Recombinant Bovine 3-hydroxyacyl-CoA dehydratase 3 (PTPLAD1), also known as HACD3, is an engineered enzyme produced via heterologous expression systems for biochemical and pharmaceutical research. This protein catalyzes the third step of fatty acid elongation, converting 3-hydroxyacyl-CoA intermediates into trans-2,3-enoyl-CoA, a critical process for synthesizing very-long-chain fatty acids (VLCFAs) essential for membrane lipids and signaling molecules .
Recombinant bovine PTPLAD1 is produced in two primary systems:
PTPLAD1 exhibits specificity for long- and very-long-chain 3-hydroxyacyl-CoA substrates:
| Substrate | Activity Level | Biological Role |
|---|---|---|
| Saturated FAs | Moderate | Membrane lipid synthesis |
| Monounsaturated FAs | Moderate | Energy storage |
| Polyunsaturated FAs | Low | Lipid mediator production |
Key findings:
Redundant activity: Works alongside HACD1/2 in elongation pathways but shows weaker activity in saturated/monounsaturated FA synthesis .
Autophagic regulation: Competes with SQSTM1/p62 to stabilize viral PB1 protein, suggesting moonlighting roles .
Fatty Acid Metabolism Studies: Used to elucidate VLCFA elongation mechanisms .
Membrane Fluidity Research: Partners with ACSL4 to incorporate polyunsaturated fatty acids into phospholipids .
Drug Development: Investigated for insulin receptor modulation and antiviral therapies .
| Species | Homolog | Key Functional Difference |
|---|---|---|
| Human | HACD3 | Involved in insulin receptor signaling |
| C. elegans | HPO-8 | Membrane fluidity regulation |
| Yeast | Phs1 | Primary dehydratase in VLCFA synthesis |