"Leucyl Aminopeptidase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide.
| Descriptor ID |
D007931
|
| MeSH Number(s) |
D08.811.277.656.350.100.511 D08.811.277.656.350.555.700 D08.811.277.656.675.555.700
|
| Concept/Terms |
Leucyl Aminopeptidase- Leucyl Aminopeptidase
- Aminopeptidase, Leucyl
- L-Leucylnaphthylamidase
- Zinc-Manganese-Leucine Aminopeptidase
- Aminopeptidase, Zinc-Manganese-Leucine
- Zinc Manganese Leucine Aminopeptidase
- Peptidase S
- Cytosol Aminopeptidase
- Aminopeptidase, Cytosol
- Leucine Aminopeptidase
- Aminopeptidase, Leucine
|
Below are MeSH descriptors whose meaning is more general than "Leucyl Aminopeptidase".
Below are MeSH descriptors whose meaning is more specific than "Leucyl Aminopeptidase".
This graph shows the total number of publications written about "Leucyl Aminopeptidase" by people in this website by year, and whether "Leucyl Aminopeptidase" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2005 | 1 | 0 | 1 |
| 2006 | 0 | 1 | 1 |
| 2013 | 0 | 1 | 1 |
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click here.
Below are the most recent publications written about "Leucyl Aminopeptidase" by people in Profiles.
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Spencer CT, Dragovic SM, Conant SB, Gray JJ, Zheng M, Samir P, Niu X, Moutaftsi M, Van Kaer L, Sette A, Link AJ, Joyce S. Sculpting MHC class II-restricted self and non-self peptidome by the class I Ag-processing machinery and its impact on Th-cell responses. Eur J Immunol. 2013 May; 43(5):1162-72.
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Forde GK, Kedzierski P, Sokalski WA, Forde AE, Hill GA, Leszczynski J. Physical nature of interactions within the active site of cytosine-5-methyltransferase. J Phys Chem A. 2006 Feb 16; 110(6):2308-13.
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Dyguda E, Grembecka J, Sokalski WA, Leszczynski J. Origins of the activity of PAL and LAP enzyme inhibitors: toward ab initio binding affinity prediction. J Am Chem Soc. 2005 Feb 16; 127(6):1658-9.