Esterase D Human

Esterase D, also known as S-formylglutathione hydrolase, is a cytoplasmic serine hydrolase that belongs to the esterase D family. This enzyme plays a crucial role in the detoxification of formaldehyde and is involved in various metabolic processes. The human recombinant form of this enzyme is widely used in research and biotechnology.

Esterase D is a member of the hydrolase family, specifically those acting on thioester bonds. The enzyme catalyzes the hydrolysis of S-formylglutathione into glutathione and formic acid . This reaction is essential for the detoxification of formaldehyde, a toxic compound that can be generated during various metabolic processes.

The enzyme is active toward numerous substrates, including O-acetylated sialic acids, and may be involved in the recycling of sialic acids . This broad substrate specificity makes Esterase D a versatile enzyme with potential applications in various biochemical pathways.

Esterase D is used as a genetic marker for certain diseases, including retinoblastoma and Wilson’s disease . Mutations in the gene encoding Esterase D can lead to deficiencies in enzyme activity, which may contribute to the development of these conditions.

The human recombinant form of Esterase D is produced using Escherichia coli as the expression system . The recombinant protein is typically purified using conventional chromatography techniques to achieve high purity levels. This recombinant enzyme is used in various research applications, including studies on enzyme kinetics, substrate specificity, and potential therapeutic uses.

Recombinant Esterase D is widely used in biochemical and clinical research. Its ability to hydrolyze a wide range of substrates makes it a valuable tool for studying metabolic pathways and enzyme mechanisms. Additionally, its role in detoxifying formaldehyde makes it an important enzyme for research on cellular detoxification processes.