| IED ID | IndEnz0010000591 |
| Enzyme Type ID | esterase000591 |
| Protein Name |
Lysozyme C EC 3.2.1.17 1,4-beta-N-acetylmuramidase C |
| Gene Name | LYZ |
| Organism | Equus asinus (Donkey) (Equus africanus asinus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Perissodactyla (odd-toed ungulates) Equidae (horses) Equus Asinus Equus asinus (Donkey) (Equus africanus asinus) |
| Enzyme Sequence | KVFSKCELAHKLKAQEMDGFGGYSLANWVCMAEYESNFNTRAFNGKNANGSYDYGLFQLNSKWWCKDNKRSSSNACNIMCSKLLDDNIDDDISCAKRVVRDPKGMSAWKAWVKHCKDKDLSEYLASCNL |
| Enzyme Length | 129 |
| Uniprot Accession Number | P11375 |
| Absorption | |
| Active Site | ACT_SITE 35; /evidence=ECO:0000255|PROSITE-ProRule:PRU00680; ACT_SITE 53; /evidence=ECO:0000255|PROSITE-ProRule:PRU00680 |
| 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 (3); Chain (1); Disulfide bond (4); Domain (1); Helix (8); Metal binding (5); Turn (4) |
| Keywords | 3D-structure;Antimicrobial;Bacteriolytic enzyme;Calcium;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Milk protein |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5XUW; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 14,688 |
| Kinetics | |
| Metal Binding | METAL 82; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P81708; METAL 85; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P81708; METAL 87; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P81708; METAL 90; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P81708; METAL 91; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P81708 |
| Rhea ID | |
| Cross Reference Brenda |