ENPEP
ENPEP (glutamyl aminopeptidase, also known as aminopeptidase A, gp160 and CD249) is a membrane-bound zinc peptidase of the M1 family. It cleaves N-terminal acidic residues from peptides such as angiotensin II and contributes to blood pressure regulation. Browse Assay Genie's current range of ENPEP research reagents below, or read on for the biology behind the target.
ENPEP is an aminopeptidase that removes N-terminal acidic residues from peptide substrates, showing a calcium-modulated preference for such residues. Its best-described substrate is angiotensin II, from which it cleaves the N-terminal aspartate. Through this activity it regulates central hypertension and can upregulate blood pressure. The enzyme also regulates blood vessel formation and can enhance tumorigenesis in some tissues.
The ENPEP gene encodes glutamyl aminopeptidase, a type II integral membrane protein found at the cell membrane. It carries an extracellular zinc-binding domain and belongs to the peptidase M1 family. In HGNC, the gene is grouped with the aminopeptidases, the CD molecules and the M1 metallopeptidases. Mouse and rat both have an orthologous Enpep gene, so the protein can be studied in common rodent models.
The protein has several names in the literature: glutamyl aminopeptidase, aminopeptidase A, gp160 and CD249. Researchers working with an ENPEP antibody, ENPEP ELISA kit or recombinant ENPEP protein will meet these terms interchangeably. In addition to its role in the angiotensin pathway, ENPEP, together with ANPEP and DPP4, was identified as a candidate co-receptor for the coronavirus SARS-CoV-2, the cause of COVID-19.
ENPEP cleaves the N-terminal aspartate from angiotensin II and can upregulate blood pressure, making it relevant to hypertension research.
Its calcium-modulated preference for N-terminal acidic residues makes ENPEP a useful enzyme for studying how angiotensin II and related peptides are processed.
ENPEP can regulate blood vessel formation and enhance tumorigenesis in some tissues, prompting study of its role in vascular and cancer biology.
Along with ANPEP and DPP4, ENPEP was identified as a candidate co-receptor for SARS-CoV-2, supporting work on viral entry factors.
ENPEP is a membrane-bound aminopeptidase that cleaves N-terminal acidic residues from peptides, with a calcium-modulated preference. It removes the N-terminal aspartate from angiotensin II, thereby upregulating blood pressure, and it also regulates blood vessel formation and can enhance tumorigenesis in some tissues.
ENPEP stands for glutamyl aminopeptidase and was previously named aminopeptidase A. Aliases include gp160 and CD249. The enzyme is classified as EC 3.4.11.7 and belongs to the peptidase M1 family, so literature searches should cover all of these terms.
Mouse and rat both carry an orthologous Enpep gene. ENPEP is linked to blood pressure control through angiotensin II cleavage, and it was reported as a candidate SARS-CoV-2 co-receptor alongside ANPEP and DPP4. Check the datasheet of any product for its validated reactivity.
Other aminopeptidases, renin-angiotensin pathway proteins and candidate SARS-CoV-2 co-receptors with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q07075; product specifications from Assay Genie datasheets.