Abstract
Abstract Tartronic semialdehyde reductase from Pseudomonas putida has been purified and crystallized. As calculated from hydrodynamic measurements, the active enzyme has a molecular weight of 104,000 and appears to be composed of four subunits, each of which has a molecular weight of approximately 26,000. The enzyme catalyzes the reversible reduction of tartronic semialdehyde to d-glycerate in the presence of DPNH or TPNH. Glyoxylate and lactate are not substrates. The equilibrium constant of 6 x 1011 has been calculated when DPNH formation is measured. The reaction is anion sensitive.
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