| IED ID | IndEnz0002008911 |
| Enzyme Type ID | protease008911 |
| Protein Name |
Aminopeptidase RNPEPL1 EC 3.4.11.- Arginyl aminopeptidase-like 1 Methionyl aminopeptidase EC 3.4.11.18 |
| Gene Name | RNPEPL1 |
| 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 | MAAQCCCRQAPGAEAAPVRPPPEPPPALDVASASSAQLFRLRHLQLGLELRPEARELAGCLVLELCALRPAPRALVLDAHPALRLHSAAFRRAPAAAAETPCAFAFSAPGPGPAPPPPLPAFPEAPGSEPACCPLAFRVDPFTDYGSSLTVTLPPELQAHQPFQVILRYTSTDAPAIWWLDPELTYGCAKPFVFTQGHSVCNRSFFPCFDTPAVKCTYSAVVKAPSGVQVLMSATRSAYMEEEGVFHFHMEHPVPAYLVALVAGDLKPADIGPRSRVWAEPCLLPTATSKLSGAVEQWLSAAERLYGPYMWGRYDIVFLPPSFPIVAMENPCLTFIISSILESDEFLVIDVIHEVAHSWFGNAVTNATWEEMWLSEGLATYAQRRITTETYGAAFTCLETAFRLDALHRQMKLLGEDSPVSKLQVKLEPGVNPSHLMNLFTYEKGYCFVYYLSQLCGDPQRFDDFLRAYVEKYKFTSVVAQDLLDSFLSFFPELKEQSVDCRAGLEFERWLNATGPPLAEPDLSQGSSLTRPVEALFQLWTAEPLDQAAASASAIDISKWRTFQTALFLDRLLDGSPLPQEVVMSLSKCYSSLLDSMNAEIRIRWLQIVVRNDYYPDLHRVRRFLESQMSRMYTIPLYEDLCTGALKSFALEVFYQTQGRLHPNLRRAIQQILSQGLGSSTEPASEPSTELGKAEADTDSDAQALLLGDEAPSSAISLRDVNVSA |
| Enzyme Length | 725 |
| Uniprot Accession Number | Q9HAU8 |
| Absorption | |
| Active Site | ACT_SITE 354; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P15144, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by calcium but not affected by chloride ions. Inhibited by amastatin and to a lower extent by bestatin. Weakly inhibited by puromycin. {ECO:0000269|PubMed:19508204}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; Evidence={ECO:0000269|PubMed:19508204}; |
| DNA Binding | |
| EC Number | 3.4.11.-; 3.4.11.18 |
| Enzyme Function | FUNCTION: Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine. {ECO:0000269|PubMed:19508204}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.6-8.0. {ECO:0000269|PubMed:19508204}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Erroneous gene model prediction (1); Erroneous initiation (3); Metal binding (3); Natural variant (1); Region (2); Sequence conflict (2); Site (1) |
| Keywords | Aminopeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20414141; 20549515; 20711500; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,000 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.37 mM for Met-AMC {ECO:0000269|PubMed:19508204}; KM=0.17 mM for Citrulline-AMC {ECO:0000269|PubMed:19508204}; KM=1.72 mM for Ala-AMC {ECO:0000269|PubMed:19508204}; KM=0.91 mM for Arg-AMC {ECO:0000269|PubMed:19508204}; KM=0.89 mM for Asn-AMC {ECO:0000269|PubMed:19508204}; KM=0.41 mM for Gln-AMC {ECO:0000269|PubMed:19508204}; KM=0.18 mM for His-AMC {ECO:0000269|PubMed:19508204}; KM=1.05 mM for Ile-AMC {ECO:0000269|PubMed:19508204}; KM=0.34 mM for Leu-AMC {ECO:0000269|PubMed:19508204}; KM=1.72 mM for Lys-AMC {ECO:0000269|PubMed:19508204}; KM=0.65 mM for Phe-AMC {ECO:0000269|PubMed:19508204}; KM=1.76 mM for Ser-AMC {ECO:0000269|PubMed:19508204}; KM=0.12 mM for Trp-AMC {ECO:0000269|PubMed:19508204}; KM=0.12 mM for Tyr-AMC {ECO:0000269|PubMed:19508204}; |
| Metal Binding | METAL 353; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15144; METAL 357; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15144; METAL 376; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P15144 |
| Rhea ID | |
| Cross Reference Brenda |