By Leon E. Rosenberg (auth.), Harry Harris, Kurt Hirschhorn (eds.)
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Extra info for Advances in Human Genetics 6
Presumable, a modified Schiff base is formed between the phosphate and aldehyde groups of PLP and moieties on the apoenzyme surface. In this configuration, specific holoenzyme functions are carried out. PLP has , been shown to have a much greater affinity for some apoenzymes than others. Thus its affinity for transaminases far exceeds that for decarboxylases or kynureninase. These differences in affinity are reflected in the enzymatic dysfunctions seen in pyridoxine deficiency states. Pyridoxine Deficiency Pyridoxine deficiency is rare but has been observed in several settings in which the total tissue pool of PLP and its precursors is reduced.
II. Chemical structures of the B6 vitamers (pyridoxine, pyridoxal, pyridoxamine) and coenzyme (pyridoxal-5'-phosphate). The coenzyme attaches to its apoenzymes by formation of a Schiff base between the aldehyde group of pyridoxal-5'phosphate and an E-amino nitrogen group of a lysine residue on the apoenzyme. been isolated from foods and extracellular fluid, but none of these is the active coenzyme form. In the cell, these chemically interconvertible precursors are phosphorylated to pyridoxal-5 ' -phosphate (PLP) or pyridoxamine-5' -phosphate by a specific kinase which requires magnesium and ATP.
The first, representative of the patients with Bl2-unresponsive methylmalonicaciduria, converts OH-Cbl to Ado-Cbl and Me-Cbl normally, but has minimal holomutase activity in cell extracts. These cells have a primary defect in their mutase apoenzyme. The second and third phenotypes, typical of patients with Bl2-responsive methylmalonicaciduria, are unable to convert OH-Cbl to Ado-Cbl in whole cells while making Me-Cbl normally (Fig. 7). Their holomutase activity in cell-free extracts is normal. They are distinguished from one another by assays of Ado-Cbl synthesis in cellfree extracts.