Title: Enzymes Catalysing Formation of Pyridoxal Phosphate From Vitamin B6
Abstract: The evolutionary retention of homologous portions of pyridoxal kinases, both broadly and narrowly specific, and the occurrence of a highly conserved region of pyridoxine (pyridoxamine) phosphate oxidase with catalytically involved residues, emphasize the importance of these enzymes that are potential agents for release of pharmalogic effectors. The interactions by which the three, natural, free forms of vitamin B6 (PN, PL, and PM) can be routed to the coenzyme pyridoxal 5'-phosphate (PLP) require the successive actions of pyridoxal kinase and pyridoxine (pyridoxamine) 5'-phosphate oxidase. Additionally phosphatases catalyze hydrolytic reversions ofthe vitaminic 5'-phosphates to free vitamers. These essential interconversions are summarized in Figure 1.
Publication Year: 2000
Publication Date: 2000-01-01
Language: en
Type: book-chapter
Indexed In: ['crossref']
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Cited By Count: 2
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