Leucyl Aminopeptidase (S, Peptidase)
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.
Also Known As:
S, Peptidase; Peptidase S; Leucine Aminopeptidase; L-Leucylnaphthylamidase; Methoxyleucine Aminopeptidase; Zinc-Manganese-Leucine Aminopeptidase; Aminopeptidase, Cytosol; Aminopeptidase, Leucine; Aminopeptidase, Leucyl; Aminopeptidase, Methoxyleucine; Aminopeptidase, Zinc-Manganese-Leucine; Zinc Manganese Leucine Aminopeptidase; Cytosol Aminopeptidase
Networked: 288
relevant articles (2 outcomes,
21 trials/studies)
Relationship Network
Bio-Agent Context: Research Results
Experts
1. | Walling, Linda L:
6 articles
(06/2014 - 03/2002)
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2. | Dalton, John P:
3 articles
(01/2010 - 01/2006)
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3. | Trenholme, Katharine R:
3 articles
(01/2010 - 01/2006)
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4. | Stack, Colin M:
3 articles
(01/2010 - 01/2006)
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5. | Gardiner, Donald L:
3 articles
(01/2010 - 01/2006)
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6. | Hattori, Akira:
3 articles
(03/2006 - 08/2003)
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7. | Tsujimoto, Masafumi:
3 articles
(03/2006 - 08/2003)
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8. | Kikkawa, Fumitaka:
3 articles
(01/2005 - 08/2003)
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9. | Ino, Kazuhiko:
3 articles
(01/2005 - 08/2003)
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10. | Shibata, Kiyosumi:
3 articles
(01/2005 - 08/2003)
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