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OVCA2 (Esterase OVCA2) is a human metabolic serine hydrolase enzyme that shows strong preference for long-chain, unbranched alkyl ester substrates, catalyzing hydrolysis reactions using a classic catalytic triad (Ser117, Asp179, His206). It is a well-folded, intracellular protein, mainly located in the cytoplasm, and is evolutionarily conserved. OVCA2 is identified as a candidate tumor suppressor in ovarian cancer and potentially serves as a biomarker for disease, with links to cancer proliferation and acetaldehyde remediation noted. While its role in cancer biology is supported by expression and genomic studies, its natural physiological substrates and full biological functions remain incompletely defined. As of current research, no drugs are known to target OVCA2 directly, but its enzymatic mechanism suggests that future inhibitors, as with other serine hydrolases, would act via catalytic triad modulation or inhibition.
Enzyme inhibition/modulation (Drugs would likely act via hydrolase inhibition if developed)
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