GFUS
GFUS (GDP-L-fucose synthase, also known as FX, P35B, SDR4E1 and TSTA3) is an NADP(H)-binding enzyme that catalyses the final steps in the synthesis of GDP-L-fucose from GDP-4-dehydro-6-deoxy-D-mannose. GDP-L-fucose is the donor substrate used by fucosyltransferases. Browse Assay Genie's current range of GFUS research reagents below, or read on for the biology behind the target.
GFUS catalyses the two-step, NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose (also described as GDP-4-keto-6-D-deoxymannose) to GDP-L-fucose. The conversion involves two chemical reactions, an epimerase step followed by a reductase step, and both are carried out by this single protein. The NCBI Gene summary places the reaction within GDP-D-mannose metabolism.
The product, GDP-L-fucose, is the substrate of several fucosyltransferases. These enzymes contribute to the expression of many glycoconjugates, including blood group ABH antigens and developmental adhesion antigens. The GFUS protein therefore sits upstream of fucosylation, which makes it a useful point of study in glycobiology. The human GFUS gene encodes a protein of the NAD(P)-dependent epimerase/dehydratase family, fucose synthase subfamily. HGNC places it in the short chain dehydrogenase/reductase superfamily. The mouse ortholog is Gfus.
The gene was first described as tissue specific transplantation antigen P35B, which explains the alias TSTA3. Other names and symbols include FX, P35B and SDR4E1. According to the NCBI Gene summary, mutations in this gene may cause leukocyte adhesion deficiency, type II, a disorder connected with the expression of fucosylated adhesion antigens. Researchers studying GFUS may look at the enzyme itself, at its role in fucose supply for glycosylation, or at the consequences of altered GDP-L-fucose synthesis.
GFUS supplies GDP-L-fucose, the substrate of fucosyltransferases that build many glycoconjugates, so it is relevant to studies of how fucosylated structures are produced.
The enzyme performs sequential epimerase and reductase reactions in GDP-D-mannose metabolism, making it a model for NADP-dependent nucleotide sugar conversion.
GDP-L-fucose is a substrate for fucosyltransferases involved in expression of blood group ABH antigens, linking GFUS to antigen synthesis.
Mutations in the gene may cause leukocyte adhesion deficiency, type II, linking GFUS to developmental adhesion antigen expression.
GFUS, or GDP-L-fucose synthase, catalyses the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose. The process involves an epimerase reaction and a reductase reaction. The resulting GDP-L-fucose is used as a substrate by fucosyltransferases.
GFUS is also known as FX, P35B, SDR4E1 and TSTA3. The previous gene name was tissue specific transplantation antigen P35B. The enzyme is classified as EC 1.1.1.271 and belongs to the fucose synthase subfamily of the NAD(P)-dependent epimerase/dehydratase family.
The NCBI Gene summary states that mutations in the GFUS gene may cause leukocyte adhesion deficiency, type II. A mouse ortholog, Gfus, is recorded. No rat ortholog is listed in the data; check the datasheet of any product for its validated reactivity.
Other fucosylation enzymes, nucleotide sugar metabolism proteins and glycosylation-related targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q13630; product specifications from Assay Genie datasheets.