| IED ID | IndEnz0002005107 |
| Enzyme Type ID | protease005107 |
| Protein Name |
Aminopeptidase M1 EC 3.4.11.2 Alpha-aminoacylpeptide hydrolase |
| Gene Name | APM1 At4g33090 F4I10_20 |
| 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 | MDQFKGEPRLPKFAVPKRYDLRLNPDLIACTFTGTVAIDLDIVADTRFIVLNAADLSVNDASVSFTPPSSSKALAAPKVVLFEEDEILVLEFGEILPHGVGVLKLGFNGVLNDKMKGFYRSTYEHNGEKKNMAVTQFEPADARRCFPCWDEPACKATFKITLEVPTDLVALSNMPIMEEKVNGNLKIVSYQESPIMSTYLVAIVVGLFDYVEDHTSDGIKVRVYCQVGKADQGKFALHVGAKTLDLFKEYFAVPYPLPKMDMIAIPDFAAGAMENYGLVTYRETALLYDEQHSAASNKQRVATVVAHELAHQWFGNLVTMEWWTHLWLNEGFATWVSYLATDSLFPEWKIWTQFLDESTEGLRLDGLEESHPIEVEVNHAAEIDEIFDAISYRKGASVIRMLQSYLGAEVFQKSLAAYIKNHAYSNAKTEDLWAALEAGSGEPVNKLMSSWTKQKGYPVVSAKIKDGKLELEQSRFLSSGSPGEGQWIVPVTLCCGSYEKRKNFLLESKSGAYDLKELLGCSIADGSDKINGTCSWIKINVDQAGFYRVKYDDSLAAGLRNATESQSLTSIDRYGILDDSFALTMARQQSLASLLTLCSAYKKELDYTVLSNLIAISYKVVKIGADANQELMSGIKHFFIGVFQFAAGKLGWDPKQGESHLDAMLRGEVLTALAVFGHDETLKEAVRRFDAFLADRNTPLLPPDIRRAAYVAVMQRANKSDKSGYESLLRVYRETDLSQEKTRILGSLASCPDPTIVQDVLNFVLSDEVRNQDALYGLSGVSWEGREVAWKWLQEKWEYIGNTWGSGFLITRFISAVVSPFASFEKAKEVEEFFATRSKPSMARTLKQSIERVHINANWVESIKKEDNLTQLVAQLSSN |
| Enzyme Length | 879 |
| Uniprot Accession Number | Q8VZH2 |
| Absorption | |
| Active Site | ACT_SITE 308; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | BINDING 138; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.; EC=3.4.11.2; |
| DNA Binding | |
| EC Number | 3.4.11.2 |
| Enzyme Function | FUNCTION: Metallopeptidase that binds to the auxin transport inhibitor N-1-naphthylphthalamic acid (NPA). Required for embryonic and seedling development as well as cell cycle progression. Homodimerization is required to proper localization and activity. May play a negative role in the regulation of PIN auxin transport proteins. {ECO:0000269|PubMed:11891249, ECO:0000269|PubMed:19531600, ECO:0000269|PubMed:20154099, ECO:0000269|PubMed:23065197}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Erroneous gene model prediction (2); Erroneous initiation (1); Metal binding (3); Motif (1); Mutagenesis (3); Region (2); Site (1) |
| Keywords | Aminopeptidase;Cytoplasm;Direct protein sequencing;Endoplasmic reticulum;Hydrolase;Membrane;Metal-binding;Metalloprotease;Microsome;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. Cytoplasm. Note=The dileucine internalization motif may be involved in intracellular sequestration. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15546358; 16684236; 17644812; 20388517; 20405473; 27457991; 28627464; 31334862; |
| Motif | MOTIF 728..729; /note=Dileucine internalization motif; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 98,179 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=59 nmol/min/mg enzyme for Tyr-aminofluoromethylcoumarin {ECO:0000269|PubMed:11891249}; Vmax=35 nmol/min/mg enzyme for Ala-aminofluoromethylcoumarin {ECO:0000269|PubMed:11891249}; Vmax=18 nmol/min/mg enzyme for Pro-aminofluoromethylcoumarin {ECO:0000269|PubMed:11891249}; |
| Metal Binding | METAL 307; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 311; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 330; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |