Details of Drug-Metabolizing Enzyme (DME)
General Information of Drug-Metabolizing Enzyme (DME) (ID: DE7PT32)
DME Name | Alanyl aminopeptidase (ANPEP) | ||||
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Synonyms | Aminopeptidase M; Aminopeptidase N; CD13; Microsomal aminopeptidase; Myeloid plasma membrane glycoprotein CD13; ANPEP; AP-M; AP-N; APN; PEPN; gp150; hAPN | ||||
Gene Name | ANPEP | ||||
UniProt ID | |||||
INTEDE ID | |||||
3D Structure | |||||
Gene ID | |||||
EC Number | EC: 3.4.11.2 | ||||
Lineage | Species: Homo sapiens | ||||
Sequence |
MAKGFYISKSLGILGILLGVAAVCTIIALSVVYSQEKNKNANSSPVASTTPSASATTNPA
SATTLDQSKAWNRYRLPNTLKPDSYRVTLRPYLTPNDRGLYVFKGSSTVRFTCKEATDVI IIHSKKLNYTLSQGHRVVLRGVGGSQPPDIDKTELVEPTEYLVVHLKGSLVKDSQYEMDS EFEGELADDLAGFYRSEYMEGNVRKVVATTQMQAADARKSFPCFDEPAMKAEFNITLIHP KDLTALSNMLPKGPSTPLPEDPNWNVTEFHTTPKMSTYLLAFIVSEFDYVEKQASNGVLI RIWARPSAIAAGHGDYALNVTGPILNFFAGHYDTPYPLPKSDQIGLPDFNAGAMENWGLV TYRENSLLFDPLSSSSSNKERVVTVIAHELAHQWFGNLVTIEWWNDLWLNEGFASYVEYL GADYAEPTWNLKDLMVLNDVYRVMAVDALASSHPLSTPASEINTPAQISELFDAISYSKG ASVLRMLSSFLSEDVFKQGLASYLHTFAYQNTIYLNLWDHLQEAVNNRSIQLPTTVRDIM NRWTLQMGFPVITVDTSTGTLSQEHFLLDPDSNVTRPSEFNYVWIVPITSIRDGRQQQDY WLIDVRAQNDLFSTSGNEWVLLNLNVTGYYRVNYDEENWRKIQTQLQRDHSAIPVINRAQ IINDAFNLASAHKVPVTLALNNTLFLIEERQYMPWEAALSSLSYFKLMFDRSEVYGPMKN YLKKQVTPLFIHFRNNTNNWREIPENLMDQYSEVNAISTACSNGVPECEEMVSGLFKQWM ENPNNNPIHPNLRSTVYCNAIAQGGEEEWDFAWEQFRNATLVNEADKLRAALACSKELWI LNRYLSYTLNPDLIRKQDATSTIISITNNVIGQGLVWDFVQSNWKKLFNDYGGGSFSFSN LIQAVTRRFSTEYELQQLEQFKKDNEETGFGSGTRALEQALEKTKANIKWVKENKEVVLQ WFTENSK |
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Function | This enzyme plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. | ||||
KEGG Pathway | |||||
Reactome Pathway | |||||
Molecular Interaction Atlas (MIA) of This DME
Molecular Interaction Atlas (MIA) | ||||||||||||||||||||||||||||
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1 Approved Drug(s) Metabolized by This DME
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Molecular Expression Atlas (MEA) of This DME
The Drug Therapeutic Target (DTT) Role of This DME
DME DTT Name | Aminopeptidase N (ANPEP) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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DME DTT Type | Clinical trial | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
1 Clinical Trial Drug(s) Targeting This DTT
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39 Investigative Drug(s) Targeting This DTT
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References
1 | Recent insights into the role of dipeptidyl aminopeptidase IV (DPIV) and aminopeptidase N (APN) families in immune functions. Clin Chem Lab Med. 2009;47(3):253-61. | ||||
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2 | Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor. Bioorg Med Chem Lett. 1999 Jun 7;9(11):1511-6. | ||||
3 | New aromatic monoesters of alpha-aminoaralkylphosphonic acids as inhibitors of aminopeptidase N/CD13. Bioorg Med Chem. 2010 Apr 15;18(8):2930-6. | ||||
4 | Novel selective inhibitors of the zinc plasmodial aminopeptidase PfA-M1 as potential antimalarial agents. J Med Chem. 2007 Mar 22;50(6):1322-34. | ||||
5 | Design, synthesis, and preliminary studies of the activity of novel derivatives of N-cinnamoyl-L-aspartic acid as inhibitors of aminopeptidase N/CD13. Bioorg Med Chem. 2009 Oct 15;17(20):7398-404. | ||||
6 | Ligands to the (IRAP)/AT4 receptor encompassing a 4-hydroxydiphenylmethane scaffold replacing Tyr2. Bioorg Med Chem. 2008 Jul 15;16(14):6924-35. | ||||
7 | Retro-inverso concept applied to the complete inhibitors of enkephalin-degrading enzymes. J Med Chem. 1988 Sep;31(9):1825-31. | ||||
8 | N-hydroxy-2-(naphthalene-2-ylsulfanyl)-acetamide, a novel hydroxamic acid-based inhibitor of aminopeptidase N and its anti-angiogenic activity. Bioorg Med Chem Lett. 2005 Jan 3;15(1):181-3. | ||||
9 | A library of novel hydroxamic acids targeting the metallo-protease family: design, parallel synthesis and screening. Bioorg Med Chem. 2007 Jan 1;15(1):63-76. | ||||
10 | Selective aminopeptidase-N (CD13) inhibitors with relevance to cancer chemotherapy. Bioorg Med Chem. 2013 Apr 1;21(7):2135-44. | ||||
11 | Ontogenic and adult whole body distribution of aminopeptidase N in rat investigated by in vitro autoradiography. Biochimie. 2004 Feb;86(2):105-13. | ||||
12 | Renal metabolism of calcitonin. Am J Physiol. 1988 Apr;254(4 Pt 2):F593-600. | ||||