Detail Information for IndEnz0010000596
IED ID IndEnz0010000596
Enzyme Type ID esterase000596
Protein Name Lysozyme C
EC 3.2.1.17
1,4-beta-N-acetylmuramidase C
Gene Name LYZ LZM
Organism Homo sapiens (Human)
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 Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV
Enzyme Length 148
Uniprot Accession Number P61626
Absorption
Active Site ACT_SITE 53; ACT_SITE 71
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 (7); Chain (1); Disulfide bond (4); Domain (1); Erroneous initiation (1); Helix (8); Natural variant (3); Sequence conflict (6); Signal peptide (1); Turn (5)
Keywords 3D-structure;Amyloid;Amyloidosis;Antimicrobial;Bacteriolytic enzyme;Direct protein sequencing;Disease variant;Disulfide bond;Glycosidase;Hydrolase;Reference proteome;Secreted;Signal
Interact With Itself
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..18; /evidence="ECO:0000269|PubMed:11946553, ECO:0000269|PubMed:11946554, ECO:0000269|PubMed:25946035, ECO:0000269|PubMed:5168859, ECO:0000269|PubMed:5284421"
Structure 3D X-ray crystallography (207); NMR spectroscopy (2); Neutron diffraction (1)
Cross Reference PDB 133L; 134L; 1B5U; 1B5V; 1B5W; 1B5X; 1B5Y; 1B5Z; 1B7L; 1B7M; 1B7N; 1B7O; 1B7P; 1B7Q; 1B7R; 1B7S; 1BB3; 1BB4; 1BB5; 1C43; 1C45; 1C46; 1C7P; 1CJ6; 1CJ7; 1CJ8; 1CJ9; 1CKC; 1CKD; 1CKF; 1CKG; 1CKH; 1D6P; 1D6Q; 1DI3; 1DI4; 1DI5; 1EQ4; 1EQ5; 1EQE; 1GAY; 1GAZ; 1GB0; 1GB2; 1GB3; 1GB5; 1GB6; 1GB7; 1GB8; 1GB9; 1GBO; 1GBW; 1GBX; 1GBY; 1GBZ; 1GDW; 1GDX; 1GE0; 1GE1; 1GE2; 1GE3; 1GE4; 1GEV; 1GEZ; 1GF0; 1GF3; 1GF4; 1GF5; 1GF6; 1GF7; 1GF8; 1GF9; 1GFA; 1GFE; 1GFG; 1GFH; 1GFJ; 1GFK; 1GFR; 1GFT; 1GFU; 1GFV; 1HNL; 1I1Z; 1I20; 1I22; 1INU; 1IOC; 1IP1; 1IP2; 1IP3; 1IP4; 1IP5; 1IP6; 1IP7; 1IWT; 1IWU; 1IWV; 1IWW; 1IWX; 1IWY; 1IWZ; 1IX0; 1IY3; 1IY4; 1JKA; 1JKB; 1JKC; 1JKD; 1JSF; 1JWR; 1LAA; 1LHH; 1LHI; 1LHJ; 1LHK; 1LHL; 1LHM; 1LMT; 1LOZ; 1LYY; 1LZ1; 1LZ4; 1LZ5; 1LZ6; 1LZR; 1LZS; 1OP9; 1OUA; 1OUB; 1OUC; 1OUD; 1OUE; 1OUF; 1OUG; 1OUH; 1OUI; 1OUJ; 1QSW; 1RE2; 1REM; 1REX; 1REY; 1REZ; 1TAY; 1TBY; 1TCY; 1TDY; 1UBZ; 1W08; 1WQM; 1WQN; 1WQO; 1WQP; 1WQQ; 1WQR; 1YAM; 1YAN; 1YAO; 1YAP; 1YAQ; 207L; 208L; 2BQA; 2BQB; 2BQC; 2BQD; 2BQE; 2BQF; 2BQG; 2BQH; 2BQI; 2BQJ; 2BQK; 2BQL; 2BQM; 2BQN; 2BQO; 2HEA; 2HEB; 2HEC; 2HED; 2HEE; 2HEF; 2LHM; 2MEA; 2MEB; 2MEC; 2MED; 2MEE; 2MEF; 2MEG; 2MEH; 2MEI; 2NWD; 2ZIJ; 2ZIK; 2ZIL; 2ZWB; 3EBA; 3FE0; 3LHM; 3LN2; 4I0C; 4ML7; 4R0P; 5LSH; 5LVK; 6LFH; 7AP7;
Mapped Pubmed ID 10350481; 10391242; 10411933; 10469827; 10504240; 10556244; 10561612; 10583407; 10630988; 10810162; 10913274; 11015217; 11087397; 11294653; 11340658; 11401442; 11455596; 11467836; 11599030; 118839; 11887182; 11927576; 11986950; 12183536; 12198298; 12214315; 12359083; 12564923; 12646687; 1270801; 12709420; 12720276; 12917687; 1363898; 13816; 1390708; 14743216; 14976184; 15155566; 1525170; 15299791; 15713462; 15962837; 16023673; 16126226; 16329101; 16416029; 1643041; 16441658; 16799949; 17054380; 17353931; 17360367; 17407782; 17524359; 18029788; 18344136; 1837051; 18391951; 18449172; 18484335; 1849145; 18591461; 19010777; 19179970; 1939116; 19435495; 19563039; 19615732; 20167661; 20452482; 20673868; 20711500; 20807650; 21182203; 2118650; 21408218; 21460390; 21486364; 21574221; 2195544; 21965601; 22096116; 22810585; 22909819; 23155290; 23264227; 23353684; 23650620; 23902751; 23919586; 2409350; 24121782; 24189400; 24296430; 24308818; 24340941; 24495950; 25217048; 25236863; 25417112; 25474758; 25575179; 25604459; 25609649; 25659958; 25706123; 25914748; 26961596; 27177644; 27294141; 27428539; 27825804; 27926837; 27931094; 279930; 28419103; 2900981; 29233221; 29446150; 3035556; 3053705; 3080684; 3094007; 31391320; 3142462; 31694163; 31978114; 32333711; 32522553; 33640796; 7473760; 7890692; 7990138; 8097946; 8105095; 8159701; 8486712; 8490014; 8692836; 8870004; 8885835; 8902616; 9006323; 9010773; 9020766; 9039909; 9041653; 9054935; 9398521; 9517539; 9649316; 9677301; 9757098; 9852096; 9862427; 9888793;
Motif
Gene Encoded By
Mass 16,537
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.17;