| IED ID | IndEnz0009000295 |
| Enzyme Type ID | chitinase000295 |
| Protein Name |
Endochitinase B EC 3.2.1.14 Chitinase B |
| Gene Name | chiB |
| Organism | Emericella nidulans (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) |
| Enzyme Sequence | MSGYKTVGYFVNWAIYGRNYNPQDLPAEKLTHILYAFANVRPETGEVYLSDTWSDIEKHYPTDSWNDTGNNVYGCVKQLGLLKRQHRQLKVLLSIGGWTYSPNFTNGAGTPENRARFAQTATKLITDLGFDGIDIDWEYPQNDQQAQNYVDLLRRCREALNAAQGQRRFQLTVAVPAGPDNYNKLRLQEMTPYLDFYNLMAYDYAGSWDQTAGHQANLYPSTSNPTSTPFNTVQAVNHYIDAGGVPSNKIILGMPIYGRAFQNTDGPGRPYSGIGQGTWEQGVYDYKALPRPGATEQLDTNIGASWSYDPSSREMVSYDTVAAADLKAAYIQSRRLGGAMWWETSADKGGKTANKADGSLIGTFVEDVGGVNNLDRTQNAISYPDSQYDNLKAGFPSS |
| Enzyme Length | 398 |
| Uniprot Accession Number | Q92222 |
| Absorption | |
| Active Site | ACT_SITE 138; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258 |
| Activity Regulation | |
| Binding Site | BINDING 139; /note=Chitooligosaccharide; /evidence=ECO:0000255|PROSITE-ProRule:PRU01258; BINDING 342; /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:17119968, ECO:0000269|PubMed:17455791}; |
| DNA Binding | |
| EC Number | 3.2.1.14 |
| Enzyme Function | FUNCTION: Major 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) (PubMed:17119968, PubMed:17455791). Plays a role in the morphogenesis and autolysis. Has also significant antifungal activity against various fungal species (PubMed:17119968). Hydrolyzes chitin. Hydrolyzes glycol chitosan very effectively and liberates also reducing sugars from cell debris. Hydrolyzes synthetic substrates 4-nitrophenyl N,N'-diacetyl-beta-D-chitobioside (4NP(GlcNAc)2) and 4-nitrophenyl N,N',N''-triacetyl-beta-D-chitotrioside (4NP(GlcNAc)3), but has no activity against 4-nitrophenyl N-acetyl-beta-D-glucosaminide (4NPGlcNAc) (PubMed:17455791). {ECO:0000269|PubMed:17119968, ECO:0000269|PubMed:17455791}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (2); Chain (1); Domain (1); Glycosylation (2); Region (3) |
| Keywords | Carbohydrate metabolism;Chitin degradation;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted |
| Interact With | |
| Induction | INDUCTION: Expression is increased when the wild-type mycelia are starved for carbon sources, a condition that induces hyphal autolysis (PubMed:17119968). Significantly up-regulated expression with colloidal chitin and chito-oligomers, namely N-acetyl-D-glucosamine (GlcNAc), N,N'-diacetylchitobiose (GlcNAc)2 and N,N',N''-triacetylchitotriose (GlcNAc)3. Expression is not affected by changes in the levels of reactive oxygen species or in the glutathione-glutathione disulfide redox balance, the changes which are physiological characteristics developing in aging and autolyzing fungal cultures. Down-regulated by the oxidative-stress-generating agent diamide, but not by menadione or hydrogen peroxide (PubMed:17455791). {ECO:0000269|PubMed:17119968, ECO:0000269|PubMed:17455791}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17455791}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 44,206 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |