IED Industry Enzyme Database

Detail Information for IndEnz0002015438
IED ID IndEnz0002015438
Enzyme Type ID protease015438
Protein Name Isoaspartyl dipeptidase
EC 3.4.19.-
Gene Name iadA yjiF b4328 JW4291
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MIDYTAAGFTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPNCTVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVALSRLTEAGVTSVVGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGVKCAISDHRSAAPDVYHLANMAAESRVGGLLGGKPGVTVFHMGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQALEFARKGGTIDITSSIDEPVAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLTHIGVAGFETLLETVQVLVKDYDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMTPELRIEQVYARGKLMVKDGKACVKGTFETA
Enzyme Length 390
Uniprot Accession Number P39377
Absorption
Active Site ACT_SITE 285; /note=Proton acceptor; /evidence=ECO:0000269|PubMed:12946361
Activity Regulation ACTIVITY REGULATION: P-hydroxymercuribenzoate causes a slight inhibition (8 to 17 %). Iodoacetamide, o-iodosobenzoate and ammonium persulfate do not inhibit the enzyme activity. {ECO:0000269|PubMed:4880759}.
Binding Site BINDING 106; /note="Substrate"; /evidence="ECO:0000305|PubMed:12718528, ECO:0000305|PubMed:12946361, ECO:0000305|PubMed:15882050"; BINDING 137; /note="Substrate"; /evidence="ECO:0000305|PubMed:12718528, ECO:0000305|PubMed:12946361, ECO:0000305|PubMed:15882050"; BINDING 169; /note="Substrate"; /evidence="ECO:0000305|PubMed:12718528, ECO:0000305|PubMed:12946361, ECO:0000305|PubMed:15882050"; BINDING 233; /note="Substrate"; /evidence="ECO:0000305|PubMed:12718528, ECO:0000305|PubMed:12946361, ECO:0000305|PubMed:15882050"; BINDING 289; /note="Substrate; via amide nitrogen and carbonyl oxygen"; /evidence="ECO:0000305|PubMed:12718528, ECO:0000305|PubMed:12946361, ECO:0000305|PubMed:15882050"
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.19.-
Enzyme Function FUNCTION: Catalyzes the hydrolytic cleavage of a subset of L-isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. The best substrate for the enzyme reported thus far is iso-Asp-Leu. {ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:4880759, ECO:0000269|PubMed:7876157}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. Active over a wide pH range. {ECO:0000269|PubMed:4880759};
Pathway
nucleotide Binding
Features Active site (1); Beta strand (25); Binding site (5); Chain (1); Helix (16); Metal binding (7); Modified residue (1); Mutagenesis (7); Region (1); Turn (1)
Keywords 3D-structure;Cobalt;Cytoplasm;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7876157}.
Modified Residue MOD_RES 162; /note="N6-carboxylysine"; /evidence="ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685"
Post Translational Modification PTM: Carboxylation allows a single lysine to coordinate two zinc ions (PubMed:12718528, PubMed:12946361, PubMed:15882050, PubMed:16289685). {ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685}.
Signal Peptide
Structure 3D Electron microscopy (1); X-ray crystallography (8)
Cross Reference PDB 1ONW; 1ONX; 1PO9; 1POJ; 1POK; 1YBQ; 2AQO; 2AQV; 5LP3;
Mapped Pubmed ID 16606699; 28783726;
Motif
Gene Encoded By
Mass 41,084
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.81 mM for beta-aspartylleucine (at pH 8.0) {ECO:0000269|PubMed:4880759};
Metal Binding METAL 68; /note="Zinc 1; via tele nitrogen; catalytic"; /evidence="ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685"; METAL 70; /note="Zinc 1; via tele nitrogen; catalytic"; /evidence="ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685"; METAL 162; /note="Zinc 1; via carbamate group; catalytic"; /evidence="ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685"; METAL 162; /note="Zinc 2; via carbamate group; catalytic"; /evidence="ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685"; METAL 201; /note="Zinc 2; via pros nitrogen; catalytic"; /evidence="ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685"; METAL 230; /note="Zinc 2; via tele nitrogen; catalytic"; /evidence="ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685"; METAL 285; /note="Zinc 1; catalytic"; /evidence="ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685"
Rhea ID
Cross Reference Brenda 3.4.19.5;