| IED ID | IndEnz0002002554 |
| Enzyme Type ID | protease002554 |
| Protein Name |
Methionine aminopeptidase MAP MetAP EC 3.4.11.18 Peptidase M |
| Gene Name | map PF0541 |
| Organism | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Pyrococcus Pyrococcus furiosus Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
| Enzyme Sequence | MDTEKLMKAGEIAKKVREKAIKLARPGMLLLELAESIEKMIMELGGKPAFPVNLSINEIAAHYTPYKGDTTVLKEGDYLKIDVGVHIDGFIADTAVTVRVGMEEDELMEAAKEALNAAISVARAGVEIKELGKAIENEIRKRGFKPIVNLSGHKIERYKLHAGISIPNIYRPHDNYVLKEGDVFAIEPFATIGAGQVIEVPPTLIYMYVRDVPVRVAQARFLLAKIKREYGTLPFAYRWLQNDMPEGQLKLALKTLEKAGAIYGYPVLKEIRNGIVAQFEHTIIVEKDSVIVTTE |
| Enzyme Length | 295 |
| Uniprot Accession Number | P56218 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 62; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01975; BINDING 161; /note=Substrate |
| 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_01975, ECO:0000269|PubMed:9399590}; |
| DNA Binding | |
| EC Number | 3.4.11.18 |
| Enzyme Function | FUNCTION: Removes the N-terminal methionine from nascent proteins. 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). {ECO:0000255|HAMAP-Rule:MF_01975, ECO:0000269|PubMed:9399590}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is about 90 degrees Celsius. {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (17); Binding site (2); Chain (1); Helix (7); Metal binding (7); Mutagenesis (2); Turn (3) |
| Keywords | 3D-structure;Aminopeptidase;Direct protein sequencing;Hydrolase;Metal-binding;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (8) |
| Cross Reference PDB | 1WKM; 1XGM; 1XGN; 1XGO; 1XGS; 2DFI; 6LVH; 6M00; |
| Mapped Pubmed ID | 17510955; |
| Motif | |
| Gene Encoded By | |
| Mass | 32,842 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.2 mM for a Met-Ala-Ser peptide (for the Fe(2+)-complexed enzyme) {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; KM=11.8 mM for a Met-Ala-Ser peptide (for the Co(2+)-complexed enzyme) {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; KM=5.0 mM for a Met-Gly-Met-Met peptide (for the Fe(2+)-complexed enzyme) {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; KM=5.1 mM for a Met-Gly-Met-Met peptide (for the Co(2+)-complexed enzyme) {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; KM=1.3 mM for a Met-Ser-Ser-His-Arg-Trp-Asp-Trp peptide (for the Fe(2+)-complexed enzyme) {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; KM=2.0 mM for a Met-Ser-Ser-His-Arg-Trp-Asp-Trp peptide (for the Co(2+)-complexed enzyme) {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; |
| Metal Binding | METAL 82; /note=Divalent metal cation 1; METAL 93; /note=Divalent metal cation 1; METAL 93; /note=Divalent metal cation 2; catalytic; METAL 153; /note=Divalent metal cation 2; catalytic; via tele nitrogen; METAL 187; /note=Divalent metal cation 2; catalytic; METAL 280; /note=Divalent metal cation 1; METAL 280; /note=Divalent metal cation 2; catalytic |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.18; |