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• W1998190344 abstract "β-Cyano-l-alanine synthase was purified ca 1000-fold to homogeneity from the immature seeds of Vicia angustifolia. The purified enzyme has an apparent Mr of 54 000 consisting of two identical subunits. The subunits contain one molecule of pyridoxal 5′-phosphate each. The Km value is 3.6 mM for l-cysteine and 0.5 mM for cyanide. β-Cyano-l-alanine synthase from V. angustifolia also catalyses the formation of some S-substituted l-cysteines and some heterocyclic β-substituted alanines from l-cysteine or O-acetyl-l-serine as an additional catalytic activity. Significant differences were found between this enzyme and β-cyano-l-alanine synthases from other sources. The amino acid composition of the purified enzyme, and also the occurrence and distribution of β-cyano-l-alanine synthase and cysteine synthase activities in some higher plants are given." @default.
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• W1998190344 date "1989-01-01" @default.
• W1998190344 modified "2023-10-02" @default.
• W1998190344 title "Purification and properties of β-cyano-l-alanine synthase from Vicia angustifolia" @default.
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• W1998190344 doi "https://doi.org/10.1016/s0031-9422(00)97969-x" @default.
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