Abstract
The preparation of crystalline threonine aldolase from the cell extract of Candida humicola is described. The enzyme is homogeneous upon ultracentrifugation and disc electrophoresis. The molecular weight is 277,000. The enzyme exhibits an absorption maximum at 420 mμ, and contains 6 moles of pyridoxal phosphate per mole of enzyme. The enzyme catalyzes the stoichiometric conversion of L-threonine into acetaldehyde and glycine. The enzyme also catalyzes the glycine formation from D, L-allothreonine and L-serine.
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