Detail Information for IndEnz0008000361
IED ID IndEnz0008000361
Enzyme Type ID cellulase000361
Protein Name Exoglucanase 2
EC 3.2.1.91
1,4-beta-cellobiohydrolase
Cellobiohydrolase 6A
Cel6A
Exocellobiohydrolase II
CBHII
Exoglucanase II
Gene Name cbh2
Organism Hypocrea jecorina (Trichoderma reesei)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Hypocreaceae Trichoderma Hypocrea jecorina (Trichoderma reesei)
Enzyme Sequence MIVGILTTLATLATLAASVPLEERQACSSVWGQCGGQNWSGPTCCASGSTCVYSNDYYSQCLPGAASSSSSTRAASTTSRVSPTTSRSSSATPPPGSTTTRVPPVGSGTATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNYAGQFVVYDLPDRDCAALASNGEYSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPDSLANLVTNLGTPKCANAQSAYLECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFANVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVYNEKLYIHAIGPLLANHGWSNAFFITDQGRSGKQPTGQQQWGDWCNVIGTGFGIRPSANTGDSLLDSFVWVKPGGECDGTSDSSAPRFDSHCALPDALQPAPQAGAWFQAYFVQLLTNANPSFL
Enzyme Length 471
Uniprot Accession Number P07987
Absorption
Active Site ACT_SITE 245; /note=Proton donor; /evidence=ECO:0000269|PubMed:12188666
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|Ref.3};
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 (Ref.3). 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|Ref.3, ECO:0000305}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-6. {ECO:0000269|PubMed:12188666};
Pathway
nucleotide Binding
Features Active site (1); Beta strand (14); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (9); Helix (15); Modified residue (1); Mutagenesis (2); Propeptide (1); Region (3); Sequence conflict (2); Signal peptide (1); Site (2); Turn (2)
Keywords 3D-structure;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Pyrrolidone carboxylic acid;Secreted;Signal
Interact With Itself
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3}.
Modified Residue MOD_RES 25; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|Ref.2
Post Translational Modification PTM: Asn-334 contains mainly a high-mannose-type glycan (Hex(7-9)GlcNAc(2)) in a 3:1 ration with a single GlcNAc. Asn-313 was primarily unglycosylated with a small fraction (18%) bearing a single GlcNAc at this site. {ECO:0000250|UniProtKB:A0A024SH76}.
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D X-ray crystallography (12)
Cross Reference PDB 1CB2; 1HGW; 1HGY; 1QJW; 1QK0; 1QK2; 3CBH; 4AU0; 4AX6; 4AX7; 4I5R; 4I5U;
Mapped Pubmed ID 10508787; 23137336; 23404363;
Motif
Gene Encoded By
Mass 49,653
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17 uM for cellotriose {ECO:0000269|PubMed:12188666}; KM=2.6 uM for cellotetraose {ECO:0000269|PubMed:12188666}; KM=1.3 uM for cellopentaose {ECO:0000269|PubMed:12188666}; KM=14 uM for cellohexaose {ECO:0000269|PubMed:12188666}; Note=kcat is 0.06 sec(-1) with cellotriose as substrate, 4.1 sec(-1) with cellotetraose as substrate, 1.1 sec(-1) with cellopentaose as substrate and 14 sec(-1) with cellopentaose as substrate. {ECO:0000269|PubMed:12188666};
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.176;3.2.1.91;