| IED ID | IndEnz0009000206 |
| Enzyme Type ID | chitinase000206 |
| Protein Name |
Endochitinase 42 EC 3.2.1.14 42 kDa endochitinase Chitinase 42 |
| Gene Name | chit42 |
| 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 | MLSFLGKSVALLAALQATLSSPKPGHRRASVEKRANGYANSVYFTNWGIYDRNFQPADLVASDVTHVIYSFMNLQADGTVISGDTYADYEKHYADDSWNDVGTNAYGCVKQLFKVKKANRGLKVLLSIGGWTWSTNFPSAASTDANRKNFAKTAITFMKDWGFDGIDIDWEYPADATQASNMILLLKEVRSQRDAYAAQYAPGYHFLLTIAAPAGKDNYSKLRLADLGQVLDYINLMAYDYAGSFSPLTGHDANLFNNPSNPNATPFNTDSAVKDYINGGVPANKIVLGMPIYGRSFQNTAGIGQTYNGVGSGSWEAGIWDYKALPKAGATVQYDSVAKGYYSYNSATKELISFDTPDMINTKVAYLKSLGLGGSMFWEASADKKGADSVIGTSHRALGGLDTTQNLLSYPNSKYDNIKNGLN |
| Enzyme Length | 423 |
| Uniprot Accession Number | P48827 |
| Absorption | |
| Active Site | ACT_SITE 171; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258 |
| Activity Regulation | |
| Binding Site | BINDING 172; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 378; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000269|PubMed:1606968}; |
| DNA Binding | |
| EC Number | 3.2.1.14 |
| Enzyme Function | FUNCTION: Secreted chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Plays a morphogenetic role during apical growth, cell division and differentiation (cell wall morphogenesis). Acts also as an antifungal agent. Involved in the degradation and further assimilation of phytopathogenic fungi, namely mycoparasitism, the major mechanism accounting for the antagonistic activity against phytopathogenic fungi displayed by Trichoderma. {ECO:0000269|PubMed:1606968}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45-50 degrees Celsius. {ECO:0000269|PubMed:1606968}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (16); Binding site (2); Chain (1); Domain (1); Glycosylation (1); Helix (20); Propeptide (1); Region (3); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Carbohydrate metabolism;Chitin degradation;Chitin-binding;Cleavage on pair of basic residues;Direct protein sequencing;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | INDUCTION: Specifically induced by chitin and is catabolite repressed. {ECO:0000269|PubMed:1606968}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1606968, ECO:0000269|PubMed:22744980}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 6EPB; 6YLJ; 6YN4; 7AKQ; |
| Mapped Pubmed ID | 29566690; |
| Motif | |
| Gene Encoded By | |
| Mass | 46,057 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.3 mg/ml for colloidal chitin {ECO:0000269|PubMed:1606968}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.14; |