Phosphomannomutase 1 Proteins (PMM1)

Human Phosphomannomutase 1 (PMM1) interaction partners

1. The 1.93 A resolution structure of PMM1 complexed with inosine monophosphate (IMP) was determined. The structure reveals IMP bound at the substrate recruitment site, thus inhibiting the mutase activity while simultaneously activating a phosphatase activity (IMP Kact = 1.5 muM) resulting from the hydrolysis of the phospho-enzyme.

2. a triple mutant of phospomannomutase1 that retains mutase and phosphatase activity, but is unable to bind inosine monophosphate, was characterized.

3. Mutations in phosphomannomutase is associated with ophthalmic manifestations of congenital disorder of glycosylation type 1a

4. human alpha-phosphomannomutase 1 crystallographic structure reveals the structural basis of congenital disorder of glycosylation type 1a

5. analysis of mental development in a patient with phosphomannomutase deficiency who is compound heterozygous for T237R/C241S mutations [case report]

6. The genes GUS and PMM1 are recommended for normalization purposes in gene expression studies of liver tissue from patients with chronic hepatitis.

7. PMM1 is responsible for the degradation of Glc-1,6-P(2) in brain

Mouse (Murine) Phosphomannomutase 1 (PMM1) interaction partners

1. Pmm1 activity in jejunum increased during the early stages of life, and it decreased at 1 month old, as does the amount of mannose incorporated into glycoproteins, whereas in the ileum, they were not affected by age.

2. Pmm1 immunoreactivity seen in prenatal brain until postnatal and adult stage and restricted in neuronal cell bodies.

3. The normal phenotype of Pmm1-deficient mice suggests that Pmm1 is not essential for normal mouse development.

4. PMM1 is responsible for the degradation of Glc-1,6-P(2) in brain