| IED ID | IndEnz0002002278 |
| Enzyme Type ID | protease002278 |
| Protein Name |
Methionine aminopeptidase 2 MAP 2 MetAP 2 EC 3.4.11.18 Peptidase M |
| Gene Name | map mapB Rv2861c MTV003.07c |
| Organism | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Enzyme Sequence | MPSRTALSPGVLSPTRPVPNWIARPEYVGKPAAQEGSEPWVQTPEVIEKMRVAGRIAAGALAEAGKAVAPGVTTDELDRIAHEYLVDNGAYPSTLGYKGFPKSCCTSLNEVICHGIPDSTVITDGDIVNIDVTAYIGGVHGDTNATFPAGDVADEHRLLVDRTREATMRAINTVKPGRALSVIGRVIESYANRFGYNVVRDFTGHGIGTTFHNGLVVLHYDQPAVETIMQPGMTFTIEPMINLGALDYEIWDDGWTVVTKDRKWTAQFEHTLLVTDTGVEILTCL |
| Enzyme Length | 285 |
| Uniprot Accession Number | P9WK19 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by bengamide derivatives and by various metalloform-selective inhibitors. {ECO:0000269|PubMed:20038112, ECO:0000269|PubMed:21465667}. |
| Binding Site | BINDING 114; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:15882055, ECO:0000269|PubMed:20038112, ECO:0000269|PubMed:21465667"; BINDING 212; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:15882055, ECO:0000269|PubMed:20038112, ECO:0000269|PubMed:21465667" |
| 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_01974}; |
| 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. {ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:19688379, ECO:0000269|PubMed:20038112}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. It lost all its activities at 55 degrees Celsius. {ECO:0000269|PubMed:19688379, ECO:0000269|PubMed:20038112}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (16); Binding site (2); Chain (1); Helix (5); Metal binding (7); Turn (3) |
| 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 (15) |
| Cross Reference PDB | 1Y1N; 1YJ3; 3IU7; 3IU8; 3IU9; 3PKA; 3PKB; 3PKC; 3PKD; 3PKE; 3ROR; 4IDY; 4IEC; 4IF7; 4OOK; |
| Mapped Pubmed ID | 12475202; 24841365; |
| Motif | |
| Gene Encoded By | |
| Mass | 30,891 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=58 uM for Met-Gly-Met-Met (at pH 7.5 and at 37 degrees Celsius) {ECO:0000269|PubMed:19688379, ECO:0000269|PubMed:20038112}; KM=394 uM for Met-Ala-Ser (at pH 7.5 and at 37 degrees Celsius) {ECO:0000269|PubMed:19688379, ECO:0000269|PubMed:20038112}; |
| Metal Binding | METAL 131; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:15882055, ECO:0000269|PubMed:20038112, ECO:0000269|PubMed:21465667"; METAL 142; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:15882055, ECO:0000269|PubMed:20038112, ECO:0000269|PubMed:21465667"; METAL 142; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:15882055, ECO:0000269|PubMed:20038112, ECO:0000269|PubMed:21465667"; METAL 205; /note="Divalent metal cation 2; catalytic; via tele nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:15882055, ECO:0000269|PubMed:20038112, ECO:0000269|PubMed:21465667"; METAL 238; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:15882055, ECO:0000269|PubMed:20038112, ECO:0000269|PubMed:21465667"; METAL 269; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:15882055, ECO:0000269|PubMed:20038112, ECO:0000269|PubMed:21465667"; METAL 269; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:15882055, ECO:0000269|PubMed:20038112, ECO:0000269|PubMed:21465667" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.18; |