| IED ID | IndEnz0002007705 |
| Enzyme Type ID | protease007705 |
| Protein Name |
Puromycin-sensitive aminopeptidase PSA EC 3.4.11.14 Cytosol alanyl aminopeptidase AAP-S |
| Gene Name | NPEPPS PSA |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MWLAAAAPSLARRLLFLGPPPPPLLLLVFSRSSRRRLHSLGLAAMPEKRPFERLPADVSPINYSLCLKPDLLDFTFEGKLEAAAQVRQATNQIVMNCADIDIITASYAPEGDEEIHATGFNYQNEDEKVTLSFPSTLQTGTGTLKIDFVGELNDKMKGFYRSKYTTPSGEVRYAAVTQFEATDARRAFPCWDEPAIKATFDISLVVPKDRVALSNMNVIDRKPYPDDENLVEVKFARTPVMSTYLVAFVVGEYDFVETRSKDGVCVRVYTPVGKAEQGKFALEVAAKTLPFYKDYFNVPYPLPKIDLIAIADFAAGAMENWGLVTYRETALLIDPKNSCSSSRQWVALVVGHELAHQWFGNLVTMEWWTHLWLNEGFASWIEYLCVDHCFPEYDIWTQFVSADYTRAQELDALDNSHPIEVSVGHPSEVDEIFDAISYSKGASVIRMLHDYIGDKDFKKGMNMYLTKFQQKNAATEDLWESLENASGKPIAAVMNTWTKQMGFPLIYVEAEQVEDDRLLRLSQKKFCAGGSYVGEDCPQWMVPITISTSEDPNQAKLKILMDKPEMNVVLKNVKPDQWVKLNLGTVGFYRTQYSSAMLESLLPGIRDLSLPPVDRLGLQNDLFSLARAGIISTVEVLKVMEAFVNEPNYTVWSDLSCNLGILSTLLSHTDFYEEIQEFVKDVFSPIGERLGWDPKPGEGHLDALLRGLVLGKLGKAGHKATLEEARRRFKDHVEGKQILSADLRSPVYLTVLKHGDGTTLDIMLKLHKQADMQEEKNRIERVLGATLLPDLIQKVLTFALSEEVRPQDTVSVIGGVAGGSKHGRKAAWKFIKDNWEELYNRYQGGFLISRLIKLSVEGFAVDKMAGEVKAFFESHPAPSAERTIQQCCENILLNAAWLKRDAESIHQYLLQRKASPPTV |
| Enzyme Length | 919 |
| Uniprot Accession Number | P55786 |
| Absorption | |
| Active Site | ACT_SITE 353; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by bestatin, leuhistin, actinonin, amastatin, 1,10-phenanthroline, DFP, PCMBS, Zn(2+), Cd(2+), Co(2+), Cu(2+), Hg(2+), EDTA and puromycin. Not inhibited by PMSF, and only slightly inhibited by leupeptin and aprotinin. Activity is increased by Mg(2+) and Ca(2+). {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:17154549, ECO:0000269|PubMed:17318184}. |
| Binding Site | BINDING 180; /note=Substrate; /evidence=ECO:0000250 |
| 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; |
| DNA Binding | |
| EC Number | 3.4.11.14 |
| Enzyme Function | FUNCTION: Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. May act as regulator of neuropeptide activity. Plays a role in the antigen-processing pathway for MHC class I molecules. Involved in the N-terminal trimming of cytotoxic T-cell epitope precursors. Digests the poly-Q peptides found in many cellular proteins. Digests tau from normal brain more efficiently than tau from Alzheimer disease brain. {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:11062501, ECO:0000269|PubMed:17154549, ECO:0000269|PubMed:17318184, ECO:0000269|PubMed:19917696}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Stable up to 40 degrees Celsius. {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:17154549}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. Stable from pH 5.0 to 8.0. {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:17154549}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (2); Binding site (1); Chain (1); Erroneous initiation (2); Metal binding (3); Modified residue (1); Motif (1); Mutagenesis (4); Region (1); Sequence conflict (1); Site (1) |
| Keywords | Alternative splicing;Aminopeptidase;Cytoplasm;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Nitration;Nucleus;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10978616}. Nucleus {ECO:0000305}. |
| Modified Residue | MOD_RES 464; /note=3'-nitrotyrosine; /evidence=ECO:0000250|UniProtKB:Q11011 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 14706550; 15224091; 15224092; 16849449; 17353931; 19494703; 19615732; 19805454; 20377816; 20562859; 20711500; 20829225; 21320871; 23455922; 25142031; 25342037; 25609649; 26078706; 31523044; 9668046; |
| Motif | MOTIF 726..730; /note=Nuclear localization signal; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 103,276 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.20 mM for Lys-p-NA {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:17154549}; KM=0.25 mM for Leu-p-NA {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:17154549}; KM=0.27 mM for Ala-p-NA {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:17154549}; KM=0.80 mM for Met-p-NA {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:17154549}; KM=0.47 mM for Pro-p-NA {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:17154549}; KM=0.21 mM for Val-p-NA {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:17154549}; KM=182 uM for Ala-MCA {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:17154549}; KM=189 uM for Met-MCA {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:17154549}; KM=220 uM for Lys-MCA {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:17154549}; KM=91 uM for Leu-MCA {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:17154549}; KM=167 uM for Phe-MCA {ECO:0000269|PubMed:10978616, ECO:0000269|PubMed:17154549}; |
| Metal Binding | METAL 352; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 356; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 375; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |