| IED ID | IndEnz0009000316 |
| Enzyme Type ID | chitinase000316 |
| Protein Name |
Lysozyme 2 EC 3.2.1.17 1,4-beta-N-acetylmuramidase 2 Invertebrate-type lysozyme 2 cv-lysozyme 2 |
| Gene Name | lysoz2 |
| 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 | MNFLILFCVVASASVVYSSISDQCLRCICEVESGCRAIGCHWDVYSNSCGYFQIKQGYWTDCGSPGHSMESCADNYNCASGCVRSYMDHYIKYNGCADTCESYARMHNGGPNGCKSSHHHATDNYWRLVQAKGCS |
| Enzyme Length | 135 |
| Uniprot Accession Number | Q1XG90 |
| Absorption | |
| Active Site | ACT_SITE 32; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01257; ACT_SITE 43; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01257 |
| Activity Regulation | ACTIVITY REGULATION: Activity decreased by 80% by addition of 0.01 M calcium, zinc or magnesium. Activity only decreased by 17% by addition of ammonium, and by 2% by addition of sodium. {ECO:0000269|PubMed:17160350}. |
| Binding Site | BINDING 86; /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:17160350}; |
| DNA Binding | |
| EC Number | 3.2.1.17 |
| Enzyme Function | FUNCTION: The main role of this lysozyme is in digestion. Has antibacterial activity against the Gram-positive bacterium P.cerevisiae and the Gram-negative bacteria E.coli and V.vulnificus. Shows some chitinase activity but no isopeptidase activity. {ECO:0000269|PubMed:17160350}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. No decrease in activity was detected after incubation at 30 degrees Celsius for 30 minutes. No activity could be detected after incubation at 90 degrees Celsius for 30 minutes or 100 degrees Celsius for 10 minutes. {ECO:0000269|PubMed:17160350}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Retains more than 90% of its maximum activity between pH 5.4 and 6.4 in the ionic strength range of I=0.005-0.01. In buffers of I=0.005 more than 75% of maximum activity is retained between pH 5.3 and 7.5. In buffers of I=0.02 more than 75% of maximum activity is retained between pH 5.3 and 6.5. {ECO:0000269|PubMed:17160350}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (1); Chain (1); Disulfide bond (6); Domain (1); Region (2); 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. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:17160350 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 14,950 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |