Inosine monophosphate (IMP) is an important substance in the process of nucleotide degradation， and is also one of the flavor substances of aquatic products. IMP is degraded to hypoxanthine riboside (HxR) and hypoxanthine (Hx) under the action of acid phosphatase. Therefore， it is of great significance to study the enzymatic characteristics of acid phosphatase and inhibit its activity. The enzymatic properties of acid phosphatases were analyzed based on bioinformatics and enzyme inhibitors were screened by virtual screening techniques. The results showed that ACPI and ACPII contained 488 and 348 amino acids， respectively， and both ACPI and ACPII were stable hydrophilic proteins. ACPI contained 37 phosphorylation sites and 5 N-glycosylation sites， whereas ACPII contains 14 phosphorylation sites and 1 N-glycosylation site， and neither of them contained an O-glycosylation site. ACPI existed in a transmembrane structural domain and had no signal peptide， and was subcellularly localized in the plasma membrane， while ACPII contained no transmembrane domain， a signal peptide， and was subcellularly localized in the extracellular matrix. ACPI and ACPII had the highest amount of randomly coiled and extended chains in their secondary structures. The optimal temperature and pH of ACPI and ACPII were both 40 ℃ and 5.0， respectively. Km was 0.23 mmol/L and 0.14 mmol/L， and vmax was 1.04 μmol/(L·min) p-NP and 1.06 μmol/(L·min) p-NP， respectively. Five inhibitors， epigallocatechin gallate (ECG)， epicatechin， epigallocatechin gallate， gallic acid and salicylic acid were virtually screened by molecular docking. ECG had the strongest inhibitory effect on ACPI and ACPII， with IC50 of 0.24 mmol/L and 0.27 mmol/L， respectively.