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- W2085676644 abstract "Three enzymes partially purified that catalyze respectively the transamination of l-norleucine, 4-aminobutyrate and σ-aminovalerate with α-ketoglutarate as aminoacceptor were characterized and isolated from l-lysine adapted cell of Candida guilliermondii var. membranaefaciens. The transaminases have a maximum activity in the pH range of 7.8–8.5 and at 55°C, 45°C and 40°C respectively. α-Ketoglutarate and to a lesser extent pyridoxal-5′-phosphate were effective protecting agents against rise in temperature. The enzymes exhibit absorption maximum at 280 nm, 330 nm and 410 nm. The fact that l-norleucine-leucine aminotransferase, 4-aminobutyrate aminotransferase and σ-aminovalerate aminotransferase are strongly induced by growing the yeast Candida on l-lysin suggests new hypothetic pathways for the catabolism of l-lysine where the main substrate of each aminotransferase could be an intermediary metabolite." @default.
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- W2085676644 date "1953-11-01" @default.
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- W2085676644 title "The conversion of lysine to pipecolic acid by Phaseolus vulgaris" @default.
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- W2085676644 doi "https://doi.org/10.1016/0003-9861(53)90457-3" @default.
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