Detail Information for IndEnz0002005214
IED ID IndEnz0002005214
Enzyme Type ID protease005214
Protein Name Dipeptidase 2
EC 3.4.13.19
Gene Name DPEP2 UNQ284/PRO323
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 MQPSGLEGPGTFGRWPLLSLLLLLLLLQPVTCAYTTPGPPRALTTLGAPRAHTMPGTYAPSTTLSSPSTQGLQEQARALMRDFPLVDGHNDLPLVLRQVYQKGLQDVNLRNFSYGQTSLDRLRDGLVGAQFWSAYVPCQTQDRDALRLTLEQIDLIRRMCASYSELELVTSAKALNDTQKLACLIGVEGGHSLDNSLSILRTFYMLGVRYLTLTHTCNTPWAESSAKGVHSFYNNISGLTDFGEKVVAEMNRLGMMVDLSHVSDAVARRALEVSQAPVIFSHSAARGVCNSARNVPDDILQLLKKNGGVVMVSLSMGVIQCNPSANVSTVADHFDHIKAVIGSKFIGIGGDYDGAGKFPQGLEDVSTYPVLIEELLSRGWSEEELQGVLRGNLLRVFRQVEKVQEENKWQSPLEDKFPDEQLSSSCHSDLSRLRQRQSLTSGQELTEIPIHWTAKLPAKWSVSESSPHMAPVLAVVATFPVLILWL
Enzyme Length 486
Uniprot Accession Number Q9H4A9
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by L-penicillamine. {ECO:0000250|UniProtKB:Q8C255}.
Binding Site BINDING 215; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 293; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 351; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid; Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000250|UniProtKB:Q8C255, ECO:0000255|PROSITE-ProRule:PRU10073}; CATALYTIC ACTIVITY: Reaction=H2O + leukotriene D4 = glycine + leukotriene E4; Xref=Rhea:RHEA:48616, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:57462, ChEBI:CHEBI:63166; Evidence={ECO:0000250|UniProtKB:Q8C255};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48617; Evidence={ECO:0000250|UniProtKB:Q8C255};
DNA Binding
EC Number 3.4.13.19
Enzyme Function FUNCTION: Dipeptidase that hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4). Does not hydrolyze cystinyl-bis-glycine. {ECO:0000250|UniProtKB:Q8C255}.; FUNCTION: Independently of its dipeptidase activity can also modulate macrophage inflammatory response by acting as a regulator of NF-kappaB inflammatory signaling pathway. {ECO:0000250|UniProtKB:Q8C255}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (3); Binding site (3); Chain (1); Disulfide bond (3); Erroneous initiation (1); Glycosylation (3); Lipidation (1); Metal binding (6); Natural variant (2); Propeptide (1); Signal peptide (1)
Keywords Alternative splicing;Dipeptidase;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipid metabolism;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8C255}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8C255}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..32; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12144777; 20711500; 2768222; 3563417; 6293969; 7764673; 8439558;
Motif
Gene Encoded By
Mass 53,365
Kinetics
Metal Binding METAL 89; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 91; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 188; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 188; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 261; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 282; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073
Rhea ID RHEA:48940; RHEA:48616; RHEA:48617
Cross Reference Brenda