| IED ID | IndEnz0010000590 |
| Enzyme Type ID | esterase000590 |
| Protein Name |
Lysozyme C EC 3.2.1.17 1,4-beta-N-acetylmuramidase C |
| Gene Name | |
| Organism | Dromaius novaehollandiae (Emu) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Palaeognathae Casuariiformes (Emu and cassowaries) Dromaiidae (emus) Dromaius Dromaius novaehollandiae (Emu) |
| Enzyme Sequence | MKFFLILGFCLLPLIAQGKVFQRCELAAAMKKHGLSNYRGYSLGHWVCAAKYESNFNTAAINRNRDGSSDYGILQINSRWWCNDGRTSGAKNLCKISCSALLSSDITASVNCAKRVVSDKNGMNAWVAWRNHCKGRDVSQWIRGCRV |
| Enzyme Length | 147 |
| Uniprot Accession Number | G3XDT7 |
| Absorption | |
| Active Site | ACT_SITE 53; /evidence="ECO:0000250|UniProtKB:P00698, ECO:0000255|PROSITE-ProRule:PRU00680"; ACT_SITE 70; /evidence="ECO:0000250|UniProtKB:P00698, ECO:0000255|PROSITE-ProRule:PRU00680" |
| Activity Regulation | |
| Binding Site | BINDING 119; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00698 |
| 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:0000250|UniProtKB:P00698}; |
| DNA Binding | |
| EC Number | 3.2.1.17 |
| Enzyme Function | FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus. {ECO:0000255|PROSITE-ProRule:PRU00680, ECO:0000269|PubMed:22044478}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (1); Chain (1); Disulfide bond (4); Domain (1); Signal peptide (1) |
| Keywords | Antimicrobial;Bacteriolytic enzyme;Disulfide bond;Glycosidase;Hydrolase;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00698}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 16,443 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |