Detail Information for IndEnz0002002325
IED ID IndEnz0002002325
Enzyme Type ID protease002325
Protein Name Methionine aminopeptidase
MAP
MetAP
EC 3.4.11.18
Peptidase M
Fragment
Gene Name map
Organism Klebsiella oxytoca
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Klebsiella Klebsiella oxytoca
Enzyme Sequence TVKTKDRSLSAQYEHTIVVTDNGCEILTLRKDDTIPAIISHNE
Enzyme Length 43
Uniprot Accession Number P41392
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18;
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 (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Non-terminal residue (1)
Keywords Aminopeptidase;Hydrolase;Metal-binding;Protease
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 4,826
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda