| IED ID | IndEnz0009000142 |
| Enzyme Type ID | chitinase000142 |
| Protein Name |
Lysozyme EC 3.2.1.17 1,4-beta-N-acetylmuramidase Invertebrate-type lysozyme |
| Gene Name | |
| Organism | Meretrix lusoria (Hard clam) (Common Orient clam) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Mollusca Bivalvia Autobranchia Heteroconchia Euheterodonta Imparidentia Neoheterodontei Venerida Veneroidea Veneridae (venus clams) Meretrix Meretrix lusoria (Hard clam) (Common Orient clam) |
| Enzyme Sequence | FAGGIVSQRCLSCICKMESGCRNVGCKMDMGSLSCGYFQIKEAYWIDCGRPGSSWKSCAASSYCASLCVQNYMKRYAKWAGCPLRCEGFAREHNGGPRGCKKGSTIGYWNRLQKISGCHGVQ |
| Enzyme Length | 122 |
| Uniprot Accession Number | P86383 |
| Absorption | |
| Active Site | ACT_SITE 18; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01257; ACT_SITE 29; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01257 |
| Activity Regulation | |
| Binding Site | BINDING 72; /note="Substrate"; /evidence="ECO:0000269|PubMed:24192349, ECO:0000305|Ref.2, ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ"; BINDING 93; /note="Substrate"; /evidence="ECO:0000269|PubMed:24192349, ECO:0000305|Ref.2, ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ"; BINDING 102; /note="Substrate"; /evidence="ECO:0000269|PubMed:24192349, ECO:0000305|Ref.2, ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; Evidence={ECO:0000269|PubMed:24200802}; |
| DNA Binding | |
| EC Number | 3.2.1.17 |
| Enzyme Function | FUNCTION: Has bacteriolytic activity against Gram-positive bacteria M.luteus. Also has chitinase activity. {ECO:0000269|PubMed:24200802}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 at 37 degrees Celsius for bacteriolytic activity. Optimum pH is 3 at 40 degrees Celsius for chitinase activity. {ECO:0000269|PubMed:24200802}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (4); Binding site (3); Chain (1); Disulfide bond (7); Domain (1); Helix (9); Natural variant (1); Region (2); Turn (1) |
| Keywords | 3D-structure;Antibiotic;Antimicrobial;Bacteriolytic enzyme;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83673}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3AB6; 3AYQ; 4PJ2; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 13,377 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.17; |