Detail Information for IndEnz0002016235
IED ID IndEnz0002016235
Enzyme Type ID protease016235
Protein Name Meprin A subunit alpha
EC 3.4.24.18
Endopeptidase-2
N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit alpha
PABA peptide hydrolase
PPH alpha
Gene Name MEP1A
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 MAWIRSTCILFFTLLFAHIAAVPIKYLPEENVHDADFGEQKDISEINLAAGLDLFQGDILLQKSRNGLRDPNTRWTFPIPYILADNLGLNAKGAILYAFEMFRLKSCVDFKPYEGESSYIIFQQFDGCWSEVGDQHVGQNISIGQGCAYKAIIEHEILHALGFYHEQSRTDRDDYVNIWWDQILSGYQHNFDTYDDSLITDLNTPYDYESLMHYQPFSFNKNASVPTITAKIPEFNSIIGQRLDFSAIDLERLNRMYNCTTTHTLLDHCTFEKANICGMIQGTRDDTDWAHQDSAQAGEVDHTLLGQCTGAGYFMQFSTSSGSAEEAALLESRILYPKRKQQCLQFFYKMTGSPSDRLVVWVRRDDSTGNVRKLVKVQTFQGDDDHNWKIAHVVLKEEQKFRYLFQGTKGDPQNSTGGIYLDDITLTETPCPTGVWTVRNFSQVLENTSKGDKLQSPRFYNSEGYGFGVTLYPNSRESSGYLRLAFHVCSGENDAILEWPVENRQVIITILDQEPDVRNRMSSSMVFTTSKSHTSPAINDTVIWDRPSRVGTYHTDCNCFRSIDLGWSGFISHQMLKRRSFLKNDDLIIFVDFEDITHLSQTEVPTKGKRLSPQGLILQGQEQQVSEEGSGKAMLEEALPVSLSQGQPSRQKRSVENTGPLEDHNWPQYFRDPCDPNPCQNDGICVNVKGMASCRCISGHAFFYTGERCQAVQVHGSVLGMVIGGTAGVIFLTFSIIAILSQRPRK
Enzyme Length 746
Uniprot Accession Number Q16819
Absorption
Active Site ACT_SITE 156; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211
Activity Regulation ACTIVITY REGULATION: Inhibited by several hydroxamate compounds, the most potent inhibitor is actinonin. {ECO:0000269|PubMed:17976009}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues.; EC=3.4.24.18;
DNA Binding
EC Number 3.4.24.18
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (8); Domain (4); Glycosylation (7); Metal binding (3); Natural variant (5); Propeptide (1); Region (1); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix;Zinc;Zymogen
Interact With P14780
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
Modified Residue
Post Translational Modification PTM: N-glycosylated; contains GlcNAc, galactose, mannose and a small amount of fucose. {ECO:0000250}.
Signal Peptide SIGNAL 1..21; /evidence=ECO:0000250
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12189145; 16378686; 17195012; 19262505; 20631730; 20806899; 22096485; 22326557; 22923609; 23123160; 24388959; 24474695; 27378469; 27999200; 28502593;
Motif
Gene Encoded By
Mass 84,419
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=110 uM for GRP {ECO:0000269|PubMed:17976009}; KM=18.0 uM for PTH 12-34 {ECO:0000269|PubMed:17976009}; KM=33.9 uM for secretin {ECO:0000269|PubMed:17976009}; KM=41.3 uM for substance P {ECO:0000269|PubMed:17976009}; KM=56.5 uM for LHRH {ECO:0000269|PubMed:17976009}; KM=73.2 uM for orcokinin {ECO:0000269|PubMed:17976009}; KM=292 uM for alpha-MSH {ECO:0000269|PubMed:17976009}; KM=125 uM for bradykinin {ECO:0000269|PubMed:17976009}; KM=200 uM for gastrin {ECO:0000269|PubMed:17976009};
Metal Binding METAL 155; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 159; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 165; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211
Rhea ID
Cross Reference Brenda 3.4.24.18;