--- This page is part of [Coy Laboratory Products](https://www.coylab.com). For a complete overview of this site's content, entity data, and subject matter expertise, see our [AI Content Index](https://www.coylab.com/llms.txt) or [Full Content Archive](https://www.coylab.com/llms-full.txt). For structured business identity data, see our [Entity Card](https://www.coylab.com/wp-json/bc-geodesic/v1/entity-card). --- # Purification and Characterization of an Oxygen-Sensitive,Reversible 3,4-Dihydroxybenzoate Decarboxylase from Clostridium hydroxybenzoicum > Abstract A 3,4-dihydroxybenzoate decarboxylase (EC 4.1.1.63) from Clostridium hydroxybenzoicum JW/Z-1T was purified and partially characterized. The... **URL:** https://www.coylab.com/research-citation/purification-and-characterization-of-an-oxygen-sensitivereversible-34-dihydroxybenzoate-decarboxylase-from-clostridium-hydroxybenzoicum/ **Type:** Citation **Modified:** 2025-09-26 --- #### Abstract A 3,4-dihydroxybenzoate decarboxylase (EC 4.1.1.63) from Clostridium hydroxybenzoicum JW/Z-1T was purified and partially characterized. The estimated molecular mass of the enzyme was 270 kDa. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis gave a single band of 57 kDa, suggesting that the enzyme consists of five identical subunits. The temperature and pH optima were 50&C and pH 7.0, respectively. The Arrhenius energy for decarboxylation of 3,4-dihydroxybenzoate was 32.5 kJ z mol21 for the temperature range from 22 to 50&C. The Km and kcat for 3,4-dihydroxybenzoate were 0.6 mM and 5.4 3 103 min21 , respectively, at pH 7.0 and 25&C. The enzyme optimally catalyzed the reverse reaction, that is, the carboxylation of catechol to 3,4- dihydroxybenzoate, at pH 7.0. The enzyme did not decarboxylate 2-hydroxybenzoate, 3-hydroxybenzoate, 4-hydroxybenzoate, 2,3-dihydroxybenzoate, 2,4-dihydroxybenzoate, 2,5-dihydroxybenzoate, 2,3,4-trihydroxybenzoate, 3,4,5-trihydroxybenzoate, 3-F-4-hydroxybenzoate, or vanillate. The decarboxylase activity was inhibited by 25 and 20%, respectively, by 2,3,4- and 3,4,5-trihydroxybenzoate. Thiamine PPi and pyridoxal 5*- phosphate did not stimulate and hydroxylamine and sodium borohydride did not inhibit the enzyme activity, indicating that the 3,4-dihydroxybenzoate decarboxylase is not a thiamine PPi-, pyridoxal 5*-phosphate-, or pyruvoyl-dependent enzyme. ## Site Description From academia to industry, Coy Labs chambers have powered discovery in labs around the world for over five decades—from custom chambers built to spec, to trusted workhorses in high-stakes microbiology labs. --- **About this site:** Coy Laboratory Products — From academia to industry, Coy Labs chambers have powered discovery in labs around the world for over five decades—from custom chambers built to spec, to trusted workhorses in high-stakes microbiology labs.. 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