IED ID | IndEnz0010000580 |
Enzyme Type ID | esterase000580 |
Protein Name |
Lysozyme C EC 3.2.1.17 1,4-beta-N-acetylmuramidase C |
Gene Name | LYZ |
Organism | Chelonia mydas (Green sea-turtle) (Chelonia agassizi) |
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 Testudinata Testudines (turtles) Cryptodira (hidden-necked turtles) Durocryptodira Americhelydia Chelonioidea Cheloniidae (sea turtles) Chelonia Chelonia mydas (Green sea-turtle) (Chelonia agassizi) |
Enzyme Sequence | KTYERCELARAMKRLGLDGYWGYSLGHWVCAAKYESNFNTGATNYNPGDQSTDYGILQINSRWWCNDGKTPRTKNACKIQCRELLTADITASVNCAKRVVRDPNGMGAWVAWTKNCKGRDVSPWIRDCGL |
Enzyme Length | 130 |
Uniprot Accession Number | P84492 |
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. {ECO:0000255|PROSITE-ProRule:PRU00680}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Disulfide bond (4); Domain (1) |
Keywords | Antimicrobial;Bacteriolytic enzyme;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Secreted |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 14,704 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |