Recombinant Xenopus laevis Estradiol 17-beta-dehydrogenase 12-A (hsd17b12-a)
Description
Functional Roles and Enzymatic Activities
hsd17b12-a exhibits dual enzymatic roles, primarily in estrogen biosynthesis and fatty acid metabolism:
**A. Estrogen Biosynthesis
hsd17b12-a catalyzes the conversion of estrone (E1) to estradiol (E2), a critical step in estrogen production. This activity is highly selective and efficient, making it a key enzyme in ovarian and mammary gland tissues . In contrast to human 17β-HSD12 (Q53GQ0), which also participates in fatty acid elongation, the Xenopus homolog demonstrates conserved catalytic mechanisms for E1→E2 conversion .
**B. Fatty Acid Metabolism
hsd17b12-a acts as a 3-ketoacyl-CoA reductase, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA during fatty acid elongation. This role is shared with human 17β-HSD12, which is involved in very-long-chain fatty acid (VLCFA) synthesis .
Research Applications
hsd17b12-a is utilized in diverse experimental contexts:
**A. Enzyme Kinetics Studies
Used to investigate substrate specificity and catalytic efficiency in E1→E2 conversion. Mutagenesis studies (e.g., F234 residue analysis) have elucidated structural determinants of substrate selectivity .
**B. ELISA Development
Recombinant hsd17b12-a serves as an antigen in immunoassays for detecting antibodies or analyzing tissue-specific expression .
**C. Metabolic Pathway Analysis
Explored in studies linking estrogen biosynthesis and fatty acid elongation, particularly in ovarian and hepatic tissues .
Comparative Analysis with Human Homolog
While Xenopus hsd17b12-a shares functional homology with human 17β-HSD12, key differences exist:
| Aspect | Xenopus laevis hsd17b12-a | Human 17β-HSD12 (Q53GQ0) |
|---|---|---|
| Primary Role | E1→E2 conversion (estrogen) | Dual role: E1→E2 conversion and VLCFA synthesis |
| Tissue Expression | Ovary, mammary gland (conserved) | Liver, adipose tissue, ovary |
| Catalytic Efficiency | High for E1→E2 (reported in studies) | Lower E1→E2 activity vs. 17β-HSD1 |
Research Findings and Implications
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Estrogenic Dominance: In Xenopus, hsd17b12-a is the predominant 17β-HSD isoform in ovarian tissue, suggesting evolutionary conservation of its role in estrogen production .
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Dual Functionality: Coexistence of estrogenic and lipogenic activities highlights its potential as a therapeutic target in endocrine disorders or lipid metabolism diseases .
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Structural Insights: Mutagenesis of residues (e.g., F234) in human 17β-HSD12 has informed mechanistic studies of substrate selectivity, applicable to Xenopus homologs .
Product Specs
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Target Background
This recombinant Xenopus laevis Estradiol 17-beta-dehydrogenase 12-A (hsd17b12-a) catalyzes the second step in the four-reaction long-chain fatty acid elongation cycle. This endoplasmic reticulum-bound enzyme adds two carbons to long- and very long-chain fatty acids (VLCFAs) per cycle. Its 3-ketoacyl-CoA reductase activity reduces 3-ketoacyl-CoA to 3-hydroxyacyl-CoA in each cycle, contributing to VLCFA production of varying chain lengths. These VLCFAs serve as precursors for membrane lipids and lipid mediators, participating in numerous biological processes. Additionally, this enzyme may convert estrone (E1) to estradiol (E2), playing a role in estrogen biosynthesis.
KEGG: xla:495218
UniGene: Xl.19362
