Identification of a PLP-Dependent Threonine Transaldolase: A Novel Enzyme Involved in 4-Fluorothreonine Biosynthesis in Streptomyces cattleya This work was supported by the Biotechnological and Biological Sciences Research Council and the University of St Andrews.

Abstract excerpt

The final enzyme on the biosynthetic pathway to 4-fluorothreonine is identified in Streptomyces cattleya. The enzyme catalyzes a pyridoxal phosphate-dependent “transaldose” reaction between L-threonine and fluoroacetaldehyde (see scheme; PLP=pyridoxal 5′-phosphate). Unlike threonine aldolases, glycine is not a substrate for this new type of enzyme.

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