| IED ID | IndEnz0009000143 |
| Enzyme Type ID | chitinase000143 |
| Protein Name |
Invertebrate-type lysozyme EC 3.2.1.17 1,4-beta-N-acetylmuramidase Destabilase |
| Gene Name | |
| Organism | Ruditapes philippinarum (Japanese littleneck clam) (Venerupis philippinarum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Mollusca Bivalvia Autobranchia Heteroconchia Euheterodonta Imparidentia Neoheterodontei Venerida Veneroidea Veneridae (venus clams) Ruditapes Ruditapes philippinarum (Japanese littleneck clam) (Venerupis philippinarum) |
| Enzyme Sequence | METVSVEEGLDFAPGMVSQKCLLCMCKLESGGCKPIGCRMDVGSLSCGYFQIKQPYWIDCGKPGKDWKSCSNDINCSSKCVQQYMKRYATHYRCPLNCEGFAREHNGGPNGCHSSRTLKYWELLQKIPGCKGVKFS |
| Enzyme Length | 136 |
| Uniprot Accession Number | Q8IU26 |
| Absorption | |
| Active Site | ACT_SITE 29; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01257, ECO:0000269|PubMed:17631496"; ACT_SITE 41; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01257, ECO:0000269|PubMed:17631496" |
| Activity Regulation | ACTIVITY REGULATION: Chitinase activity is activated by high salt concentrations which cause the release of the monomer from the autoinhibited homodimer. {ECO:0000269|PubMed:17631496}. |
| Binding Site | BINDING 84; /note="Substrate"; /evidence="ECO:0000269|PubMed:17631496, ECO:0007744|PDB:2DQA"; BINDING 92; /note="Substrate"; /evidence="ECO:0000269|PubMed:17631496, ECO:0007744|PDB:2DQA"; BINDING 119; /note="Substrate"; /evidence="ECO:0000269|PubMed:17631496, ECO:0007744|PDB:2DQA" |
| 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:14523554, ECO:0000269|PubMed:15249048, ECO:0000269|PubMed:17631496, ECO:0000269|PubMed:9914527}; |
| DNA Binding | |
| EC Number | 3.2.1.17 |
| Enzyme Function | FUNCTION: Bacteriolytic activity against Gram-positive bacterium M.luteus and thereby probably protects against bacterial infection (PubMed:9914527, PubMed:14523554, PubMed:15249048). Also has chitinase activity (PubMed:15249048, PubMed:9914527, PubMed:17631496, PubMed:14523554). May act as an ispopeptidase, cleaving isopeptide bonds between the side chains of Lys and Gln residues in proteins or in the cross-linking peptide of peptidoglycan in bacterial cell walls (PubMed:15249048, PubMed:14523554). {ECO:0000269|PubMed:14523554, ECO:0000269|PubMed:15249048, ECO:0000269|PubMed:17631496, ECO:0000269|PubMed:9914527}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 76 degrees Celsius. {ECO:0000269|PubMed:9914527}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-5 at 40 degrees Celsius for chitinase activity. {ECO:0000269|PubMed:9914527}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (4); Binding site (3); Chain (1); Disulfide bond (7); Domain (1); Glycosylation (1); Helix (8); Mutagenesis (2); Region (2); Sequence conflict (1); Signal peptide (1); Site (1); Turn (1) |
| Keywords | 3D-structure;Antibiotic;Antimicrobial;Bacteriolytic enzyme;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83673}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..11; /evidence="ECO:0000269|PubMed:14523554, ECO:0000269|PubMed:9914527" |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2DQA; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 15,198 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=34 uM for p-nitrophenyl beta 1,4-linked pentamer of N-acetyl-D-glucosamine ((GlcNAc)5-PNP) at pH 5 and 40 degrees Celsius {ECO:0000269|PubMed:9914527}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |