Detail Information for IndEnz0002016725
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