Wlasciwosci roslinnych aminotransferaz glioksylanowych

• Autorzy: Paszkowski A
• Języki publikacji: PL

Abstrakty

EN

Glyoxylate aminotransferases are unique among aminotransferases (EC 2.6.1.) because they catalyze the conversion of glyoxylate to glycine and this reaction is often considered to be physiologically irreversible. Glutamate: glyoxylate aminotransferase (GGAT, EC 2.6.1.4.) and serine: glyoxylate aminotransferase (SGAT, EC 2.6.1.45.) are the most extensively studied plant glyoxylate aminotransferases. The most important metabolic function of these two enzymes is to catalyze the transamination of glyoxylate to glycine in peroxisomes during photorespiration of higher plants. In this review some other possible metabolic roles of GGAT and SGAT are also discussed. Purification and substrate specificity of GGAT, SGAT and other glyoxylate aminotransferases are considered. The physical and kinetic properties of these enzymes such as their molecular weight, subunit composition, pyridoxal phosphate requirement, effect of pH and cations on activity and their mechanism of action are reviewed. Effects of natural metabolites on GGAT and SGAT activity with special consideration of mechanism of the inhibition by glyoxylate in the presence of ammonium ion are discussed as well.

Słowa kluczowe

PL

metabolizm komorek; aktywnosc enzymatyczna; lokalizacja subkomorkowa; preparaty enzymatyczne; pH; enzymy; biochemia roslin; mechanizm dzialania; masa czasteczkowa; wystepowanie; klasyfikacja; specyficznosc substratowa; reakcje enzymatyczne; aminotransferazy glioksylanowe; wlasciwosci kinetyczne; sklad podjednostkowy

• Wydawca: -
• Czasopismo: Postępy Nauk Rolniczych
• Rocznik: 1995
• Tom: 42
• Numer: 2
• Opis fizyczny: s.49-66,rys.,tab.,bibliogr.

Twórcy

autor

Paszkowski A

• Szkola Glowna Gospodarstwa Wiejskiego, Warszawa

Bibliografia

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