Disease relevance of ATFX/GER1

• The combined action of the MUR1 and GER1 gene products converts GDP-D-mannose to GDP-L-fucose in vitro demonstrating that this entire nucleotide-sugar interconversion pathway could be reconstituted using plant genes expressed in Escherichia coli [1].

High impact information on ATFX/GER1

• In vitro assays indicated that the GER1 protein does not act as a GDP-D-mannose 3, 5-epimerase, an enzymatic activity involved in the de novo synthesis of GDP-L-galactose and L-ascorbic acid [1].
• Similarly, L-ascorbate levels in GER1 antisense plants were unchanged indicating that GDP-D-mannose 3,5-epimerase is encoded by a separate gene [1].
• Based on sequence similarities to a bacterial gene involved in capsule synthesis we have cloned a gene from Arabidopsis, now designated GER1, which encodes a bifunctional 3, 5-epimerase-4-reductase in L-fucose synthesis [1].
• The amount of GDP-fucose in cells coexpressing MUR1 and AtFX/GER1 genes was 3.5 times higher than the amount of GDP-mannose in the same cells, indicating that this coexpression system is suitable for production of the valuable sugar nucleotide GDP-fucose in yeast [2].

Associations of ATFX/GER1 with chemical compounds

• In vitro GDP-fucose synthesis activity was observed in the cytoplasmic fraction of cells coexpressing the AtFX/GER1 gene and MUR1 gene [2].

References