| IED ID | IndEnz0010000614 |
| Enzyme Type ID | esterase000614 |
| Protein Name |
Lysozyme C EC 3.2.1.17 1,4-beta-N-acetylmuramidase C |
| Gene Name | |
| Organism | Penaeus merguiensis (Banana prawn) (Fenneropenaeus merguiensis) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Crustacea Multicrustacea Malacostraca Eumalacostraca Eucarida Decapoda Dendrobranchiata Penaeoidea Penaeidae (penaeid shrimps) Penaeus Penaeus merguiensis (Banana prawn) (Fenneropenaeus merguiensis) |
| Enzyme Sequence | MRVLPLALLVGLLAVSDAKVLGKCEFARLLETRYNLSRNDIKNWVCIAEFESSFNTAATNRNRNRSTDYGIFQINNKYWCGSDYGKNVCGIPCSDLMSDDITAALRCAETVRRATERYRGRGKGYTAWVAYNSKCKKRDLDQYMAECWSRGSNSIFPF |
| Enzyme Length | 158 |
| Uniprot Accession Number | C1IIX1 |
| Absorption | |
| Active Site | ACT_SITE 51; /evidence=ECO:0000255|PROSITE-ProRule:PRU00680; ACT_SITE 68; /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; Evidence={ECO:0000255|PROSITE-ProRule:PRU00680}; |
| 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 (By similarity). Has bacteriolytic activity against Gram-positive bacterium M.luteus, and Gram-negative shrimp pathogenic bacteria V.alginolyticus, V.parahaemolyticus and V.vulnificus. May play a role in host defense (PubMed:18798009). {ECO:0000255|PROSITE-ProRule:PRU00680, ECO:0000269|PubMed:18798009}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (4); Domain (1); Signal peptide (1) |
| Keywords | Antimicrobial;Bacteriolytic enzyme;Disulfide bond;Glycosidase;Hydrolase;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: (Microbial infection) Expression is up-regulated in response to heat-killed V.alginolyticus injection in kidney, hepatopancreas and muscle, with the strongest up-regulation in hemolymph, gill, gonad and lymphoid organ. After M.luteus challenge there is an increase in expression level at 2 (11.3-fold) and 6 hours (18.3-fold) postinjection, with the maximum level at 8 hours (25.4-fold), and then lowering down to the original level at 16 hours postinjection. After V.alginolyticus challenge there is significant increase in expression level at 4, 6 and 8 hours postinjection, with the maximum level at 16 hours (15.7-fold), and then down-regulated at 24 hours postinjection. {ECO:0000269|PubMed:18798009}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P85045}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 17,999 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |