ACY3 Human
Description
Introduction to ACY3 Human
ACY3 (Aminoacylase-3) is a human enzyme encoded by the ACY3 gene (NCBI Gene ID: 91703) and belongs to the aspartoacylase subfamily. This 37.6 kDa cytoplasmic protein, composed of 342 amino acids, plays a critical role in hydrolyzing N-acylated amino acids and mercapturic acids, particularly in kidney proximal tubules . It is also implicated in Hepatitis C virus (HCV) interactions as a core-binding protein (HCBP1) . ACY3 is expressed in multiple tissues, including the liver, brain, stomach, and testis, with elevated expression observed in hepatocellular carcinoma (HCC) . Recombinant ACY3 (ENZ-153) is produced in E. coli as a His-tagged protein and purified via chromatographic techniques .
Biochemical Properties of ACY3 Human
Key biochemical characteristics include:
Metabolic Functions
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Substrate Specificity: ACY3 deacetylates N-acetylated aromatic amino acids (e.g., phenylalanine) and mercapturic acids, facilitating detoxification pathways .
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Role in Prenylation: ACY3 generates farnesylcysteine (FC) and geranylgeranylcysteine (GGC) by deacetylating NAFC and NAGGC, which are critical for Ras protein membrane association in HCC .
Oncogenic Pathways in HCC
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Elevated Expression: ACY3 levels are 5–20× higher in HCC cell lines (e.g., HepG2, HuH7) compared to normal hepatocytes .
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Therapeutic Target: Inhibition of ACY3 via siRNA or small molecules (e.g., inhibitors 10 and 11) reduces Ras membrane association and induces cytotoxicity in HCC cells () .
Diagnostic Marker Potential
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ACY3 expression correlates with HCC progression, showing moderate-to-high levels in tumor tissues versus minimal expression in normal liver .
Therapeutic Applications
| Strategy | Effect |
|---|---|
| siRNA Knockdown | Reduces Ras membrane association by 60–70% in HepG2/HuH7 cells |
| Pharmacological Inhibition | Increases intracellular NAFC/NAGGC, suppressing tumor cell viability |
Functional Associations and Interactions
ACY3 interacts with diverse biological entities, as shown below :
Product Specs
Aspartoacylase-2, Acylase III, Aminoacylase-3, ACY-3, Hepatitis C virus core-binding protein 1, HCBP1, ACY3, ASPA2.
MGSSHHHHHH SSGLVPRGSH MGSMCSLPVP REPLRRVAVT GGTHGNEMSG VYLARHWLHA PAELQRASFS AVPVLANPAA TSGCRRYVDHDLNRTFTSSF LNSRPTPDDP YEVTRARELN QLLGPKASGQ AFDFVLDLHN TTANMGTCLI AKSSHEVFAM HLCRHLQLQY PELSCQVFLY QRSGEESYNL DSVAKNGLGL ELGPQPQGVL RADIFSRMRT LVATVLDFIE LFNQGTAFPA FEMEAYRPVG VVDFPRTEAG HLAGTVHPQL QDRDFQPLQP GAPIFQMFSG EDLLYEGEST VYPVFINEAA YYEKGVAFVQ TEKFTFTVPA MPALTPAPSP AS.
Product Science Overview
ACY3 is primarily located in the cytoplasm of S2 and S3 proximal tubules and the apical domain of S1 proximal tubules in the kidney . It is also expressed at low levels in other tissues such as the stomach, testis, heart, brain, lung, and liver . The enzyme may function as a core binding protein for the Hepatitis C virus (HCV) .
Recombinant human ACY3 is produced using an Escherichia coli (E. coli) expression system . The recombinant protein typically includes a 6His tag at the N-terminus to facilitate purification and detection . The full-length protein ranges from amino acids 1 to 319 and has a molecular weight of approximately 35 kDa under reducing conditions . The protein is supplied in a buffer solution containing Tris-HCl, NaCl, DTT, and glycerol, and is stable for several months when stored at -70°C .
