animal tissues are PLP and PMP; plant-derived foods contain primarily PN and PNP, sometimes in the form of a glucoside. In humans, the major excretory form is 4-pyridoxic acid (4-PA).

PLP is a coenzyme for more than 100 enzymes involved in amino acid metabolism, including aminotransferases, decarboxylases, racemases, and dehydratases. It is a coenzyme for δ-aminolevulinate synthase, which catalyzes the first step in heme biosynthesis, and for cystathionine β-synthase and cystathioninase, enzymes involved in the transsulfuration pathway from homocysteine to cysteine. The carbonyl group of PLP binds to proteins as a Schiff’s base with the ε-amine of lysine. For practically all PLP enzymes the initial step in catalysis involves formation of a Schiff’s base between an incoming amino acid, via its α-amino group, and the carbonyl group of PLP. Much of the total PLP in the body is found in muscle bound to phosphorylase. PLP is a coenzyme in the phosphorylase reaction and is also directly involved in catalysis.

In animal tissue the major form of B₆ is PLP; next is PMP. Absorption in the gut involves phosphatase-mediated hydrolysis followed by transport of the nonphosphorylated form into the mucosal cell. Transport is by a nonsaturable passive diffusion mechanism. Even extremely large doses are well absorbed (Hamm et al., 1979). PN glucoside is absorbed less effectively than are PLP and PMP and, in humans, is deconjugated by a mucosal glucosidase (Nakano and Gregory, 1997). Some PN glucoside is absorbed intact and can be hydrolyzed in various tissues.

Most of the absorbed nonphosphorylated B₆ goes to the liver. PN, PL, and PM are converted to PNP, PLP, and PMP by PL kinase. PNP, which is normally found only at very low concentrations, and PMP are oxidized to PLP by PNP oxidase. PMP is also generated from PLP via aminotransferase reactions. PLP is bound to various proteins in tissues; this protects it from the action of phosphatases. The capacity for protein binding limits the accumulation of PLP by