Detail Information for IndEnz0002002270
IED ID IndEnz0002002270
Enzyme Type ID protease002270
Protein Name Methionine aminopeptidase 1
MAP 1
MetAP 1
EC 3.4.11.18
Peptidase M
Gene Name map-1 mapA Rv0734
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 MRPLARLRGRRVVPQRSAGELDAMAAAGAVVAAALRAIRAAAAPGTSSLSLDEIAESVIRESGATPSFLGYHGYPASICASINDRVVHGIPSTAEVLAPGDLVSIDCGAVLDGWHGDAAITFGVGALSDADEALSEATRESLQAGIAAMVVGNRLTDVAHAIETGTRAAELRYGRSFGIVAGYGGHGIGRQMHMDPFLPNEGAPGRGPLLAAGSVLAIEPMLTLGTTKTVVLDDKWTVTTADGSRAAHWEHTVAVTDDGPRILTLG
Enzyme Length 266
Uniprot Accession Number P9WK21
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by various metalloform-selective inhibitors. {ECO:0000269|PubMed:20363127}.
Binding Site BINDING 88; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; BINDING 193; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01974
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}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. It retained half of its activity after 10 min of incubation at 55 degrees Celsius. {ECO:0000269|PubMed:19688379, ECO:0000269|PubMed:20363127};
PH Dependency
Pathway
nucleotide Binding
Features Binding site (2); Chain (1); Metal binding (7)
Keywords Aminopeptidase;Hydrolase;Metal-binding;Protease;Reference proteome
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 27,277
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 uM for Met-Ala-Ser (at pH 7.5 and at 37 degrees Celsius) {ECO:0000269|PubMed:19688379, ECO:0000269|PubMed:20363127}; KM=328 uM for Met-Gly-Met-Met (at pH 7.5 and at 37 degrees Celsius) {ECO:0000269|PubMed:19688379, ECO:0000269|PubMed:20363127};
Metal Binding METAL 106; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 117; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 117; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 186; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 219; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 250; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_01974; METAL 250; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01974
Rhea ID
Cross Reference Brenda 3.4.11.18;