| IED ID | IndEnz0008000358 |
| Enzyme Type ID | cellulase000358 |
| Protein Name |
Exoglucanase 1 EC 3.2.1.91 1,4-beta-cellobiohydrolase Cellobiohydrolase 7A Cel7A Exocellobiohydrolase I CBHI Exoglucanase I |
| Gene Name | cbh1 |
| Organism | Trichoderma harzianum (Hypocrea lixii) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Hypocreaceae Trichoderma Trichoderma harzianum (Hypocrea lixii) |
| Enzyme Sequence | MYRKLAVISAFLAAARAQQVCTQQAETHPPLTWQKCTASGCTPQQGSVVLDANWRWTHDTKSTTNCYDGNTWSSTLCPDDATCAKNCCLDGANYSGTYGVTTSGDALTLQFVTASNVGSRLYLMANDSTYQEFTLSGNEFSFDVDVSQLPCGLNGALYFVSMDADGGQSKYPGNAAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNANTGVGGHGSCCSEMDIWEANSISEALTPHPCETVGQTMCSGDSCGGTYSNDRYGGTCDPDGCDWNPYRLGNTSFYGPGSSFALDTTKKLTVVTQFATDGSISRYYVQNGVKFQQPNAQVGSYSGNTINTDYCAAEQTAFGGTSFTDKGGLAQINKAFQGGMVLVMSLWDDYAVNMLWLDSTYPTNATASTPGAKRGSCSTSSGVPAQVEAQSPNSKVIYSNIRFGPIGSTGGNTGSNPPGTSTTRAPPSSTGSSPTATQTHYGQCGGTGWTGPTRCASGYTCQVLNPFYSQCL |
| Enzyme Length | 505 |
| Uniprot Accession Number | Q9P8P3 |
| Absorption | |
| Active Site | ACT_SITE 225; /note=Nucleophile; /evidence=ECO:0000305|PubMed:23114223; ACT_SITE 230; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:23114223 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.; EC=3.2.1.91; Evidence={ECO:0000269|PubMed:21876370, ECO:0000269|PubMed:23114223}; |
| DNA Binding | |
| EC Number | 3.2.1.91 |
| Enzyme Function | FUNCTION: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose (PubMed:21876370). The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units (Probable). {ECO:0000269|PubMed:21876370, ECO:0000305}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:21876370}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:21876370}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (28); Chain (1); Disulfide bond (10); Domain (1); Glycosylation (4); Helix (10); Modified residue (1); Region (4); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Pyrrolidone carboxylic acid;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21876370}. |
| Modified Residue | MOD_RES 18; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:23114223 |
| Post Translational Modification | PTM: O-glycosylated. O-glycosylation of the cellulase linker provides protection from proteolysis. Linker glycans also contribute to binding affinity of cellobiohydrolases to cellulose. {ECO:0000250|UniProtKB:P62694}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 2Y9N; 2YOK; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,216 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.4 mM for p-nitrophenyl-D-cellobioside {ECO:0000269|PubMed:23114223}; KM=3.7 mM for 2-chloro-4-nitrophenyl-beta-lactoside {ECO:0000269|PubMed:23114223}; Vmax=0.016 mmol/min/mg enzyme for p-nitrophenyl-D-cellobioside {ECO:0000269|PubMed:23114223}; Vmax=0.031 mmol/min/mg enzyme for 2-chloro-4-nitrophenyl-beta-lactoside {ECO:0000269|PubMed:23114223}; Note=kcat is 23.2 min(-1) with p-nitrophenyl-D-cellobioside as substrate and 44.6 min(-1) with 2-chloro-4-nitrophenyl-beta-lactoside as substrate. {ECO:0000269|PubMed:23114223}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.176; |