Page last updated: 2024-08-07 15:50:05
Leukotriene A-4 hydrolase
A leukotriene A-4 hydrolase that is encoded in the genome of human. [PRO:DNx, UniProtKB:P09960]
Synonyms
LTA-4 hydrolase;
EC 3.3.2.6;
Leukotriene A(4) hydrolase;
Tripeptide aminopeptidase LTA4H;
3.4.11.4
Research
Bioassay Publications (18)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (5.56) | 18.2507 |
| 2000's | 9 (50.00) | 29.6817 |
| 2010's | 7 (38.89) | 24.3611 |
| 2020's | 1 (5.56) | 2.80 |
Compounds (42)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| captopril | Homo sapiens (human) | Kd | 7.0300 | 3 | 3 |
| ubenimex | Homo sapiens (human) | Kd | 3.9433 | 3 | 3 |
| sc 57461 | Homo sapiens (human) | Kd | 0.2333 | 3 | 3 |
Drugs with Other Measurements
Thermodynamic properties of leukotriene ABioorganic & medicinal chemistry, , 11-01, Volume: 24, Issue:21, 2016
Synthesis and biological evaluation of N-mercaptoacylproline and N-mercaptoacylthiazolidine-4-carboxylic acid derivatives as leukotriene A4 hydrolase inhibitors.Bioorganic & medicinal chemistry letters, , Aug-15, Volume: 18, Issue:16, 2008
Computer-Aided Fragment Growing Strategies to Design Dual Inhibitors of Soluble Epoxide Hydrolase and LTA4 Hydrolase.ACS medicinal chemistry letters, , Jun-11, Volume: 11, Issue:6, 2020
Synthesis, docking, cytotoxicity, and LTABioorganic & medicinal chemistry, , 02-01, Volume: 25, Issue:3, 2017
Thermodynamic properties of leukotriene ABioorganic & medicinal chemistry, , 11-01, Volume: 24, Issue:21, 2016
Optimization of 5-hydroxytryptamines as dual function inhibitors targeting phospholipase A2 and leukotriene A4 hydrolase.European journal of medicinal chemistry, , Volume: 59, 2013
Amino-benzosuberone: a novel warhead for selective inhibition of human aminopeptidase-N/CD13.Bioorganic & medicinal chemistry, , Feb-15, Volume: 19, Issue:4, 2011
Synthesis and biological evaluation of N-mercaptoacylproline and N-mercaptoacylthiazolidine-4-carboxylic acid derivatives as leukotriene A4 hydrolase inhibitors.Bioorganic & medicinal chemistry letters, , Aug-15, Volume: 18, Issue:16, 2008
Synthesis and structure activity relationships of novel non-peptidic metallo-aminopeptidase inhibitors.Bioorganic & medicinal chemistry, , Nov-01, Volume: 14, Issue:21, 2006
Synthesis of imidazopyridines and purines as potent inhibitors of leukotriene A4 hydrolase.Bioorganic & medicinal chemistry letters, , Mar-24, Volume: 13, Issue:6, 2003
Pyrrolidine and piperidine analogues of SC-57461A as potent, orally active inhibitors of leukotriene A(4) hydrolase.Bioorganic & medicinal chemistry letters, , Dec-02, Volume: 12, Issue:23, 2002
Structure-activity relationship studies on 1-[2-(4-Phenylphenoxy)ethyl]pyrrolidine (SC-22716), a potent inhibitor of leukotriene A(4) (LTA(4)) hydrolase.Journal of medicinal chemistry, , Feb-24, Volume: 43, Issue:4, 2000
Thermodynamic properties of leukotriene ABioorganic & medicinal chemistry, , 11-01, Volume: 24, Issue:21, 2016
Pyrrolidine and piperidine analogues of SC-57461A as potent, orally active inhibitors of leukotriene A(4) hydrolase.Bioorganic & medicinal chemistry letters, , Dec-02, Volume: 12, Issue:23, 2002
Enables
This protein enables 9 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] |
| epoxide hydrolase activity | molecular function | Catalysis of the reaction: an epoxide + H2O = an ethanediol. [EC:3.3.2.10] |
| leukotriene-A4 hydrolase activity | molecular function | Catalysis of the reaction: H2O + leukotriene A(4) = leukotriene B(4). [EC:3.3.2.6, RHEA:22324] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| peptidase activity | molecular function | Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. [GOC:jl, ISBN:0815332181] |
| zinc ion binding | molecular function | Binding to a zinc ion (Zn). [GOC:ai] |
| tripeptide aminopeptidase activity | molecular function | Catalysis of the hydrolysis of a single N-terminal amino acid residue from a tripeptide. [EC:3.4.11.4] |
| 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 6 target(s):
| Target | Category | Definition |
|---|
| extracellular region | cellular component | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators] |
| nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
| 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] |
| extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
| tertiary granule lumen | cellular component | Any membrane-enclosed lumen that is part of a tertiary granule. [GO_REF:0000064, GOC:TermGenie, PMID:23650620] |
| ficolin-1-rich granule lumen | cellular component | Any membrane-enclosed lumen that is part of a ficolin-1-rich granule. [GO_REF:0000064, GOC:TermGenie, PMID:23650620] |
Active In
This protein is active in 2 target(s):
| Target | Category | Definition |
|---|
| 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] |
| nucleus | cellular component | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators] |
Involved In
This protein is involved in 8 target(s):
| Target | Category | Definition |
|---|
| proteolysis | biological process | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah] |
| lipid metabolic process | biological process | The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids. [GOC:ma] |
| response to zinc ion | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a zinc ion stimulus. [GOC:sm] |
| leukotriene biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of leukotriene, a pharmacologically active substance derived from a polyunsaturated fatty acid, such as arachidonic acid. [GOC:go_curators] |
| protein metabolic process | biological process | The chemical reactions and pathways involving a protein. Includes protein modification. [GOC:ma] |
| peptide catabolic process | biological process | The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. [GOC:jl] |
| response to peptide hormone | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a peptide hormone stimulus. A peptide hormone is any of a class of peptides that are secreted into the blood stream and have endocrine functions in living animals. [PMID:11027914, PMID:15134857, Wikipedia:Peptide_hormone] |
| type I pneumocyte differentiation | biological process | The process in which a relatively unspecialized cell acquires specialized features of a type I pneumocyte. A type I pneumocyte is a flattened cell with greatly attenuated cytoplasm and a paucity of organelles. [GOC:dph, GOC:mtg_lung, ISBN:0721662544] |