IED ID | IndEnz0002016727 |
Enzyme Type ID | protease016727 |
Protein Name |
Leucine aminopeptidase 1, chloroplastic EC 3.4.11.1 DR57 Leucyl aminopeptidase 1 LAP 1 Proline aminopeptidase 1 EC 3.4.11.5 Prolyl aminopeptidase 1 |
Gene Name | LAPA1 LAP LAP2 Solyc12g010020 |
Organism | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Solanales Solanaceae Solanoideae Solaneae Solanum Solanum subgen. Lycopersicon Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
Enzyme Sequence | MATLRVSSLFASSSSSLHSNPSVFTKYQSSPKWAFSFPVTPLCSKRSKRIVHCIAGDTLGLTRPNESDAPKISIGAKDTAVVQWQGDLLAIGATENDMARDENSKFKNPLLQQLDSELNGLLSAASSEEDFSGKSGQSVNLRFPGGRITLVGLGSSASSPTSYHSLGQAAAAAAKSSQARNIAVALASTDGLSAESKINSASAIATGVVLGSFEDNRFRSESKKSTLESLDILGLGTGPEIERKIKYAEHVCAGVILGRELVNAPANIVTPAVLAEEAKKIASTYSDVISVNILDAEQCKELKMGAYLAVAAAATENPPYFIHLCFKTPTKERKTKLALVGKGLTFDSGGYNLKVGAGSRIELMKNDMGGAAAVLGAAKALGEIRPSRVEVHFIVAACENMISAEGMRPGDIVTASNGKTIEVNNTDAEGRLTLADALIYACNQGVEKIIDLATLTGAIMVALGPSVAGAFTPNDDLAREVVEAAEASGEKLWRMPMEESYWESMKSGSGDMINTGPGNGGAITGALFLKQFVDEKVQWLHLDVAGPVWSDEKKNATGYGVSTLVEWVLRN |
Enzyme Length | 571 |
Uniprot Accession Number | Q10712 |
Absorption | |
Active Site | ACT_SITE 354; /evidence=ECO:0000255; ACT_SITE 431; /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. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (17); Chain (1); Helix (19); Metal binding (7); Sequence conflict (7); Transit peptide (1); Turn (5) |
Keywords | 3D-structure;Aminopeptidase;Chloroplast;Hydrolase;Magnesium;Metal-binding;Plastid;Protease;Reference proteome;Transit peptide |
Interact With | |
Induction | INDUCTION: Induced by wounding (PubMed:8234334, PubMed:15231736). Induced by methyl jasmonate (PubMed:15231736). {ECO:0000269|PubMed:15231736, ECO:0000269|PubMed:8234334}. |
Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (2) |
Cross Reference PDB | 4KSI; 5D8N; |
Mapped Pubmed ID | 27139632; |
Motif | |
Gene Encoded By | |
Mass | 60,154 |
Kinetics | |
Metal Binding | METAL 342; /note="Magnesium 1"; /evidence="ECO:0000269|PubMed:24914976, ECO:0007744|PDB:4KSI"; METAL 347; /note="Magnesium 1"; /evidence="ECO:0000269|PubMed:24914976, ECO:0007744|PDB:4KSI"; METAL 347; /note="Magnesium 2"; /evidence="ECO:0000269|PubMed:24914976, ECO:0007744|PDB:4KSI"; METAL 367; /note="Magnesium 1"; /evidence="ECO:0000269|PubMed:24914976, ECO:0007744|PDB:4KSI"; METAL 427; /note="Magnesium 2"; /evidence="ECO:0000269|PubMed:24914976, ECO:0007744|PDB:4KSI"; METAL 429; /note="Magnesium 1"; /evidence="ECO:0000269|PubMed:24914976, ECO:0007744|PDB:4KSI"; METAL 429; /note="Magnesium 2"; /evidence="ECO:0000269|PubMed:24914976, ECO:0007744|PDB:4KSI" |
Rhea ID | |
Cross Reference Brenda | 3.4.11.1; |