IED Industry Enzyme Database

Detail Information for IndEnz0002002320
IED ID IndEnz0002002320
Enzyme Type ID protease002320
Protein Name Methionine aminopeptidase
MAP
MetAP
EC 3.4.11.18
Peptidase M
Gene Name map b0168 JW0163
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MAISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIKDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGAAIQKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTFTIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLRKDDTIPAIISHDE
Enzyme Length 264
Uniprot Accession Number P0AE18
Absorption
Active Site
Activity Regulation
Binding Site BINDING 79; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228"; BINDING 99; /note="Substrate"; /evidence="ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228"; BINDING 178; /note="Substrate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228"
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, ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:20521764, ECO:0000269|PubMed:3027045};
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:20521764, ECO:0000269|PubMed:3027045}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (18); Binding site (3); Chain (1); Helix (6); Initiator methionine (1); Metal binding (7); Mutagenesis (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 Electron microscopy (3); X-ray crystallography (39)
Cross Reference PDB 1C21; 1C22; 1C23; 1C24; 1C27; 1MAT; 1XNZ; 1YVM; 2BB7; 2EVC; 2EVM; 2EVO; 2GG0; 2GG2; 2GG3; 2GG5; 2GG7; 2GG8; 2GG9; 2GGB; 2GGC; 2GTX; 2GU4; 2GU5; 2GU6; 2GU7; 2MAT; 2P98; 2P99; 2P9A; 2Q92; 2Q93; 2Q94; 2Q95; 2Q96; 3D27; 3MAT; 4MAT; 4Z7M; 6IZ7; 6IZI; 6J0A;
Mapped Pubmed ID 10805534; 12861438; 15506752; 15690043; 15880695; 16300729; 16552144; 16606699; 17948983; 30753870; 9770455;
Motif
Gene Encoded By
Mass 29,331
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.0 mM for a Met-Gly-Met-Met peptide (for the Fe(2+)-complexed enzyme) {ECO:0000269|PubMed:10460163, ECO:0000269|PubMed:12755633, ECO:0000269|PubMed:18855426, ECO:0000269|PubMed:19019076}; KM=1.3 mM for a Met-Gly-Met-Met peptide (for the Mn(2+)-complexed enzyme) {ECO:0000269|PubMed:10460163, ECO:0000269|PubMed:12755633, ECO:0000269|PubMed:18855426, ECO:0000269|PubMed:19019076}; KM=3.2 mM for a Met-Gly-Met-Met peptide (for the Co(2+)-complexed enzyme) {ECO:0000269|PubMed:10460163, ECO:0000269|PubMed:12755633, ECO:0000269|PubMed:18855426, ECO:0000269|PubMed:19019076}; Vmax=55 umol/min/mg enzyme (for the Fe(2+)-complexed enzyme) {ECO:0000269|PubMed:10460163, ECO:0000269|PubMed:12755633, ECO:0000269|PubMed:18855426, ECO:0000269|PubMed:19019076}; Vmax=77 umol/min/mg enzyme (for the Co(2+)-complexed enzyme) {ECO:0000269|PubMed:10460163, ECO:0000269|PubMed:12755633, ECO:0000269|PubMed:18855426, ECO:0000269|PubMed:19019076};
Metal Binding METAL 97; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729"; METAL 108; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729"; METAL 108; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729"; METAL 171; /note="Divalent metal cation 2; catalytic; via tele nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729"; METAL 204; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729"; METAL 235; /note="Divalent metal cation 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729"; METAL 235; /note="Divalent metal cation 2; catalytic"; /evidence="ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729"
Rhea ID
Cross Reference Brenda 3.4.11.18;