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Issue 2, 1993
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Stereospecific lysis of a range of β-hydroxy-α-amino acids catalysed by a novel aldolase from Streptomyces amakusaensis

Abstract

Cell-free preparations of Streptomyces amakusaensis contain a novel aldolase which catalyses the conversion of β-hydroxy-α-amino acids (as 2) into the corresponding aldehyde plus glycine; the aldolase is stable, shows broad substrate tolerance, is highly selective for threo stereochemistry and, where examined, is Stereospecific for the (2S,3R) configuration.

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Article type: Paper
DOI: 10.1039/C39930000205
Citation: J. Chem. Soc., Chem. Commun., 1993, 205-206
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    Stereospecific lysis of a range of β-hydroxy-α-amino acids catalysed by a novel aldolase from Streptomyces amakusaensis

    R. B. Herbert, B. Wilkinson, G. J. Ellames and E. K. Kunec, J. Chem. Soc., Chem. Commun., 1993, 205
    DOI: 10.1039/C39930000205

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