| IED ID | IndEnz0002002298 |
| Enzyme Type ID | protease002298 |
| Protein Name |
Methionine aminopeptidase 1b EC 3.4.11.18 PfMetAP1b |
| Gene Name | METAP1b PF3D7_1015300 |
| Organism | Plasmodium falciparum (isolate 3D7) |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate 3D7) |
| Enzyme Sequence | MANIDDIEKQIENIKINSDDNKNNVSKNKNILLNGVNLKDHEIKDNVKSVDYNNNNNENDTMNEINKHVKNDEYCNKENSNNNNNNNNNNNNNLDTQINETLNLNEKFEKKNEENLCSGCKKVLIKKLSCPICLKNKIFSYFCNQECFKGSWKEHQKIHENMNKENNEKEDHLKTIVKKHLSPENFDPTNRKYWVYDDHLKNFVNFKFTGDVRPWPLSKINHVPSHIERPDYAISSIPESELIYKRKSDIYVNNEEEIQRIREACILGRKTLDYAHTLVSPGVTTDEIDRKVHEFIIKNNAYPSTLNYYKFPKSCCTSVNEIVCHGIPDYRPLKSGDIINIDISVFYKGVHSDLNETYFVGDINDVPKEGKELVETCYFSLMEAIKKCKPGMFYKNIGTLIDAYVSKKNFSVVRSYSGHGVGKLFHSNPTVPHFKKNKAVGIMKPGHVFTIEPMINQGHYSDVLWPDQWTSATSDGKLSAQFEHTLLITNNGVEILTKRTQDSPPLGFDTKDELYYN |
| Enzyme Length | 517 |
| Uniprot Accession Number | Q8IJP2 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by pyrimidine derivative XC11. {ECO:0000269|PubMed:16983082}. |
| Binding Site | BINDING 325; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174; BINDING 426; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03174 |
| 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:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16983082, ECO:0000269|PubMed:27023914}; |
| DNA Binding | |
| EC Number | 3.4.11.18 |
| Enzyme Function | FUNCTION: Cotranslationally removes the N-terminal methionine from nascent proteins (PubMed:16983082, PubMed:27023914). The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val) (By similarity). May play an important role in parasite growth during the blood asexual stage (PubMed:16983082). {ECO:0000255|RuleBase:RU003653, ECO:0000269|PubMed:16983082, ECO:0000269|PubMed:27023914}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius (PubMed:27023914). However, has substantial activity at 25 degrees Celsius (PubMed:27023914). {ECO:0000269|PubMed:27023914}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:27023914}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (15); Binding site (2); Chain (1); Compositional bias (1); Helix (11); Metal binding (7); Mutagenesis (1); Region (1); Site (1); Turn (4) |
| Keywords | 3D-structure;Aminopeptidase;Hydrolase;Metal-binding;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3S6B; |
| Mapped Pubmed ID | 16267556; |
| Motif | |
| Gene Encoded By | |
| Mass | 59,724 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=327.3 uM for methionine containing-oligopeptide {ECO:0000269|PubMed:16983082}; KM=845.08 uM for Met-Gly-Met-Met peptide (in presence of 1 uM Zn(2+), at 37 degrees Celsius, pH 7.5) {ECO:0000269|PubMed:27023914}; KM=1117.7 uM for Met-Gly-Met-Met peptide (in presence of 10 uM Zn(2+), at 37 degrees Celsius, pH 7.5) {ECO:0000269|PubMed:27023914}; KM=1662.4 uM for Met-Gly-Met-Met peptide (in presence of 100 uM Zn(2+), at 37 degrees Celsius, pH 7.5) {ECO:0000269|PubMed:27023914}; KM=1759 uM for Met-Gly-Met-Met peptide (in presence of 1 uM Co(2+), at 37 degrees Celsius, pH 7.5) {ECO:0000269|PubMed:27023914}; KM=1142.4 uM for Met-Gly-Met-Met peptide (in presence of 10 uM Co(2+), at 37 degrees Celsius, pH 7.5) {ECO:0000269|PubMed:27023914}; KM=1061.5 uM for Met-Gly-Met-Met peptide (in presence of 100 uM Co(2+), at 37 degrees Celsius, pH 7.5) {ECO:0000269|PubMed:27023914}; Note=kcat is 13.9 min(-1) with methionine containing-oligopeptide as substrate (PubMed:16983082). kcat is 552.49 min(-1) in presence of 1 uM Zn(2+), 442.48 min(-1) in presence of 10 uM Zn(2+) and 364.30 min(-1) in presence of 100 uM Zn(2+), with Met-Gly-Met-Met peptide as substrate (PubMed:27023914). kcat is 1005 min(-1) in presence of 1 uM Co(2+), 583.09 min(-1) in presence of 10 uM Co(2+) and 547.95 min(-1) in presence of 100 uM Co(2+), with Met-Gly-Met-Met peptide as substrate (PubMed:27023914). {ECO:0000269|PubMed:16983082, ECO:0000269|PubMed:27023914}; |
| Metal Binding | METAL 342; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; METAL 353; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; METAL 353; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174, ECO:0007744|PDB:3S6B"; METAL 419; /note="Divalent metal cation 2; catalytic; via tele nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174, ECO:0007744|PDB:3S6B"; METAL 452; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174, ECO:0007744|PDB:3S6B"; METAL 483; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174"; METAL 483; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_03174, ECO:0007744|PDB:3S6B" |
| Rhea ID | |
| Cross Reference Brenda |