| IED ID | IndEnz0009000265 |
| Enzyme Type ID | chitinase000265 |
| Protein Name |
Lysozyme 1 EC 3.2.1.17 1,4-beta-N-acetylmuramidase 1 Invertebrate-type lysozyme 1 cv-lysozyme 1 |
| Gene Name | lysoz1 lysoz |
| Organism | Crassostrea virginica (Eastern oyster) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Mollusca Bivalvia Autobranchia Pteriomorphia Ostreida Ostreoidea Ostreidae (oysters) Crassostrea Crassostrea virginica (Eastern oyster) |
| Enzyme Sequence | MNGLILFCAVVFATAVCTYGSDAPCLRAGGRCQHDSITCSGRYRTGLCSGGVRRRCCVPSSSNSGSFSTGMVSQQCLRCICNVESGCRPIGCHWDVNSDSCGYFQIKRAYWIDCGSPGGDWQTCANNLACSSRCVQAYMARYHRRSGCSNSCESFARIHNGGPRGCRNSNTEGYWRRVQAQGCN |
| Enzyme Length | 184 |
| Uniprot Accession Number | P83673 |
| Absorption | |
| Active Site | ACT_SITE 84; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01257; ACT_SITE 95; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01257 |
| Activity Regulation | |
| Binding Site | BINDING 138; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q8IU26 |
| 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:15364284}; |
| DNA Binding | |
| EC Number | 3.2.1.17 |
| Enzyme Function | FUNCTION: Has antibacterial activity against the Gram-positive bacteria L.garvieae, M.luteus and Enterococcus sp., and the Gram-negative bacteria E.coli and V.vulnificus. Weak antibacterial activity against the Gram-negative bacterium A.hydrophila. No antibacterial activity detected against the Gram-positive bacterium S.iniae or against the Gram-negative bacterium E.ictaluri. Shows some chitinase activity but no isopeptidase activity. {ECO:0000269|PubMed:15364284, ECO:0000269|PubMed:17160350}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Activity increases as temperature increases from 0 to 45 degrees Celsius and decreases markedly at temperatures greater than 55 degrees Celsius. {ECO:0000269|PubMed:15364284}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:15364284}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (1); Chain (1); Disulfide bond (6); Domain (1); Region (2); Sequence conflict (4); Signal peptide (1) |
| Keywords | Antibiotic;Antimicrobial;Bacteriolytic enzyme;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15364284}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000269|PubMed:15364284 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 19,986 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |