Detail Information for IndEnz0002002278
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;