GMDS Human

GMD catalyzes the conversion of GDP-mannose to GDP-4-dehydro-6-deoxy-D-mannose, which is subsequently converted to GDP-fucose . The reaction can be summarized as follows: [ \text{GDP-mannose} \rightleftharpoons \text{GDP-4-dehydro-6-deoxy-D-mannose} + \text{H}_2\text{O} ]

This reaction is the first step in the de novo synthesis pathway of GDP-fucose, which is essential for the transfer of fucose sugars .

GDP-fucose is a critical component in the formation of fucosylated glycans, which have significant roles in various biological functions, including:

• Cell Immunity and Signaling: Fucosylated glycans are involved in cell-cell interactions, immune responses, and signaling pathways .
• Blood Transfusion Reactions: Fucose-containing glycans play a role in blood group antigenicity .
• Leukocyte-Endothelial Adhesion: Selectin-mediated adhesion processes are influenced by fucosylated glycans .
• Host-Microbe Interactions: Fucosylated glycans are involved in interactions between host cells and microbes .

The primary structure of human recombinant GMD consists of 372 amino acids . The enzyme requires NADP+ as a cofactor for its catalytic activity . The enzyme’s structure and function are crucial for maintaining proper cellular functions and immune responses.

Alterations in the expression of fucosylated oligosaccharides have been observed in several pathological processes, including cancer and atherosclerosis . Additionally, fucose deficiency is associated with conditions such as leukocyte adhesion deficiency type II (LAD II), also known as congenital disorder of glycosylation type IIc .

Human recombinant GMD is used in research to study the biosynthesis of GDP-fucose and its role in various biological processes. Understanding the enzyme’s function and regulation can provide insights into potential therapeutic targets for diseases associated with fucose metabolism.