IED ID | IndEnz0010000619 |
Enzyme Type ID | esterase000619 |
Protein Name |
Lysozyme C EC 3.2.1.17 1,4-beta-N-acetylmuramidase C Fragment |
Gene Name | LYZ |
Organism | Pseudocheirus peregrinus (Common ring-tailed possum) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Metatheria Diprotodontia Pseudocheiridae (ring-tailed possums) Pseudocheirus Pseudocheirus peregrinus (Common ring-tailed possum) |
Enzyme Sequence | SKMKKCEFAKIAKEQHMDGYHGVSLADWVCLVNNESDFNTKAINRNKGI |
Enzyme Length | 49 |
Uniprot Accession Number | P21776 |
Absorption | |
Active Site | ACT_SITE 35; /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 (1); Chain (1); Domain (1); Non-terminal residue (1) |
Keywords | Antimicrobial;Bacteriolytic enzyme;Direct protein sequencing;Glycosidase;Hydrolase;Milk protein;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 | 5,570 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |