Page last updated: 2024-08-07 16:47:50
Methionine aminopeptidase 2
A methionine aminopeptidase 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P50579]
Synonyms
MAP 2;
MetAP 2;
EC 3.4.11.18;
Initiation factor 2-associated 67 kDa glycoprotein;
p67;
p67eIF2;
Peptidase M
Research
Bioassay Publications (14)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 6 (42.86) | 29.6817 |
| 2010's | 8 (57.14) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
Compounds (15)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| ppi 2458 | Homo sapiens (human) | EC50 | 0.0001 | 1 | 1 |
Rickettsia prowazekii methionine aminopeptidase as a promising target for the development of antibacterial agents.Bioorganic & medicinal chemistry, , 02-01, Volume: 25, Issue:3, 2017
Discovery of Inhibitors of ACS medicinal chemistry letters, , Jul-01, Volume: 4, Issue:8, 2013
Subtype-selectivity of metal-dependent methionine aminopeptidase inhibitors.Bioorganic & medicinal chemistry letters, , Jul-15, Volume: 20, Issue:14, 2010
Rickettsia prowazekii methionine aminopeptidase as a promising target for the development of antibacterial agents.Bioorganic & medicinal chemistry, , 02-01, Volume: 25, Issue:3, 2017
Discovery of Inhibitors of ACS medicinal chemistry letters, , Jul-01, Volume: 4, Issue:8, 2013
Rickettsia prowazekii methionine aminopeptidase as a promising target for the development of antibacterial agents.Bioorganic & medicinal chemistry, , 02-01, Volume: 25, Issue:3, 2017
Discovery of Inhibitors of ACS medicinal chemistry letters, , Jul-01, Volume: 4, Issue:8, 2013
Discovery and Structure-Based Optimization of Next-Generation Reversible Methionine Aminopeptidase-2 (MetAP-2) Inhibitors.Journal of medicinal chemistry, , 05-23, Volume: 62, Issue:10, 2019
Discovery of Inhibitors of ACS medicinal chemistry letters, , Jul-01, Volume: 4, Issue:8, 2013
Synthesis and antitumor activity of 1,3,4-oxadiazole possessing 1,4-benzodioxan moiety as a novel class of potent methionine aminopeptidase type II inhibitors.Bioorganic & medicinal chemistry letters, , May-15, Volume: 23, Issue:10, 2013
Synthesis and antitumor activity of 1,2,4-triazoles having 1,4-benzodioxan fragment as a novel class of potent methionine aminopeptidase type II inhibitors.Bioorganic & medicinal chemistry, , Oct-15, Volume: 19, Issue:20, 2011
A selective account of effective paradigms and significant outcomes in the discovery of inspirational marine natural products.Journal of natural products, , Mar-27, Volume: 72, Issue:3, 2009
Highly potent inhibitors of methionine aminopeptidase-2 based on a 1,2,4-triazole pharmacophore.Journal of medicinal chemistry, , Aug-09, Volume: 50, Issue:16, 2007
Fumarranol, a rearranged fumagillin analogue that inhibits angiogenesis in vivo.Journal of medicinal chemistry, , Sep-21, Volume: 49, Issue:19, 2006
A selective account of effective paradigms and significant outcomes in the discovery of inspirational marine natural products.Journal of natural products, , Mar-27, Volume: 72, Issue:3, 2009
4-Aryl-1,2,3-triazole: a novel template for a reversible methionine aminopeptidase 2 inhibitor, optimized to inhibit angiogenesis in vivo.Journal of medicinal chemistry, , Sep-08, Volume: 48, Issue:18, 2005
Investigation of novel fumagillin analogues as angiogenesis inhibitors.Bioorganic & medicinal chemistry letters, , Jan-05, Volume: 14, Issue:1, 2004
Fumagalone, a reversible inhibitor of type 2 methionine aminopeptidase and angiogenesis.Journal of medicinal chemistry, , Jul-31, Volume: 46, Issue:16, 2003
Enables
This protein enables 7 target(s):
| Target | Category | Definition |
|---|
| RNA binding | molecular function | Binding to an RNA molecule or a portion thereof. [GOC:jl, GOC:mah] |
| aminopeptidase activity | molecular function | Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain. [https://www.ebi.ac.uk/merops/about/glossary.shtml#AMINOPEPTIDASE, PMID:24157837] |
| initiator methionyl aminopeptidase activity | molecular function | Catalysis of the release of N-terminal initiator methionine from peptides. [EC:3.4.11.18] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| metalloexopeptidase activity | molecular function | Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml] |
| metal ion binding | molecular function | Binding to a metal ion. [GOC:ai] |
| metalloaminopeptidase activity | molecular function | Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. [https://www.ebi.ac.uk/merops/about/glossary.shtml#AMINOPEPTIDASE] |
Located In
This protein is located in 3 target(s):
| Target | Category | Definition |
|---|
| cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
| cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
| plasma membrane | cellular component | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363] |
Active In
This protein is active in 1 target(s):
| Target | Category | Definition |
|---|
| cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
Involved In
This protein is involved in 3 target(s):
| Target | Category | Definition |
|---|
| protein processing | biological process | Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein. [GOC:curators, GOC:jl, GOC:jsg] |
| peptidyl-methionine modification | biological process | The modification of peptidyl-methionine. [GOC:go_curators] |
| N-terminal protein amino acid modification | biological process | The alteration of the N-terminal amino acid residue in a protein. [GOC:mah] |