| IED ID | IndEnz0009000001 |
| Enzyme Type ID | chitinase000001 |
| Protein Name |
Endochitinase A EC 3.2.1.14 ChitA Chitinase-A Seed chitinase A allergen Zea m 8 |
| Gene Name | CHIA |
| Organism | Zea mays (Maize) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae PACMAD clade Panicoideae Andropogonodae Andropogoneae Tripsacinae Zea Zea mays (Maize) |
| Enzyme Sequence | MANAPRILALGLLALLCAAAGPAAAQNCGCQPNFCCSKFGYCGTTDAYCGDGCQSGPCRSGGGGGGGGGGGGGGSGGANVANVVTDAFFNGIKNQAGSGCEGKNFYTRSAFLSAVNAYPGFAHGGTEVEGKREIAAFFAHVTHETGHFCYISEINKSNAYCDASNRQWPCAAGQKYYGRGPLQISWNYNYGPAGRDIGFNGLADPNRVAQDAVIAFKTALWFWMNNVHGVMPQGFGATIRAINGALECNGNNPAQMNARVGYYKQYCQQLRVDPGPNLIC |
| Enzyme Length | 280 |
| Uniprot Accession Number | P29022 |
| Absorption | |
| Active Site | ACT_SITE 144; /note=Proton donor; /evidence=ECO:0000305|PubMed:24616181 |
| Activity Regulation | ACTIVITY REGULATION: Inactivated by l-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) in the absence of exogenous nucleophiles (e.g. GlcNAc4, GlcNAc3 and GlcNAc2) (PubMed:1740436). Not inhibited by tetra-N-acetylchitopentaose or modified chitotetraose substrate TMG-chitotriomycin-pMP, containing a free, non-acetylated glucosaminyl residue or a N-trimethylamino glucosamine (TMG) residue at the non-reducing terminus, respectively (PubMed:24616181). {ECO:0000269|PubMed:1740436, ECO:0000269|PubMed:24616181}. |
| Binding Site | |
| 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:1551872, ECO:0000269|PubMed:1740436, ECO:0000269|PubMed:24616181, ECO:0000269|PubMed:28328103}; |
| DNA Binding | |
| EC Number | 3.2.1.14 |
| Enzyme Function | FUNCTION: Defense against chitin-containing fungal pathogens (PubMed:1551872). Hydrolyzes glycol chitin and tetra-N-acetylchitotetraose in vitro (PubMed:28328103). {ECO:0000269|PubMed:1551872, ECO:0000269|PubMed:28328103}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Active between 50-70 degrees Celsius. {ECO:0000269|PubMed:28328103}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Active between pH 6-3. {ECO:0000269|PubMed:28328103}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (2); Chain (1); Disulfide bond (7); Domain (1); Helix (9); Mutagenesis (1); Region (2); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Allergen;Carbohydrate metabolism;Chitin degradation;Chitin-binding;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Plant defense;Polysaccharide degradation;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28328103}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4MCK; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 29,125 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.97 mM for tetra-N-acetylchitotetraose (at 37 degrees Celsius and pH 6) {ECO:0000269|PubMed:28328103}; KM=0.51 mM for tetra-N-acetylchitotetraose (at 37 degrees Celsius and pH 4) {ECO:0000269|PubMed:28328103}; KM=1.27 mM for tetra-N-acetylchitotetraose (at 50 degrees Celsius and pH 6) {ECO:0000269|PubMed:28328103}; KM=1.29 mM for tetra-N-acetylchitotetraose (at 70 degrees Celsius and pH 6) {ECO:0000269|PubMed:28328103}; Note=kcat is 56.27 sec(-1) with tetra-N-acetylchitotetraose as substrate (at 37 degrees Celsius and pH 6). kcat is 55.67 sec(-1) with tetra-N-acetylchitotetraose as substrate (at 37 degrees Celsius and pH 4). kcat is 69.01 sec(-1) with tetra-N-acetylchitotetraose as substrate (at 50 degrees Celsius and pH 6). kcat is 53.1 sec(-1) with tetra-N-acetylchitotetraose as substrate (at 70 degrees Celsius and pH 6). {ECO:0000269|PubMed:28328103}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.14; |