Detail Information for IndEnz0010000559
IED ID IndEnz0010000559
Enzyme Type ID esterase000559
Protein Name Lysozyme C-2
EC 3.2.1.17
1,4-beta-N-acetylmuramidase C
Gene Name LYZ2
Organism Bos taurus (Bovine)
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 Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine)
Enzyme Sequence MKALVILGFLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKATNYNPSSESTDYGIFQINSKWWCNDGKTPNAVDGCHVSCSELMENDIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL
Enzyme Length 147
Uniprot Accession Number Q06283
Absorption
Active Site ACT_SITE 53; /evidence=ECO:0000255|PROSITE-ProRule:PRU00680; ACT_SITE 71; /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 (6); Chain (1); Disulfide bond (4); Domain (1); Helix (7); Signal peptide (1); Turn (4)
Keywords 3D-structure;Antimicrobial;Bacteriolytic enzyme;Digestion;Disulfide bond;Glycosidase;Hydrolase;Reference proteome;Signal
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000250
Structure 3D X-ray crystallography (1)
Cross Reference PDB 2Z2F;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 16,304
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.17;