CHEBI:166834 - MLN-4760

Main ChEBI Ontology Automatic Xrefs Reactions Pathways Models
ChEBI Name MLN-4760
ChEBI ID CHEBI:166834
Definition A L-histidine derivative that is L-histidine in which a hydrogen of the primary amino group is substituted by a (1S)-1-carboxy-3-methylbutyl group and the ring NH group is substituted by a 3,5-dichlorobenzyl group. It is a potent and selective human angiotensin-converting enzyme 2 (ACE2) inhibitor (IC50 = 0.44 nM) which was in clinical development for the treatment of ulcerative colitis.
Stars This entity has been manually annotated by the ChEBI Team.
Submitter Margaret Duesbury
Secondary ChEBI IDs CHEBI:47755
Supplier Information
Download Molfile XML SDF
Roles Classification
Biological Role(s): EC 3.4.17.23 (angiotensin-converting enzyme 2) inhibitor
Any EC 3.4.17.* (metallocarboxypeptidase) inhibitor that inhibits the action of angiotensin-converting enzyme 2 (EC 3.4.17.23).
Application(s): anti-inflammatory agent
Any compound that has anti-inflammatory effects.
Related Structures
MLN-4760 is a Structural Derivative of
L-histidine
Mass : 155.15468
Formula : C6H9N3O2
15971 		histidine
Mass : 155.15468
Formula : C6H9N3O2
27570 		proteinogenic amino acid
Definition : Any of the 23 alpha-amino acids that are precursors to proteins, and are incorporated into proteins during translation. The group includes the 20 amino acids encoded by the nuclear genes of eukaryotes together with selenocysteine, pyrrolysine, and N-formylmethionine. Apart from glycine, which is non-chiral, all have L configuration.
 L-leucine
Mass : 131.17296
Formula : C6H13NO2
15603
Graph View Tree View
panning
Move up
Move left
Move down
Move right
Graph compression

Simplified view Show me the possible minimal nodes in this graph
Full view Show me all the nodes in this graph
Personalised view Create your own personalised ontology view, if you wish to remove any entity from your future visualisations please right click the entity (e.g. molecular entity)
My hidden entities
Edit
+Zoom in
-Zoom out
Download
Enter fullscreen