On the possibility of involvement of glutamate glyoxylate and serine glyoxylate aminotransferases from rye [Secale cereale] seedlings in the metabolism of tetrapyrrole compounds

• Autorzy: Paszkowski A.
• Języki publikacji: EN

Abstrakty

EN

The activity of highly purified L-serine:glyoxylate aminotransferase (SGAT, EC 2.6.1 AS) from rye seedlings was inhibited competitively by 5-aminolevulinate (ALA, Ki = 5 mM) SGAT was activated by hematin. Protoporphyrin IX and hematin inhibited irreversibly the activity of highly purified glutamate:glyoxylate aminotransferase (GGAT, EC 2.6.1.2) from rye seedlings. SGAT was found to catalyse transamination between ALA and hydroxypyruvate, whereas GGAT that between ALA and 2-oxoglu- tarate or pyruvate. It is suggested that SGAT is involved in the process of degradation of the excess ALA which has not been incorporated into porphyrin compounds.

Słowa kluczowe

EN

metabolism; rye; Secale cereale; aminotransferase; glyoxylate; tetrapyrrole compound; seedling; serine glyoxylate; glutamate glyoxylate

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1992
• Tom: 39
• Numer: 4
• Opis fizyczny: p.345-353,fig.

Twórcy

autor

Paszkowski A.

• Warsaw Agricultural University, Rakowiecka 26-30, 02-528 Warsaw, Poland

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