| IED ID | IndEnz0002016725 |
| Enzyme Type ID | protease016725 |
| Protein Name |
Leucine aminopeptidase 1 EC 3.4.11.1 Leucyl aminopeptidase 1 AtLAP1 Proline aminopeptidase 1 EC 3.4.11.5 Prolyl aminopeptidase 1 |
| Gene Name | LAP1 PM25 At2g24200 F27D4.11 |
| 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 | MAHTLGLTQPNSTEPHKISFTAKEIDVIEWKGDILVVGVTEKDLAKDGNSKFENPILSKVDAHLSGLLAQVSSEEDFTGKPGQSTVLRLPGLGSKRIALIGLGQSVSSPVAFHSLGEAVATVSKASQSTSAAIVLASSVSDESKLSSVSALASGIVLGLFEDGRYKSESKKPSLKAVDIIGFGTGAEVEKKLKYAEDVSYGVIFGRELINSPANVLTPAVLAEEAAKVASTYSDVFTANILNEEQCKELKMGSYLAVAAASANPPHFIHLVYKPPNGSVKTKLALVGKGLTFDSGGYNIKTGPGCSIELMKFDMGGSAAVLGAAKAIGEIKPPGVEVHFIVAACENMISGTGMRPGDVITASNGKTIEVNNTDAEGRLTLADALVYACNQGVDKIVDLATLTGACVIALGTSMAGIYTPSDELAKEVIAASERSGEKLWRMPLEESYWEMMKSGVADMVNTGGRAGGSITAALFLKQFVSEKVQWMHIDMAGPVWNEKKKSGTGFGVATLVEWVQKNSSS |
| Enzyme Length | 520 |
| Uniprot Accession Number | P30184 |
| Absorption | |
| Active Site | ACT_SITE 300; /evidence=ECO:0000255; ACT_SITE 377; /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; Evidence={ECO:0000269|PubMed:1555602}; 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 (Probable). Possesses leucine aminopeptidase activity against the model substrate leucine-amido methyl coumarin (PubMed:22493451). Possesses Cys-Gly dipeptidase activity. In addition, can cleave Cys-Leu and Leu-Cys dipeptides (PubMed:25716890). {ECO:0000269|PubMed:22493451, ECO:0000269|PubMed:25716890, ECO:0000305|PubMed:1555602}.; FUNCTION: Functions as molecular chaperone to protect proteins from heat-induced damage. {ECO:0000269|PubMed:22493451}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 for leucine aminopeptidase activity. {ECO:0000269|PubMed:1555602}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (7) |
| Keywords | Alternative splicing;Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12185496; 14558660; 14576160; 15010611; 15047896; 15215502; 15449379; 15908592; 16055689; 16502469; 16679420; 16698900; 17028149; 17828791; 18650403; 28627464; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,509 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 mM for L-leucine-p-nitroanilide {ECO:0000269|PubMed:1555602}; KM=1.3 mM for Cys-Gly dipeptide {ECO:0000269|PubMed:25716890}; KM=1.1 mM for Cys-Leu dipeptide {ECO:0000269|PubMed:25716890}; KM=2.4 mM for Leu-Cys dipeptide {ECO:0000269|PubMed:25716890}; |
| Metal Binding | METAL 288; /note=Manganese 1; /evidence=ECO:0000305|PubMed:1555602; METAL 293; /note=Manganese 1; /evidence=ECO:0000305|PubMed:1555602; METAL 293; /note=Manganese 2; /evidence=ECO:0000305|PubMed:1555602; METAL 313; /note=Manganese 1; /evidence=ECO:0000305|PubMed:1555602; METAL 373; /note=Manganese 2; /evidence=ECO:0000305|PubMed:1555602; METAL 375; /note=Manganese 1; /evidence=ECO:0000305|PubMed:1555602; METAL 375; /note=Manganese 2; /evidence=ECO:0000305|PubMed:1555602 |
| Rhea ID | |
| Cross Reference Brenda |