IED ID | IndEnz0002013970 |
Enzyme Type ID | protease013970 |
Protein Name |
Acylamino-acid-releasing enzyme AARE EC 3.4.19.1 Oxidized protein hydrolase OPH |
Gene Name | AARE At4g14570 dl3325w |
Organism | Arabidopsis thaliana (Mouse-ear cress) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
Enzyme Sequence | MDSSGTDSAKELHVGLDPTTEEEYATQSKLLQEFINIPSIDKAWIFNSDSGSQAMFALSQANLLANKKKKFMLSGHISNESNQSVNFHWAPFPIEMTGASAFVPSPSGLKLLVIRNPENESPTKFEIWNSSQLEKEFHIPQKVHGSVYVDGWFEGISWDSDETHVAYVAEEPSRPKPTFDHLGYYKKENSLDKGIGSWKGEGDWEEEWGEAYAGKRQPALFVINVDSGEVEPIKGIPRSISVGQVVWSPNSNGSAQYLVFAGWLGDKRKFGIKYCYNRPCAIYAIKFTSDEPKDDDANEFPIHNLTKSISSGFCPRFSKDGKFLVFVSAKTAVDSGAHWATESLHRIDWPSDGKLPESTNIVDVIQVVNCPKDGCFPGLYVTGLLSDPWLSDGHSLMLSTYWRSCRVILSVNLLSGEVSRASPSDSDYSWNALALDGDSIVAVSSSPVSVPEIKYGKKGLDSAGKPSWLWSNIQSPIRYSEKVMAGLSSLQFKILKVPISDVSEGLAEGAKNPIEAIYVSSSKSKENGKCDPLIAVLHGGPHSVSPCSFSRTMAYLSSIGYSQLIINYRGSLGYGEDALQSLPGKVGSQDVKDCLLAVDHAIEMGIADPSRITVLGGSHGGFLTTHLIGQAPDKFVAAAARNPVCNMASMVGITDIPDWCFFEAYGDQSHYTEAPSAEDLSRFHQMSPISHISKVKTPTLFLLGTKDLRVPISNGFQYVRALKEKGVEVKVLVFPNDNHPLDRPQTDYESFLNIAVWFNKYCKL |
Enzyme Length | 764 |
Uniprot Accession Number | Q84LM4 |
Absorption | |
Active Site | ACT_SITE 618; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:12966075"; ACT_SITE 707; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:12966075"; ACT_SITE 739; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:12966075" |
Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by the serine protease inhibitor diisopropyl fluorophosphate. {ECO:0000269|PubMed:12966075}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.; EC=3.4.19.1; Evidence={ECO:0000269|PubMed:12966075}; |
DNA Binding | |
EC Number | 3.4.19.1 |
Enzyme Function | FUNCTION: Catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. Can degrade the glycated RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) protein but not the native protein. May be involved in the elimination of glycated proteins (PubMed:12966075). Plays a homeostatic role in sustaining the cytoplasmic antioxidative system. May contribute to the elimination of the oxidized proteins in the cytoplasm (PubMed:22398639). {ECO:0000269|PubMed:12966075, ECO:0000269|PubMed:22398639}. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:12966075}; |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Erroneous gene model prediction (2); Mutagenesis (3) |
Keywords | Cytoplasm;Hydrolase;Nucleus;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22398639}. Nucleus {ECO:0000269|PubMed:22398639}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 15215502; 16895613; 18315867; 18431481; 21166475; 27247031; 28627464; |
Motif | |
Gene Encoded By | |
Mass | 83,938 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for Ac-Ala-pNA {ECO:0000269|PubMed:12966075}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.19.1; |