| IED ID | IndEnz0010000615 |
| Enzyme Type ID | esterase000615 |
| Protein Name |
Lysozyme C EC 3.2.1.17 1,4-beta-N-acetylmuramidase C |
| Gene Name | LYZ |
| Organism | Phasianus colchicus colchicus (Black-necked pheasant) |
| 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 Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Phasianus Phasianus colchicus (Common pheasant) Phasianus colchicus colchicus (Black-necked pheasant) |
| Enzyme Sequence | MRSLLILVLCFLPLAAPGKVYGRCELAAAMKRMGLDNYRGYSLGNWVCAAKFESNFNTGATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCHIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRKHCKGTDVNVWIRGCRL |
| Enzyme Length | 147 |
| Uniprot Accession Number | P00702 |
| Absorption | |
| Active Site | ACT_SITE 53; ACT_SITE 70 |
| Activity Regulation | |
| Binding Site | |
| 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; |
| 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (5); Chain (1); Disulfide bond (4); Domain (1); Helix (7); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;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 | PTM: By an evolutionary shift in the site of proteolytic cleavage of prelysozyme, Gly-18 became the N-terminal residue of the mature protein instead of being the C-terminal residue of the signal sequence as in other birds. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000269|PubMed:476049 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1GHL; 1JHL; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 16,166 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |