Synthesis of GDP-L-fucose by the human FX protein
Autor: | Angela Bisso, Michela Tonetti, Umberto Benatti, Laura Sturla, Antonio De Flora |
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Rok vydání: | 1996 |
Předmět: |
Guanosine Diphosphate Mannose
Carcinoma Hepatocellular DNA Complementary Erythrocytes Molecular Sequence Data Syntaxin 1 Nerve Tissue Proteins Reductase Biology medicine.disease_cause Biochemistry Polymerase Chain Reaction Fucose Homology (biology) Cell Line chemistry.chemical_compound Mice Cytosol Guanosine Diphosphate Fucose medicine Escherichia coli Animals Humans Amino Acid Sequence Caenorhabditis elegans Molecular Biology Peptide sequence Chromatography High Pressure Liquid chemistry.chemical_classification Base Sequence Molecular Structure Sequence Homology Amino Acid Liver Neoplasms Protein primary structure Ketone Oxidoreductases Cell Biology Blood Proteins Molecular biology Amino acid Enzyme chemistry Antigens Surface Carbohydrate Epimerases Carrier Proteins |
Zdroj: | The Journal of biological chemistry. 271(44) |
ISSN: | 0021-9258 |
Popis: | FX is a homodimeric NADP(H)-binding protein of 68 kDa, first identified in human erythrocytes, from which it was purified to homogeneity. Its function has been unrecognized despite partial structural and genetic characterization. Recently, on the basis of partial amino acid sequence, it proved to be the human homolog of the murine protein P35B, a tumor rejection antigen. In order to address the biochemical role of FX, its primary structure was completed by cDNA sequencing. This sequence revealed a significant homology with many proteins from different organisms. Specifically, FX showed a remarkable similarity with a putative Escherichia coli protein, named Yefb, whose gene maps in a region of E. coli chromosome coding for enzymes involved in synthesis and utilization of GDP-D-mannose. Accordingly, a possible role of FX in this metabolism was investigated. The data obtained indicate FX as the enzyme responsible for the last step of the major metabolic pathway resulting in GDP-L-fucose synthesis from GDP-D-mannose in procaryotic and eucaryotic cells. Specifically, purified FX apparently catalyzes a combined epimerase and NADPH-dependent reductase reaction, converting GDP-4-keto-6-D-deoxymannose to GDP-L-fucose. This is the substrate of several fucosyltranferases involved in the correct expression of many glyconjugates, including blood groups and developmental antigens. |
Databáze: | OpenAIRE |
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