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CATH domain | Related DB codes (homologues) |
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2.60.40.290 : Immunoglobulin-like | M00219,D00502,D00504,M00026,M00192 | 3.20.20.80 : TIM Barrel | S00202,S00210,S00748,S00906,S00907,S00911,S00912,S00915,M00134,M00160,S00204,S00205,S00206,S00207,S00203,S00208,S00209,S00211,S00213,S00214,M00113,T00307,D00165,D00166,D00169,D00176,D00501,D00502,D00503,D00844,D00861,D00864,M00026,M00112,M00193,M00346,T00057,T00062,T00063,T00066,T00067 |
Enzyme Name | UniProtKB | KEGG |
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| P07986 |
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Protein name | Exoglucanase/xylanase | endo-1,4-beta-xylanase (EC 3.2.1.8)endo-(1->4)-beta-xylan 4-xylanohydrolase (EC 3.2.1.8)endo-1,4-xylanase (EC 3.2.1.8)xylanase (EC 3.2.1.8)beta-1,4-xylanase (EC 3.2.1.8)endo-1,4-xylanase (EC 3.2.1.8)endo-beta-1,4-xylanase (EC 3.2.1.8)endo-1,4-beta-D-xylanase (EC 3.2.1.8)1,4-beta-xylan xylanohydrolase (EC 3.2.1.8)beta-xylanase (EC 3.2.1.8)beta-1,4-xylan xylanohydrolase (EC 3.2.1.8)endo-1,4-beta-xylanase (EC 3.2.1.8)beta-D-xylanase (EC 3.2.1.8)cellulose 1,4-beta-cellobiosidase (EC 3.2.1.91)exo-cellobiohydrolase (EC 3.2.1.91)beta-1,4-glucan cellobiohydrolase (EC 3.2.1.91)beta-1,4-glucan cellobiosylhydrolase (EC 3.2.1.91)1,4-beta-glucan cellobiosidase (EC 3.2.1.91)exoglucanase (EC 3.2.1.91)avicelase (EC 3.2.1.91)CBH 1 (EC 3.2.1.91)C1 cellulase (EC 3.2.1.91)cellobiohydrolase I (EC 3.2.1.91)cellobiohydrolase (EC 3.2.1.91)exo-beta-1,4-glucan cellobiohydrolase (EC 3.2.1.91)1,4-beta-D-glucan cellobiohydrolase (EC 3.2.1.91)cellobiosidase (EC 3.2.1.91) |
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Synonyms | None |
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Includes | Exoglucanase EC 3.2.1.91Exocellobiohydrolase 1,4-beta-cellobiohydrolase Beta-1,4-glycanase CEXEndo-1,4-beta-xylanase B(Xylanase B) EC 3.2.1.8 |
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Pfam | PF00553 (CBM_2) PF00331 (Glyco_hydro_10) [Graphical view]
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CAZy | GH10 (Glycoside Hydrolase Family)
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UniProtKB:Accession Number | P07986 |
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Entry name | GUX_CELFI |
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Activity | Hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non- reducing ends of the chains.,Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. |
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Subunit |
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Subcellular location |
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Cofactor |
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Compound table: links to PDB-related databases & PoSSuM |
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| Substrates | Products | intermediates |
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KEGG-id | C00707 | C00760 | C02013 | C00001 | C00707 | C00185 | C00760 |
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E.C. | 3.2.1.8 | 3.2.1.91 | 3.2.1.91 | 3.2.1.8,3.2.1.91 | 3.2.1.8 | 3.2.1.91 | 3.2.1.91 |
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Compound | Xylan | Cellulose | Cellotetraose | H2O | Xylan | Cellobiose | Cellulose | Transition-state in glycosylation | Enzyme-Substrate intermediate | Transition-state in deglycosylation |
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Type | polysaccharide | polysaccharide | polysaccharide | H2O | polysaccharide | polysaccharide | polysaccharide |
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ChEBI |
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| 62974
| 15377
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| 17057
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PubChem |
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| 439626
| 962 22247451
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| 439178
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| | | | | | | | | | | | | | | | | |
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1expA |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:GLC-G2F | Unbound |
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1fh7A |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:XYP-XDN |
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1fh8A |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:XYP-XIF |
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1fh9A |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Analogue:XYP-LOX | Unbound | Unbound | Unbound | Unbound | Unbound |
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1fhdA |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Analogue:XYP-XIM | Unbound | Unbound | Unbound | Unbound | Unbound |
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1j01A |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Analogue:XIL | Unbound | Unbound | Unbound | Unbound | Unbound |
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2exoA |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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2hisA |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Intermediate-bound:GLC-GLC | Unbound |
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2xylA |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:XYP-X2F | Unbound |
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1exgA |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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1exhA |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[4] | p.6372 |
| [5] | p.12549-12552 |
| [8] | Scheme 1 | 4 | [9] | Fig. 1, p.150-151 |
| [11] | Scheme 1, Scheme 2 |
| [13] | Fig.1, Fig.5, p.813-817 |
| [16] | Fig.2, p.11560-11561 |
| [20] | FIG. 1, p.86 |
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references | [1] |
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Comments | DISULFIDE BONDS. |
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Medline ID | 92104156 |
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PubMed ID | 1761039 |
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Journal | Eur J Biochem |
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Year | 1991 |
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Volume | 202 |
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Pages | 367-77 |
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Authors | Gilkes NR, Claeyssens M, Aebersold R, Henrissat B, Meinke A, Morrison HD, Kilburn DG, Warren RA, Miller RC Jr |
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Title | Structural and functional relationships in two families of beta-1,4-glycanases. |
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Related UniProtKB | P07986 |
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[2] |
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Comments | ACTIVE SITE GLU-274. |
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Medline ID | 91340691 |
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PubMed ID | 1678739 |
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Journal | J Biol Chem |
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Year | 1991 |
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Volume | 266 |
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Pages | 15621-5 |
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Authors | Tull D, Withers SG, Gilkes NR, Kilburn DG, Warren RA, Aebersold R |
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Title | Glutamic acid 274 is the nucleophile in the active site of a "retaining" exoglucanase from Cellulomonas fimi. |
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Related UniProtKB | P07986 |
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[3] |
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PubMed ID | 1453471 |
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Journal | J Mol Biol |
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Year | 1992 |
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Volume | 228 |
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Pages | 693-5 |
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Authors | Bedarkar S, Gilkes NR, Kilburn DG, Kwan E, Rose DR, Miller RC Jr, Warren RA, Withers SG |
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Title | Crystallization and preliminary X-ray diffraction analysis of the catalytic domain of Cex, an exo-beta-1,4-glucanase and beta-1,4-xylanase from the bacterium Cellulomonas fimi. |
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[4] |
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Comments | MUTAGENESIS OF GLU-168. |
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Medline ID | 94250681 |
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PubMed ID | 7910761 |
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Journal | Biochemistry |
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Year | 1994 |
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Volume | 33 |
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Pages | 6371-6 |
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Authors | MacLeod AM, Lindhorst T, Withers SG, Warren RA |
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Title | The acid/base catalyst in the exoglucanase/xylanase from Cellulomonas fimi is glutamic acid 127: evidence from detailed kinetic studies of mutants. |
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Related UniProtKB | P07986 |
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[5] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). |
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Medline ID | 95001978 |
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PubMed ID | 7918478 |
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Journal | Biochemistry |
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Year | 1994 |
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Volume | 33 |
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Pages | 12546-52 |
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Authors | White A, Withers SG, Gilkes NR, Rose DR |
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Title | Crystal structure of the catalytic domain of the beta-1,4-glycanase cex from Cellulomonas fimi. |
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Related PDB | 2exo |
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Related UniProtKB | P07986 |
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[6] |
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Comments | STRUCTURE BY NMR OF 377-484. |
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Medline ID | 95284032 |
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PubMed ID | 7766609 |
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Journal | Biochemistry |
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Year | 1995 |
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Volume | 34 |
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Pages | 6993-7009 |
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Authors | Xu GY, Ong E, Gilkes NR, Kilburn DG, Muhandiram DR, Harris-Brandts M, Carver JP, Kay LE, Harvey TS |
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Title | Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy. |
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Related PDB | 1exg,1exh |
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Related UniProtKB | P07986 |
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[7] |
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PubMed ID | 8714589 |
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Journal | Anal Biochem |
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Year | 1996 |
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Volume | 234 |
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Pages | 119-25 |
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Authors | Tull D, Burgoyne DL, Chow DT, Withers SG, Aebersold R |
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Title | A mass spectrometry-based approach for probing enzyme active sites: identification of Glu 127 in Cellulomonas fimi exoglycanase as the residue modified by N-bromoacetyl cellobiosylamine. |
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[8] |
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PubMed ID | 8855954 |
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Journal | Biochemistry |
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Year | 1996 |
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Volume | 35 |
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Pages | 13165-72 |
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Authors | MacLeod AM, Tull D, Rupitz K, Warren RA, Withers SG |
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Title | Mechanistic consequences of mutation of active site carboxylates in a retaining beta-1,4-glycanase from Cellulomonas fimi. |
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[9] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). |
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Medline ID | 96163434 |
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PubMed ID | 8564541 |
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Journal | Nat Struct Biol |
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Year | 1996 |
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Volume | 3 |
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Pages | 149-54 |
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Authors | White A, Tull D, Johns K, Withers SG, Rose DR |
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Title | Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase. |
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Related PDB | 1exp |
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Related UniProtKB | P07986 |
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[10] |
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PubMed ID | 8901562 |
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Journal | Proc Natl Acad Sci U S A |
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Year | 1996 |
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Volume | 93 |
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Pages | 12229-34 |
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Authors | Creagh AL, Ong E, Jervis E, Kilburn DG, Haynes CA |
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Title | Binding of the cellulose-binding domain of exoglucanase Cex from Cellulomonas fimi to insoluble microcrystalline cellulose is entropically driven. |
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[11] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-353. |
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Medline ID | 98206890 |
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PubMed ID | 9537990 |
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Journal | Biochemistry |
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Year | 1998 |
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Volume | 37 |
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Pages | 4751-8 |
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Authors | Notenboom V, Birsan C, Warren RA, Withers SG, Rose DR |
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Title | Exploring the cellulose/xylan specificity of the beta-1,4-glycanase cex from Cellulomonas fimi through crystallography and mutation. |
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Related PDB | 2xyl |
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Related UniProtKB | P07986 |
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[12] |
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PubMed ID | 9822697 |
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Journal | J Biol Chem |
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Year | 1998 |
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Volume | 273 |
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Pages | 32187-99 |
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Authors | Charnock SJ, Spurway TD, Xie H, Beylot MH, Virden R, Warren RA, Hazlewood GP, Gilbert HJ |
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Title | The topology of the substrate binding clefts of glycosyl hydrolase family 10 xylanases are not conserved. |
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[13] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 42-353. |
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Medline ID | 98400502 |
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PubMed ID | 9731776 |
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Journal | Nat Struct Biol |
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Year | 1998 |
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Volume | 5 |
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Pages | 812-8 |
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Authors | Notenboom V, Birsan C, Nitz M, Rose DR, Warren RA, Withers SG |
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Title | Insights into transition state stabilization of the beta-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants. |
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Related PDB | 2his |
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Related UniProtKB | P07986 |
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[14] |
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PubMed ID | 10571062 |
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Journal | FEBS Lett |
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Year | 1999 |
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Volume | 460 |
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Pages | 61-6 |
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Authors | Kaneko S, Kuno A, Fujimoto Z, Shimizu D, Machida S, Sato Y, Yura K, Go M, Mizuno H, Taira K, Kusakabe I, Hayashi K |
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Title | An investigation of the nature and function of module 10 in a family F/10 xylanase FXYN of Streptomyces olivaceoviridis E-86 by module shuffling with the Cex of Cellulomonas fimi and by site-directed mutagenesis. |
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[15] |
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PubMed ID | 10570988 |
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Journal | Gene |
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Year | 1999 |
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Volume | 238 |
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Pages | 93-101 |
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Authors | Sato Y, Niimura Y, Yura K, Go M |
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Title | Module-intron correlation and intron sliding in family F/10 xylanase genes. |
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[16] |
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Comments | X-ray crystallography |
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PubMed ID | 10995222 |
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Journal | Biochemistry |
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Year | 2000 |
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Volume | 39 |
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Pages | 11553-63 |
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Authors | Notenboom V, Williams SJ, Hoos R, Withers SG, Rose DR |
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Title | Detailed structural analysis of glycosidase/inhibitor interactions: complexes of Cex from Cellulomonas fimi with xylobiose-derived aza-sugars. |
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Related PDB | 1fh7,1fh8,1fh9,1fhd |
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[17] |
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PubMed ID | 11239087 |
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Journal | Protein Eng |
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Year | 2000 |
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Volume | 13 |
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Pages | 873-9 |
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Authors | Kaneko S, Iwamatsu S, Kuno A, Fujimoto Z, Sato Y, Yura K, Go M, Mizuno H, Taira K, Hasegawa T, Kusakabe I, Hayashi K |
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Title | Module shuffling of a family F/10 xylanase: replacement of modules M4 and M5 of the FXYN of Streptomyces olivaceoviridis E-86 with those of the Cex of Cellulomonas fimi. |
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[18] |
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PubMed ID | 11025547 |
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Journal | Proteins |
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Year | 2000 |
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Volume | 41 |
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Pages | 362-73 |
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Authors | Leggio LL, Jenkins J, Harris GW, Pickersgill RW |
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Title | X-ray crystallographic study of xylopentaose binding to Pseudomonas fluorescens xylanase A. |
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[19] |
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PubMed ID | 11963886 |
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Journal | Appl Biochem Biotechnol |
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Year | 2001 |
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Volume | 91-93 |
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Pages | 575-92 |
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Authors | Esteghlalian AR, Srivastava V, Gilkes NR, Kilburn DG, Warren RA, Saddle JN |
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Title | Do cellulose binding domains increase substrate accessibility? |
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[20] |
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PubMed ID | 12418218 |
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Journal | Methods Enzymol |
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Year | 2002 |
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Volume | 354 |
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Pages | 84-105 |
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Authors | Wicki J, Rose DR, Withers SG |
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Title | Trapping covalent intermediates on beta-glycosidases. |
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comments | This family belongs to the glycosidase family-10, which has a retaining mechanism (equatorial to equatorial conformation), and also a family of 4/7 superfamily, which has got catalytic residues at the C-terminal ends of beta-4 and beta-7 on the (alpha/beta)8 barrel fold. The catalytic mechanism must be similar to those of 4/7 superfamily enzymes (such as S00203 in EzCatDB). According to the literature [4], [5] & [8], Glu233 and Glu127 act as a nucleophile and acid-base, respectively. The catalytic reaction is initiated by the protonation of Glu127 to the O1 atom of Xylan/Cellurose substrate. This suggests that the reaction proceeds through a dissociative-type (or SN1-like) mechanism, with a formation of oxocarbonium ion in the transition state, during the glycosylation of the active site. During the glycosylation, Glu233 makes a covalent bond with the C1 atom of the substrate. At the second stage, or during the deglycosylation, a water molecule can be activated by a general base, Glu127. According to the literature [9] & [13], His205-Asp235 dyad seems to stabilize the leaving nucleophile, Glu233, during the deglycosylation.
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created | updated |
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2005-03-14 | 2009-02-26 |
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