA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 212;ASP 214;GLU 217;HIS 228 mutant D241C,D249C
1q2eA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 212;ASP 214;GLU 217;HIS 228 mutant deletion 245-252
1q2eB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 212;ASP 214;GLU 217;HIS 228 mutant deletion 245-252
2celA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;ASP 214;GLU 217;HIS 228 mutant E212Q
2celB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;ASP 214;GLU 217;HIS 228 mutant E212Q
3celA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;ASP 214;GLU 217;HIS 228 mutant E212Q
4celA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 212;;GLU 217;HIS 228 mutant D214N
4celB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 212;;GLU 217;HIS 228 mutant D214N
5celA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;ASP 214;GLU 217;HIS 228 mutant E212Q
6celA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;ASP 214;GLU 217;HIS 228 mutant E212Q
7celA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 212;ASP 214;;HIS 228 mutant E217Q
1gpiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 207;ASP 209;GLU 212;HIS 223
1h46X Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 207;ASP 209;GLU 212;HIS 223
1z3tA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 207;ASP 209;GLU 212;HIS 223
1z3vA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 207;ASP 209;GLU 212;HIS 223
1z3wA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 207;ASP 209;GLU 212;HIS 223
1q9hA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 209;ASP 211;GLU 214;HIS 225
1az6A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant Y5A,Y31A,Y32A
1azhA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant Y5A,Y31A,Y32A
1azkA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant Y5A,Y31A,Y32A
1cbhA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant E126Q,D130N,D132A
2cbhA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. 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]
Resource
Comments
Medline ID
PubMed ID 3178831
Journal Biochem Biophys Res Commun
Year 1988
Volume 156
Pages 180-5
Authors Abuja PM, Pilz I, Claeyssens M, Tomme P
Title Domain structure of cellobiohydrolase II as studied by small angle X-ray scattering: close resemblance to cellobiohydrolase I.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2597150
Journal Biochem Biophys Res Commun
Year 1989
Volume 165
Pages 615-23
Authors Abuja PM, Pilz I, Tomme P, Claeyssens M
Title Structural changes in cellobiohydrolase I upon binding of a macromolecular ligand as evident by SAXS investigations.
Related PDB
Related UniProtKB
[3]
Resource
Comments STRUCTURE BY NMR OF 478-513.
Medline ID 90057416
PubMed ID 2554967
Journal Biochemistry
Year 1989
Volume 28
Pages 7241-57
Authors Kraulis J, Clore GM, Nilges M, Jones TA, Pettersson G, Knowles J, Gronenborn AM
Title Determination 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 PDB 1cbh 2cbh
Related UniProtKB P62694
[4]
Resource
Comments ACTIVE SITE
Medline ID
PubMed ID
Journal FEBS Lett
Year 1989
Volume 243
Pages 239-43
Authors Tomme P, Clayssens M
Title Identification of a functionally important carboxyl group in cellobiohydrolase I from Trichoderma reesei.
Related PDB
Related UniProtKB P62694
[5]
Resource
Comments
Medline ID
PubMed ID 2332056
Journal FEBS Lett
Year 1990
Volume 263
Pages 89-92
Authors Claeyssens M, Tomme P, Brewer CF, Hehre EJ
Title Stereochemical course of hydrolysis and hydration reactions catalysed by cellobiohydrolases I and II from Trichoderma reesei.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 2261982
Journal FEBS Lett
Year 1990
Volume 275
Pages 135-8
Authors Mitsuishi Y, Nitisinprasert S, Saloheimo M, Biese I, Reinikainen T, Claeyssens M, Keranen S, Knowles JK, Teeri TT
Title Site-directed mutagenesis of the putative catalytic residues of Trichoderma reesei cellobiohydrolase I and endoglucanase I.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 1567377
Journal Biochem J
Year 1992
Volume 283
Pages 31-4
Authors Brooks MM, Tuohy MG, Savage AV, Claeyssens M, Coughlan MP
Title The stereochemical course of reactions catalysed by the cellobiohydrolases produced by Talaromyces emersonii.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8489514
Journal Biochem J
Year 1993
Volume 291
Pages 883-8
Authors Konstantinidis AK, Marsden I, Sinnott ML
Title Hydrolyses of alpha- and beta-cellobiosyl fluorides by cellobiohydrolases of Trichoderma reesei.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 8252556
Journal Carbohydr Res
Year 1993
Volume 249
Pages 77-90
Authors McCarter JD, Adam MJ, Braun C, Namchuk M, Tull D, Withers SG
Title Syntheses of 2-deoxy-2-fluoro mono- and oligo-saccharide glycosides from glycals and evaluation as glycosidase inhibitors.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 8407900
Journal J Biol Chem
Year 1993
Volume 268
Pages 20756-61
Authors Srisodsuk M, Reinikainen T, Penttila M, Teeri TT
Title Role of the interdomain linker peptide of Trichoderma reesei cellobiohydrolase I in its interaction with crystalline cellulose.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 8254686
Journal J Mol Biol
Year 1993
Volume 234
Pages 905-7
Authors Divne C, Sinning I, Stahlberg J, Pettersson G, Bailey M, Siika-aho M, Margolles-Clark E, Teeri T, Jones TA
Title Crystallization and preliminary X-ray studies on the core proteins of cellobiohydrolase I and endoglucanase I from Trichoderma reesei.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 8037459
Journal Arch Biochem Biophys
Year 1994
Volume 312
Pages 459-66
Authors Evans BR, Margalit R, Woodward J
Title Veratryl alcohol oxidase activity of a chemically modified cellulase protein.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 8192865
Journal Biotechnol Appl Biochem
Year 1994
Volume 19
Pages 141-53
Authors Woodward J, Brown JP, Evans BR, Affholter KA
Title Papain digestion of crude Trichoderma reesei cellulase: purification and properties of cellobiohydrolase I and II core proteins.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 18-452.
Medline ID 94310436
PubMed ID 8036495
Journal Science
Year 1994
Volume 265
Pages 524-8
Authors Divne C, Stahlberg J, Reinikainen T, Ruohonen L, Pettersson G, Knowles JK, Teeri TT, Jones TA
Title The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei.
Related PDB 1cel
Related UniProtKB P62694
[15]
Resource
Comments
Medline ID
PubMed ID 7549870
Journal Protein Sci
Year 1995
Volume 4
Pages 1056-64
Authors Linder M, Mattinen ML, Kontteli M, Lindeberg G, Stahlberg J, Drakenberg T, Reinikainen T, Pettersson G, Annila A
Title Identification of functionally important amino acids in the cellulose-binding domain of Trichoderma reesei cellobiohydrolase I.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 8706890
Journal FEBS Lett
Year 1996
Volume 390
Pages 339-44
Authors Henriksson H, Stahlberg J, Isaksson R, Pettersson G
Title The active sites of cellulases are involved in chiral recognition: a comparison of cellobiohydrolase 1 and endoglucanase 1.
Related PDB
Related UniProtKB
[17]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8951380
Journal J Mol Biol
Year 1996
Volume 264
Pages 337-49
Authors Stahlberg J, Divne C, Koivula A, Piens K, Claeyssens M, Teeri TT, Jones TA
Title Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei.
Related PDB 2cel 3cel 4cel
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 9449766
Journal Carbohydr Res
Year 1997
Volume 304
Pages 143-54
Authors Klarskov K, Piens K, Stahlberg J, Hoj PB, Beeumen JV, Claeyssens M
Title Cellobiohydrolase I from Trichoderma reesei: identification of an active-site nucleophile and additional information on sequence including the glycosylation pattern of the core protein.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 9325098
Journal J Mol Biol
Year 1997
Volume 272
Pages 383-97
Authors Kleywegt GJ, Zou JY, Divne C, Davies GJ, Sinning I, Stahlberg J, Reinikainen T, Srisodsuk M, Teeri TT, Jones TA
Title The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 A resolution, and a comparison with related enzymes.
Related PDB
Related UniProtKB
[20]
Resource
Comments STRUCTURE BY NMR OF 478-513.
Medline ID 97194052
PubMed ID 9041630
Journal Protein Sci
Year 1997
Volume 6
Pages 294-303
Authors Mattinen ML, Kontteli M, Kerovuo J, Linder M, Annila A, Lindeberg G, Reinikainen T, Drakenberg T
Title Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei.
Related PDB 1az6 1azh 1azj 1azk
Related UniProtKB P62694
[21]
Resource
Comments
Medline ID
PubMed ID 9761741
Journal Biochem J
Year 1998
Volume 335
Pages 409-16
Authors MacKenzie LF, Sulzenbacher G, Divne C, Jones TA, Woldike HF, Schulein M, Withers SG, Davies GJ
Title Crystal 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 PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 9760165
Journal Eur J Biochem
Year 1998
Volume 256
Pages 279-86
Authors Mattinen ML, Linder M, Drakenberg T, Annila A
Title Solution structure of the cellulose-binding domain of endoglucanase I from Trichoderma reesei and its interaction with cello-oligosaccharides.
Related PDB
Related UniProtKB
[23]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 18-452.
Medline ID 98128795
PubMed ID 9466911
Journal J Mol Biol
Year 1998
Volume 275
Pages 309-25
Authors Divne C, Stahlberg J, Teeri TT, Jones TA
Title High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei.
Related PDB 5cel 6cel 7cel
Related UniProtKB P62694
[24]
Resource
Comments
Medline ID
PubMed ID 9989594
Journal FEBS Lett
Year 1999
Volume 443
Pages 149-53
Authors Harjunpaa V, Helin J, Koivula A, Siika-aho M, Drakenberg T
Title A comparative study of two retaining enzymes of Trichoderma reesei: transglycosylation of oligosaccharides catalysed by the cellobiohydrolase I, Cel7A, and the beta-mannanase, Man5A.
Related PDB
Related UniProtKB
[25]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11336632
Journal Biochem J
Year 2001
Volume 356
Pages 19-30
Authors Becker 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
Title Engineering 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 PDB 1egn
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 11743726
Journal J Mol Biol
Year 2001
Volume 314
Pages 1097-111
Authors Munoz IG, Ubhayasekera W, Henriksson H, Szabo I, Pettersson G, Johansson G, Mowbray SL, Stahlberg J
Title Family 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 PDB 1gpi
Related UniProtKB
[27]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11114249
Journal J Mol Biol
Year 2001
Volume 305
Pages 79-93
Authors Stahlberg J, Henriksson H, Divne C, Isaksson R, Pettersson G, Johansson G, Jones TA
Title Structural 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 PDB 1dy4
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 12832787
Journal Acta Crystallogr D Biol Crystallogr
Year 2003
Volume 59
Pages 1283-4
Authors Grassick A, Birrane G, Tuohy M, Murray P, Higgins T
Title Crystallization and preliminary crystallographic analysis of the catalytic domain cellobiohydrolase I from Talaromyces emersonii.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 12657782
Journal Acta Crystallogr D Biol Crystallogr
Year 2003
Volume 59
Pages 637-43
Authors Munoz IG, Mowbray SL, Stahlberg J
Title The catalytic module of Cel7D from Phanerochaete chrysosporium as a chiral selector: structural studies of its complex with the beta blocker (R)-propranolol.
Related PDB 1h46
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 14501131
Journal Acta Crystallogr D Biol Crystallogr
Year 2003
Volume 59
Pages 1838-9
Authors Yaoi K, Kondo H, Suzuki M, Noro N, Tsuda S, Mitsuishi Y
Title Crystallization and preliminary X-ray crystallographic study on a xyloglucan-specific exo-beta-glycosidase, oligoxyloglucan reducing-end specific cellobiohydrolase.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 12603317
Journal Eur J Biochem
Year 2003
Volume 270
Pages 841-8
Authors Boer H, Koivula A
Title The relationship between thermal stability and pH optimum studied with wild-type and mutant Trichoderma reesei cellobiohydrolase Cel7A.
Related PDB
Related UniProtKB
[32]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 14568538
Journal J Mol Biol
Year 2003
Volume 333
Pages 817-29
Authors von 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
Title Engineering the exo-loop of Trichoderma reesei cellobiohydrolase, Cel7A. A comparison with Phanerochaete chrysosporium Cel7D.
Related PDB 1q2b 1q2e
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 15560790
Journal Eur J Biochem
Year 2004
Volume 271
Pages 4495-506
Authors Grassick A, Murray PG, Thompson R, Collins CM, Byrnes L, Birrane G, Higgins TM, Tuohy MG
Title Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB,and molecular characterization of the cel7 gene from the filamentous fungus,Talaromyces emersonii.
Related PDB 1q9h
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 15819888
Journal FEBS J
Year 2005
Volume 272
Pages 1952-64
Authors Ubhayasekera W, Munoz IG, Vasella A, Stahlberg J, Mowbray SL
Title Structures of Phanerochaete chrysosporium Cel7D in complex with product andinhibitors.
Related PDB 1z3t 1z3v 1z3w
Related UniProtKB

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.

Created Updated
2004-01-21 2009-09-29