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The formation of homogentisate in the biosynthesis of tocopherol and plastoquinone in spinach chloroplasts

1982; Springer Science+Business Media; Volume: 155; Issue: 6 Linguagem: Inglês

10.1007/bf01607575

1432-2048

Erich Fiedler, Jürgen Soll, Gernot Schultz,

Algal biology and biofuel production

Homogentisate is the precursor in the biosynthesis of α-tocopherol and plastoquinone-9 in chloroplasts. It is formed of 4-hydroxyphenylpyruvate of the shikimate pathway by the 4-hydroxyphenylpyruvate dioxygenase. In experiments with spinach the dioxygenase was shown to be localized predominatedly in the chloroplasts. Envelope membranes exhibit the highest specific activity, however, because of the high stromal portion of chloroplasts, 60–80% of the total activity is housed in the stroma. The incorporation of 4-hydroxyphenylpyruvate into 2-methyl-6-phytylquinol as the first intermediate in the tocopherol synthesis by the two-step-reaction: 4-Hydroxyphenylpyruvate → Homogentisate $$\xrightarrow{{Phytyl - PP}}$$ 2-Methyl-6-phytylquinol was demonstrated by using envelope membranes. Homogentisate originates directly from 4-hydroxyphenylpyruvate of the shikimate pathway. Additionally, a bypass exists in chloroplasts which forms 4-hydroxyphenylpyruvate from tyrosine by an L-amino-acid oxidase of the thylakoids and in peroxisomes by a transaminase reaction. Former results about the dioxygenase in peroxisomes were verified.