IED Industry Enzyme Database

Detail Information for IndEnz0002014314
IED ID IndEnz0002014314
Enzyme Type ID protease014314
Protein Name Cytosolic non-specific dipeptidase
EC 3.4.13.18
CNDP dipeptidase 2
Threonyl dipeptidase
Gene Name CNDP2
Organism Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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) Ponginae Pongo Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Enzyme Sequence MAALTTLFKYIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLGGSVELVDIGKQKLPDGSEIPLPPILLGRLGSDPQKKTVCIYGHLDVQPAALEDGWDSEPFTLVERDGKLHGRGSTDDKGPVAGWINALEAYQKTDQEIPVNVRFCLEGMEESGSEGLDELIFAQKDTFFKDVDYVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMGSLVDKRGNILIPGINEAVAAVTEEEHKLYDDIDFDIEEFAKDVGAQILLHSNKKDILMHRWRYPSLSLHGIEGAFSGSGAKTVIPRKVVGKFSIRLVPNMTPEVVSEQVTSYLTKKFAELRSPNEFKVYMGHGGKPWVSDFSHPHYVAGRRAMRTVFGVEPDLTREGGSIPVTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRHNYIEGTKMLAAYLYEVSQLKD
Enzyme Length 475
Uniprot Accession Number Q5R432
Absorption
Active Site ACT_SITE 101; /evidence=ECO:0000250; ACT_SITE 166; /note=Proton acceptor; /evidence=ECO:0000250
Activity Regulation
Binding Site BINDING 195; /note=Substrate; via carbonyl oxygen; /evidence=ECO:0000250; BINDING 228; /note=Substrate; shared with homodimeric partner; /evidence=ECO:0000250; BINDING 330; /note=Substrate; shared with homodimeric partner; /evidence=ECO:0000250; BINDING 343; /note=Substrate; /evidence=ECO:0000250; BINDING 417; /note=Substrate; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250; BINDING 445; /note=Substrate; /evidence=ECO:0000250
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.; EC=3.4.13.18; Evidence={ECO:0000250|UniProtKB:Q96KP4}; CATALYTIC ACTIVITY: Reaction=H2O + L-threonyl-L-threonine = 2 L-threonine; Xref=Rhea:RHEA:67360, ChEBI:CHEBI:15377, ChEBI:CHEBI:57926, ChEBI:CHEBI:169953; Evidence={ECO:0000250|UniProtKB:Q9D1A2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67361; Evidence={ECO:0000250|UniProtKB:Q9D1A2}; CATALYTIC ACTIVITY: Reaction=H2O + L-threonyl-L-serine = L-serine + L-threonine; Xref=Rhea:RHEA:67364, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57926, ChEBI:CHEBI:169954; Evidence={ECO:0000250|UniProtKB:Q9D1A2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67365; Evidence={ECO:0000250|UniProtKB:Q9D1A2}; CATALYTIC ACTIVITY: Reaction=H2O + L-seryl-L-threonine = L-serine + L-threonine; Xref=Rhea:RHEA:67372, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57926, ChEBI:CHEBI:169955; Evidence={ECO:0000250|UniProtKB:Q9D1A2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67373; Evidence={ECO:0000250|UniProtKB:Q9D1A2}; CATALYTIC ACTIVITY: Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine; Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235, ChEBI:CHEBI:57305, ChEBI:CHEBI:61694; Evidence={ECO:0000250|UniProtKB:Q96KP4};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784; Evidence={ECO:0000250|UniProtKB:Q96KP4}; CATALYTIC ACTIVITY: Reaction=(S)-lactate + L-phenylalanine = H2O + N-[(S)-lactoyl]-L-phenylalanine; Xref=Rhea:RHEA:66724, ChEBI:CHEBI:15377, ChEBI:CHEBI:16651, ChEBI:CHEBI:58095, ChEBI:CHEBI:167456; Evidence={ECO:0000250|UniProtKB:Q96KP4};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66725; Evidence={ECO:0000250|UniProtKB:Q96KP4};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:66726; Evidence={ECO:0000250|UniProtKB:Q96KP4};
DNA Binding
EC Number 3.4.13.18
Enzyme Function FUNCTION: Catalyzes the peptide bond hydrolysis in dipeptides, displaying a non-redundant activity toward threonyl dipeptides. Mediates threonyl dipeptide catabolism in a tissue-specific way (By similarity). Has high dipeptidase activity toward cysteinylglycine, an intermediate metabolite in glutathione metabolism. Metabolizes N-lactoyl-amino acids, both through hydrolysis to form lactic acid and amino acids, as well as through their formation by reverse proteolysis. Plays a role in the regulation of cell cycle arrest and apoptosis (By similarity). {ECO:0000250|UniProtKB:Q96KP4, ECO:0000250|UniProtKB:Q9D1A2}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Binding site (6); Chain (1); Initiator methionine (1); Metal binding (6); Modified residue (4); Region (1); Sequence conflict (3); Site (1)
Keywords Acetylation;Carboxypeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96KP4}.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:Q96KP4; MOD_RES 9; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q96KP4; MOD_RES 58; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q6Q0N1; MOD_RES 299; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q96KP4
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 52,877
Kinetics
Metal Binding METAL 99; /note=Manganese 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q96KP4; METAL 132; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q96KP4; METAL 132; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:Q96KP4; METAL 167; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:Q96KP4; METAL 195; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:Q96KP4; METAL 445; /note=Manganese 1; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q96KP4
Rhea ID RHEA:67360; RHEA:67361; RHEA:67364; RHEA:67365; RHEA:67372; RHEA:67373; RHEA:28783; RHEA:28784; RHEA:66724; RHEA:66725; RHEA:66726
Cross Reference Brenda