Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells
Copyright policy )Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells
Carbohydrate‐deficient glycoprotein syndrome type I (CDGI) is most often due to phosphomannomutase deficiency; paradoxically, the human phosphomannomutase gene PMM1 is located on chromosome 22, whereas the CDGI locus is on chromosome 16. We show that phosphomannomutases present in rat or human liver share with homogeneous recombinant PMM1 several kinetic properties and the ability to form an alkali‐ and NH2OH‐sensitive phosphoenzyme with a subunit mass of ≈30 000 M r. However, they have a higher affinity for the activator mannose‐1,6‐bisphosphate than PMM1 and are not recognized by anti‐PMM1 antibodies, indicating that they represent a related but different isozyme. Phosphomannomutases belong to a novel mutase family in which the active residue is a phosphoaspartyl or a phosphoglutamyl.
- Université Catholique de Louvain Belgium
- KU Leuven Belgium
- Katholieke Universiteit Leuven Belgium
Binding Sites, Mannosephosphates, Blotting, Western, Chromatography, Ion Exchange, Phosphoproteins, Recombinant Proteins, Rats, Enzyme Activation, Isoenzymes, Molecular Weight, Kinetics, Congenital Disorders of Glycosylation, Liver, Phosphoglucomutase, Phosphotransferases (Phosphomutases), Animals, Humans, Electrophoresis, Polyacrylamide Gel
Binding Sites, Mannosephosphates, Blotting, Western, Chromatography, Ion Exchange, Phosphoproteins, Recombinant Proteins, Rats, Enzyme Activation, Isoenzymes, Molecular Weight, Kinetics, Congenital Disorders of Glycosylation, Liver, Phosphoglucomutase, Phosphotransferases (Phosphomutases), Animals, Humans, Electrophoresis, Polyacrylamide Gel
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