| IED ID | IndEnz0002012986 |
| Enzyme Type ID | protease012986 |
| Protein Name |
Puromycin-sensitive aminopeptidase PSA EC 3.4.11.14 Cytosol alanyl aminopeptidase AAP-S |
| Gene Name | pam-1 F49E8.3 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MLGRLAVRQAVRCSKASIKPVNTHQLCLRNFSAIRRLSFVAGAQCRPYHTTANMLHRTARGEHGMAACGNPSAAVKFERLPTFAEPTHYNVRLSPCLNQFSFDGHATIDVTIKEATDVLKVHAQSLLIQSVSLITQPGDASKSLETSYDDKLNILTIKLPTTMQPQKVQLDFKFVGELNDKMRGFYRSQYKDKNGTEKFLASTQFESTYARYAFPCFDEPIYKATFDVTLEVENHLTALSNMNVISETPTADGKRKAVTFATSPKMSSYLVAFAVGELEYISAQTKSGVEMRVYTVPGKKEQGQYSLDLSVKCIDWYNEWFDIKYPLPKCDLIAIPDFSMGAMENWGLVTYREIALLVDPGVTSTRQKSRVALVVAHELAHLWFGNLVTMKWWTDLWLKEGFASFMEYMFVGANCPEFKIWLHFLNDELASGMGLDALRNSHPIEVEIDNPNELDEIYDSITYAKSNSVNRMLCYYLSEPVFQKGLRLYLKRFQYSNAVTQDLWTALSEASGQNVNELMSGWTQQMGFPVLKVSQRQDGNNRILTVEQRRFISDGGEDPKNSQWQVPITVAVGSSPSDVKARFLLKEKQQEFTIEGVAPGEWVKLNSGTTGFYRVEYSDEMLTAMLPDIASRRMPVLDRFGLINDLSALLNTGRVSIAQFVQVAASSAKEDEYVVWGAIDEGMSKLLACAREMSEDTLKSAKQLVVKMFEQTGAELGFAEQAGEDSQKMMLRSLVQARLARAGHQPTIDKFTQMFNDFLEKGTPIHPDIRLATFGVVARYGGKEGFDKLMNLRETTTFQEIERQTMVAMSQTPEESLLAQLFEYGFEKNKVRPQDQLYLFLGTGATHMGQQYAWKYFCEHIKEFLDKYGGANSSLFQRCLKFAGESFGNEKRAVEFQDFFCNCNVLSDTDRQTLARPIGQTVEAIRLNARLLESNRQIIENLLKQSNV |
| Enzyme Length | 948 |
| Uniprot Accession Number | Q4TT88 |
| Absorption | |
| Active Site | ACT_SITE 378; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by chelating agent 1,10-phenanthroline, aminopeptidase inhibitors actinonin, amastatin, and leuhistin, and to a lesser extent by puromycin. {ECO:0000269|PubMed:12930831}. |
| Binding Site | BINDING 206; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q6P179 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially alanine, from a wide range of peptides, amides and arylamides.; EC=3.4.11.14; Evidence={ECO:0000305|PubMed:12930831}; |
| DNA Binding | |
| EC Number | 3.4.11.14 |
| Enzyme Function | FUNCTION: Aminopeptidase (PubMed:12930831). Required for the exit from meiosis, probably upstream of cyclin cyb-3 (PubMed:17021038). Involved in the establishment of the anterior-posterior polarity at the embryonic 1-cell stage by regulating the dynamics of sperm-donated centrosomes (PubMed:17021038, PubMed:20599902, PubMed:28065742). Plays a role in oocyte maturation (PubMed:24663498). Required for embryonic development (PubMed:12930831). {ECO:0000269|PubMed:12930831, ECO:0000269|PubMed:17021038, ECO:0000269|PubMed:20599902, ECO:0000269|PubMed:24663498, ECO:0000269|PubMed:28065742}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Binding site (1); Chain (1); Metal binding (3); Region (1); Site (1) |
| Keywords | Alternative splicing;Aminopeptidase;Chromosome;Cytoplasm;Cytoskeleton;Differentiation;Hydrolase;Meiosis;Metal-binding;Metalloprotease;Oogenesis;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20599902}. Cytoplasm, cell cortex {ECO:0000269|PubMed:20599902}. Chromosome {ECO:0000269|PubMed:20599902}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:20599902}. Note=During meiosis I, localizes to the cell cortex. During meiosis II, localizes to the cytoplasm. During embryonic mitosis, localizes around mitotic chromosomes at metaphase and anaphase and near the spindle poles. In spermatids, excluded from the chromosomes. {ECO:0000269|PubMed:20599902}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12529635; 16439208; 17164286; 17486083; 19343510; 19922876; 20439776; 21177967; 21367940; 22286215; 22347378; 22560298; 23209443; 23800452; 25487147; 26009280; 29167199; 29348603; 29748380; 33681968; |
| Motif | |
| Gene Encoded By | |
| Mass | 107,150 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=34 uM for L-Arg-AMC {ECO:0000269|PubMed:12930831}; KM=59 uM for L-Met-AMC {ECO:0000269|PubMed:12930831}; KM=63 uM for L-Leu-AMC {ECO:0000269|PubMed:12930831}; KM=73 uM for L-Tyr-AMC {ECO:0000269|PubMed:12930831}; KM=78 uM for L-Lys-AMC {ECO:0000269|PubMed:12930831}; KM=97 uM for L-Ala-AMC {ECO:0000269|PubMed:12930831}; KM=160 uM for L-Phe-AMC {ECO:0000269|PubMed:12930831}; KM=390 uM for L-Gly-AMC {ECO:0000269|PubMed:12930831}; KM=840 uM for L-Ser-AMC {ECO:0000269|PubMed:12930831}; |
| Metal Binding | METAL 377; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 381; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 400; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15144 |
| Rhea ID | |
| Cross Reference Brenda |