IED ID | IndEnz0002016731 |
Enzyme Type ID | protease016731 |
Protein Name |
Leucine aminopeptidase 2, chloroplastic EC 3.4.11.1 Leucyl aminopeptidase 2 AtLAP2 Proline aminopeptidase 2 EC 3.4.11.5 Prolyl aminopeptidase 2 |
Gene Name | LAP2 At4g30920 F6I18.170 |
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 | MAVTLVTSFASSSSRFHFRSFSSSPSSLSSCFVRFQFPSRLRLAFAVTPLYSSSRAMAHTISHATLGLTQANSVDHPKISFSGKEIDVTEWKGDILAVGVTEKDMAKDVNSKFENPILKKLDAHLGGLLADVSSEEDFSGKPGQSTVLRLPGLGSKRVGLIGLGKSASTPSAFQSLGEAVAAAAKASQASSVAVVLASSESVSNESKLCSASAIASGTVLGLFEDSRYKSESKKPSLKSVDIIGFGSGPELEKKLKYAEHVSYGVIFGKELVNSPANVLTPAVLAEEALNLASMYSDVMTANILNEEQCKELKMGSYLAVAAASANPPHFIHLIYKPSSGPVKTKLALVGKGLTFDSGGYNIKTGPGCLIELMKFDMGGSAAVLGAAKAIGQIKPPGVEVHFIVAACENMISGTGMRPGDVLTASNGKTIEVNNTDAEGRLTLADALVYACNQGVDKVVDLATLTGACIIALGTSMAGIYTPSDKLAKEVIAASERSGEKLWRMPMEESYWEMMKSGVADMVNTGGRAGGSITAALFLKQFVSEDVEWMHIDMAGPVWNEKKKAATGFGVATLVEWVQNHSSS |
Enzyme Length | 583 |
Uniprot Accession Number | Q944P7 |
Absorption | |
Active Site | ACT_SITE 363; /evidence=ECO:0000255; ACT_SITE 440; /evidence=ECO:0000255 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1; CATALYTIC ACTIVITY: Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; |
DNA Binding | |
EC Number | 3.4.11.1; 3.4.11.5 |
Enzyme Function | FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity). Possesses leucine aminopeptidase activity against the model substrate leucine-amido methyl coumarin (PubMed:22493451). Does not seem to possess Cys-Gly dipeptidase activity (PubMed:25716890). {ECO:0000250|UniProtKB:P30184, ECO:0000269|PubMed:22493451, ECO:0000269|PubMed:25716890}.; FUNCTION: Functions as molecular chaperone to protect proteins from heat-induced damage. {ECO:0000269|PubMed:22493451}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Erroneous gene model prediction (2); Metal binding (7); Sequence conflict (4); Transit peptide (1) |
Keywords | Aminopeptidase;Chloroplast;Hydrolase;Manganese;Metal-binding;Plastid;Protease;Reference proteome;Transit peptide |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12185496; 14576160; 15215502; 16055689; 18431481; 21569035; 21918372; 27820795; 28627464; |
Motif | |
Gene Encoded By | |
Mass | 61,307 |
Kinetics | |
Metal Binding | METAL 351; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:P30184; METAL 356; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:P30184; METAL 356; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:P30184; METAL 376; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:P30184; METAL 436; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:P30184; METAL 438; /note=Manganese 1; /evidence=ECO:0000250|UniProtKB:P30184; METAL 438; /note=Manganese 2; /evidence=ECO:0000250|UniProtKB:P30184 |
Rhea ID | |
Cross Reference Brenda |