Detail Information for IndEnz0002018692
IED ID IndEnz0002018692
Enzyme Type ID protease018692
Protein Name Dipeptidase 3
EC 3.4.13.19
Gene Name DPEP3 UNQ834/PRO1772
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 MQPTGREGSRALSRRYLRRLLLLLLLLLLRQPVTRAETTPGAPRALSTLGSPSLFTTPGVPSALTTPGLTTPGTPKTLDLRGRAQALMRSFPLVDGHNDLPQVLRQRYKNVLQDVNLRNFSHGQTSLDRLRDGLVGAQFWSASVSCQSQDQTAVRLALEQIDLIHRMCASYSELELVTSAEGLNSSQKLACLIGVEGGHSLDSSLSVLRSFYVLGVRYLTLTFTCSTPWAESSTKFRHHMYTNVSGLTSFGEKVVEELNRLGMMIDLSYASDTLIRRVLEVSQAPVIFSHSAARAVCDNLLNVPDDILQLLKKNGGIVMVTLSMGVLQCNLLANVSTVADHFDHIRAVIGSEFIGIGGNYDGTGRFPQGLEDVSTYPVLIEELLSRSWSEEELQGVLRGNLLRVFRQVEKVREESRAQSPVEAEFPYGQLSTSCHSHLVPQNGHQATHLEVTKQPTNRVPWRSSNASPYLVPGLVAAATIPTFTQWLC
Enzyme Length 488
Uniprot Accession Number Q9H4B8
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by L-penicillamine. {ECO:0000250|UniProtKB:Q9DA79}.
Binding Site
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:Q9DA79, ECO:0000255|PROSITE-ProRule:PRU10073}; CATALYTIC ACTIVITY: Reaction=2 H2O + L-cystine-bis-glycine = 2 glycine + L-cystine; Xref=Rhea:RHEA:60520, ChEBI:CHEBI:15377, ChEBI:CHEBI:35491, ChEBI:CHEBI:57305, ChEBI:CHEBI:143812; Evidence={ECO:0000250|UniProtKB:Q9DA79};
DNA Binding
EC Number 3.4.13.19
Enzyme Function FUNCTION: Dipeptidase that hydrolyzes cystinyl-bis-glycine. Does not hydrolyze leukotriene D4 (LTD4) into leukotriene E4 (LTE4). {ECO:0000250|UniProtKB:Q9DA79}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (14); Chain (1); Disulfide bond (3); Erroneous initiation (4); Glycosylation (1); Helix (19); Lipidation (1); Metal binding (6); Propeptide (1); Sequence conflict (2); Signal peptide (1); Turn (4)
Keywords 3D-structure;Dipeptidase;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9DA79}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9DA79}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..35; /evidence=ECO:0000255
Structure 3D X-ray crystallography (2)
Cross Reference PDB 6VGO; 6VGR;
Mapped Pubmed ID 12144777; 2768222; 32325220; 3563417; 6293969; 7764673; 8439558;
Motif
Gene Encoded By
Mass 53,687
Kinetics
Metal Binding METAL 97; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 99; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 196; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 196; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 269; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 290; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073
Rhea ID RHEA:48940; RHEA:60520
Cross Reference Brenda