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- W1575331323 abstract "This chapter provides an overview of asparagine transaminase from rat liver. Rat liver possesses two asparaginases, that is, “asparaginase I” which is not enhanced by pyruvate and “asparaginase II” which is enhanced by pyruvate. The two activities can be distinguished by their relative susceptibility to heat and acid denaturation. Asparaginase II is composed of two enzymes: an asparagine transaminase that catalyzes the reversible transfer of the α-amino group of asparagine to a suitable α-keto acid acceptor and ω-amidase that catalyzes the deamidation of α-ketosuccinamate. The metabolic function of this enzyme in mammals is to convert glyoxylate to glycine. The L-amino acid-α-Ketosuccinamate transaminase activity is discussed and its purification procedure is reviewed. The amino acid specificity of asparagine transaminase is broad, with at least 13 amino acids acting as substrates. Glycine inhibits the asparagine–pyruvate transaminase reaction but it is not a detectable substrate." @default.
- W1575331323 created "2016-06-24" @default.
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- W1575331323 date "1985-01-01" @default.
- W1575331323 modified "2023-10-18" @default.
- W1575331323 title "[78] Asparagine transaminase from rat liver" @default.
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- W1575331323 doi "https://doi.org/10.1016/s0076-6879(85)13081-8" @default.
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