| IED ID | IndEnz0002010483 |
| Enzyme Type ID | protease010483 |
| Protein Name |
Neurolysin, mitochondrial EC 3.4.24.16 Angiotensin-binding protein Microsomal endopeptidase MEP Mitochondrial oligopeptidase M Neurotensin endopeptidase |
| Gene Name | NLN AGTBP KIAA1226 |
| 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 | MIARCLLAVRSLRRVGGSRILLRMTLGREVMSPLQAMSSYTVAGRNVLRWDLSPEQIKTRTEELIVQTKQVYDAVGMLGIEEVTYENCLQALADVEVKYIVERTMLDFPQHVSSDKEVRAASTEADKRLSRFDIEMSMRGDIFERIVHLQETCDLGKIKPEARRYLEKSIKMGKRNGLHLPEQVQNEIKSMKKRMSELCIDFNKNLNEDDTFLVFSKAELGALPDDFIDSLEKTDDDKYKITLKYPHYFPVMKKCCIPETRRRMEMAFNTRCKEENTIILQQLLPLRTKVAKLLGYSTHADFVLEMNTAKSTSRVTAFLDDLSQKLKPLGEAEREFILNLKKKECKDRGFEYDGKINAWDLYYYMTQTEELKYSIDQEFLKEYFPIEVVTEGLLNTYQELLGLSFEQMTDAHVWNKSVTLYTVKDKATGEVLGQFYLDLYPREGKYNHAACFGLQPGCLLPDGSRMMAVAALVVNFSQPVAGRPSLLRHDEVRTYFHEFGHVMHQICAQTDFARFSGTNVETDFVEVPSQMLENWVWDVDSLRRLSKHYKDGSPIADDLLEKLVASRLVNTGLLTLRQIVLSKVDQSLHTNTSLDAASEYAKYCSEILGVAATPGTNMPATFGHLAGGYDGQYYGYLWSEVFSMDMFYSCFKKEGIMNPEVGMKYRNLILKPGGSLDGMDMLHNFLKREPNQKAFLMSRGLHAP |
| Enzyme Length | 704 |
| Uniprot Accession Number | Q9BYT8 |
| Absorption | |
| Active Site | ACT_SITE 498; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage in neurotensin: 10-Pro-|-Tyr-11.; EC=3.4.24.16; |
| DNA Binding | |
| EC Number | 3.4.24.16 |
| Enzyme Function | FUNCTION: Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (11); Chain (1); Helix (33); Metal binding (3); Modified residue (1); Natural variant (5); Transit peptide (1); Turn (11) |
| Keywords | 3D-structure;Acetylation;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Protease;Reference proteome;Transit peptide;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250}. Cytoplasm {ECO:0000250}. |
| Modified Residue | MOD_RES 664; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5LUZ; 5LV0; |
| Mapped Pubmed ID | 17251185; 20379614; 20877624; 21888893; 26496610; 27496565; 29183787; 32269163; 3525564; 7836437; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,652 |
| Kinetics | |
| Metal Binding | METAL 497; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 501; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 504; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.16; |